Functions of Insulin in the Body: Good Guy or Bad Guy?

The functions of insulin in the body are widely misunderstood. In this article, we will explore the actions of insulin on a cellular level to gain a better appreciation for all it does as well as a clearer understanding of how to keep this hormone functioning in balance and at its optimal capacity.

Insulin is perhaps the most important compound circulating in our bodies. It is involved in more than 60 key biological processes. Impairments in insulin function affect many facets of health and well-being and, if left uncorrected, are ultimately fatal. Despite its paramount importance, the functions of insulin in the body are widely misunderstood.

Insulin is an anabolic hormone, meaning it acts to promote synthesis and building, as opposed to catabolic hormones that break down and deconstruct bodily tissues and compounds. Given its vital importance, it is curious that insulin is sometimes portrayed as the bad guy. Consider, for instance, how we cast insulin as the villain responsible for the development of adverse health conditions: type 1 and type 2 diabetes, metabolic syndrome, polycystic ovary syndrome, and even certain types of cancer.

In this article, we will explore the basic functions of insulin in the body to gain a better appreciation for all it does as well as a clearer understanding of how to keep this hormone functioning in balance and at its optimal capacity.

What Is Insulin?

In technical terms, insulin is a peptide hormone produced by pancreatic beta cells located in the islets of Langerhans. As touched on in the introduction, insulin is the primary anabolic hormone found in the human body.

It governs the metabolic processes your body uses to digest and absorb carbohydrates, proteins, and fats, playing a particularly prominent role in the absorption of carbohydrates—specifically, the movement of glucose from the bloodstream into the liver, muscle, and fat cells throughout the body. Insulin acts on receptors located on the membranes of cells in the liver, other organs, and muscles to promote the uptake of glucose from the blood into the tissue where it is used as fuel or stored as glycogen for later use. Once insulin has successfully engineered the absorption of glucose into the cells, blood glucose levels return to the healthy, baseline range within a few hours.

This touches on the function of insulin that’s most familiar to the average person: its role in regulating blood glucose levels, also called blood sugar levels. Blood glucose or sugar serves as fuel for all the muscles, tissues and organs of the body. Most importantly, it is the primary fuel for the brain. As such, it is extremely important that blood glucose levels be maintained within a very narrow range.

Low blood sugar, or hypoglycemia leaves us shaky, irritable, weak, and unable to focus or think clearly. Very high blood sugar levels wreak havoc on our organs and can even induce a coma. Insulin is released by the beta cells in the pancreas when blood sugar levels increase in response to ingestion of carbohydrates and other nutrients. When blood glucose levels are low, the secretion of insulin is inhibited.

Insulin is not only anabolic with regard to delivering fuel and building glucose stores. It also promotes muscle building and fat storage. Depending on your diet and exercise regimen, insulin can work to build muscle and improve body composition. Alternatively, if calories are consumed in excess, creating a positive energy balance, insulin works to clear excess circulating fatty acids in the blood by promoting their storage in adipose cells.

It’s important to understand that the relationship between insulin and glucose goes both ways. When insulin levels in the blood are high, the liver’s production and secretion of glucose decreases and systems throughout the body prioritize the growth and development of new cells. When levels are low, those effects are reversed, and widespread catabolism (the process by which cells are broken down to release the energy they contain) sets in. The catabolic effect associated with low insulin levels has a particularly prominent impact on stores of body fat.

When beta cells become damaged, insulin synthesis as well as insulin secretion become impaired. One example of this would be the autoimmune reaction that results in type 1 diabetes mellitus, the primary symptoms of which are abnormally high blood glucose concentrations as well as excessive catabolism through the body. Type 2 diabetes mellitus stems from the same cause—the destruction of beta cells—however, it’s differentiated from type 1 diabetes in that damage is not spurred by an autoimmune reaction and is less severe.

A Timeline of Key Discoveries About Insulin

Because of the vital importance of insulin as a diabetes treatment, it has been intensely studied for close to a century.

In the early 1920s, a team of researchers from the University of Toronto hit on a method for extracting insulin from the pancreases of animals and purifying it to make it safe to administer to humans as a treatment for diabetes. This discovery earned them the Nobel Prize in 1923.

As an interesting side note, an eminent Romanian scientist named Nicolae Paulescu successfully extracted insulin and demonstrated its efficacy as a diabetes treatment prior to the Canadian team, however, his extract could not be used on humans. No mention of Paulescu’s work was made when the Nobel Prize was awarded, which has since been viewed as a “historic wrong,” in the words of Ian Murray, a professor of physiology, vice-president of the British Association of Diabetes, and founding member of the International Diabetes Foundation.

In 1955, biochemist Fred Sanger determined the order of the amino acids in insulin, making it the first protein to be sequenced. His work with insulin, which he found was made up of two chains of amino acids (the A chain containing 21 amino acids and the B chain 30) linked by disulphide bonds, led to the knowledge that all proteins found in the human body are composed of varying sequences of some or all of the same set of amino acids. This work resulted in another Nobel Prize, which was awarded to Sanger in 1959.

Insulin spurred another major scientific breakthrough in 1963 when it became the first protein to be chemically synthesized. However, it was not yet possible to produce it on a large scale, meaning that individuals with diabetes had to continue to use animal insulin, which causes side effects such as immune responses in some patients.

In 1969, Dorothy Hodgkin (also a Nobel Prize winner), used X-ray crystallography to map the molecular structure of insulin. This allowed researchers to learn more about the functions of insulin in the body as well as how it’s produced.

The form of insulin used for diabetes care today dates back to 1978, when scientists used genetic modification to get bacteria to generate the A and B chains of insulin, then developed a chemical process to link the chains together. This allowed synthetic human insulin to be mass produced and diabetes to be treated far more effectively.

7 Key Discoveries About Insulin

The 4 Different Types of Insulin

At this time, insulin therapy involves the use of four primary types of insulin differentiated by how rapidly the effect of insulin sets in, when the effect reaches its peak, and how long the effect lasts.

The four types are:

  1. Rapid-acting insulin
  2. Short-acting insulin
  3. Intermediate-acting insulin
  4. Long-acting insulin

Per information provided by the American Diabetes Association, the first type, rapid-acting insulin, can be detected in the bloodstream within 15 minutes of injection, reaches peak concentrations in the blood between 30 and 90 minutes, and continues to be detectable for approximately 5 hours.

Short-acting insulin can be detected within 30 minutes, reaches peak concentrations about 2 to 4 hours after injection, and remains present for between 4 and 8 hours.

Intermediate-acting insulin reaches the bloodstream between 2 and 6 hours after injection, peaks between 4 and 14 hours after, and stays in the blood for around 14 to 20 hours.

Long-acting insulin does not reach the bloodstream for 6 to 14 hours, reaches peak concentrations shortly after, and remains in the blood for between 20 hours and a full day.

Every diabetic has individual insulin needs and responses, and there’s no single type that’s universally best. Rather, it’s important to tailor insulin therapy to a patient’s specific needs. It’s even possible to use two types mixed together to access a range of different delivery times, peaks, and durations.

What You Should Know About the 4 Types of Insulin

Insulin’s Role in the Development of Adverse Health Conditions

Experts have found that abnormal insulin levels as well as changes to the body’s ability to detect the presence of insulin contribute to the development of several health conditions, including:

  • Diabetes mellitus: The symptoms of both type 1 diabetes and type 2 diabetes stem from insulin abnormalities resulting in hyperglycemia (high blood sugar levels).
    • Type 1 diabetes is an autoimmune condition that causes the body to destroy the pancreatic beta cells that produce insulin, ultimately resulting in complete insulin deficiency.
    • Type 2 diabetes results from either impaired insulin production, insulin resistance, or a combination of both. The mechanisms that cause type 2 diabetes have yet to be fully comprehended, but contributing factors seem to include a lack of physical activity and imbalanced diet.
  • Metabolic syndrome: This accounts for a cluster of conditions including high blood pressure, high cholesterol and triglycerides, and abdominal obesity, all of which seem to originate from insulin resistance. Metabolic syndrome often precedes the development of type 2 diabetes as well as heart disease.
  • Polycystic ovary syndrome (PCOS): This hormonal disorder affects women during their reproductive years, resulting in elevated levels of androgen and poorly functioning ovaries. It’s common for PCOS to involve insulin resistance. Once insulin resistance sets in, the body increases its insulin production, which in turn leads to increased production of androgens.
  • Cancer: Insulin promotes extremely rapid cell division, which can cause cancer to metastasize. High levels of insulin also appear to tigger dangerous changes to DNA regulatory genes that can result in cancer. Furthermore, tumors of the beta cells (whether cancerous or noncancerous) result in a condition called insulinoma that causes high levels of insulin as well as reactive hypoglycemia.

Let’s get into some specifics about the role insulin plays in the development of these conditions.

Diabetes

Type 1 diabetes occurs because the beta cells of the pancreas stop producing insulin. The condition is either present from birth or from an early point in childhood. The treatment of type 1 diabetes necessitates careful monitoring of blood sugar levels in combination with regular insulin injections to keep those levels stable.

Type 2 diabetes, once called adult-onset diabetes, though it’s now becoming quite common among adolescents and children, transpires when the body begins to require higher and higher levels of insulin in order for that protein to carry out its essential functions. This happens due to insulin resistance—though a sufficient amount of insulin is present in the bloodstream, the body cannot detect it, meaning it must continue to produce more and more and more. At a certain point, the demand for insulin exceeds the beta cell’s ability to produce it, and synthetic human insulin must be introduced in order to regulate blood sugar levels.

As has been noted already, without enough insulin, physiological disturbances occur that result in unpleasant symptoms such as:

  • Low energy levels
  • Frequent infections
  • Impaired eyesight
  • Numbness or tingling in the extremities
  • High levels of thirst
  • Poor healing of cuts and bruises

As this transpires, the cells of the body shift away from glucose metabolism—since a reliable supply of glucose is no longer available—and begin the breakdown of fat stored as an emergency energy source. If the cells remain in this fat-fueled mode long enough, they begin producing ketones.

As a side note, individuals adhering to the keto diet intentionally pursue the production of ketones by strictly restricting carbohydrates in order to force to body to switch from glucogenesis to ketogenesis as its mode of energy production. In this resulting state of ketosis, the body burns off fat stores at a much higher rate than usual. Intentionally induced nutritional ketosis can be beneficial in terms of weight loss and other potentially positive physiological changes, however, diabetic ketoacidosis is not beneficial at all and is instead quite harmful. In addition to the question of intention, the two states can be differentiated by blood ketone levels. The blood ketone threshold for nutritional ketosis is 0.6 mmol/L. When those levels exceed 1.5 mmol/L, a person is at high risk of ketoacidosis. When left untreated, ketoacidosis can result in severe illness, coma, and even death.

Metabolic Syndrome

Sometimes referred to as insulin resistance syndrome, metabolic syndrome involves the presence of at least three of the following five conditions:

  1. High blood pressure
  2. Low levels of high-density lipoprotein (HDL) cholesterol
  3. High triglyceride levels
  4. High fasting blood glucose levels
  5. Abdominal obesity

A growing consensus among experts holds that insulin resistance is the catalyst behind the development of metabolic syndrome. “Once acquired, those with a genetic predisposition would develop all the other aspects of the disorder,” they claim.

Other researchers believe insulin resistance arises from a sedentary lifestyle, but whether or not the insulin resistance comes first, it’s clear that it plays a pivotal role in the pathogenesis of metabolic syndrome.

Polycystic Ovary Syndrome (PCOS)

Polycystic ovary syndrome results from imbalanced reproductive hormones. It can involve the presence of a fluid-filled cyst inside the ovaries, but the name is somewhat misleading as it’s entirely possible for individuals to have PCOS without developing cysts.

It’s also possible for PCOS to produce very little disruption to a person’s life. In other cases, however, it leads to more serious  health problems including type 2 diabetes and metabolic syndrome.

As touched on above, insulin resistance drives the development of PCOS. Some risk factors that lead to insulin resistance can’t be controlled, but others relate to lifestyle such as diet and physical activity. Proactive steps can help prevent insulin resistance, and making adjustments can also help to reverse this condition.

Cancer

Insulin has been implicated as a factor in overall cancer risk—specifically, high levels of circulating insulin appear to raise your odds of developing cancer.

Because insulin is a growth factor, hyperinsulinemia promotes extremely rapid cell division, which is not desirable when it comes to cancer cells. Cancer cells exposed to high insulin concentrations can proliferate and migrate aggressively.

DNA regulatory genes are also influenced by chronically elevated insulin and blood sugar, which can trigger changes or mutations in the cell. These alterations can lead to cancers in different tissues and organs in the body.

Last but not least, with insulinoma, the tumors (which can be non-cancerous) constantly secrete insulin, thereby causing hypoglycemia (low blood sugar).

How Insulin Leads to the Development of These 4 Conditions

Understanding the Functions of Insulin in the Body

As touched on previously, the presence of glucose stimulates the body to secrete insulin. However, other macronutrients, hormones, and biological compounds also stimulate insulin secretion. The primary function of insulin, as well as its counterpart, glucagon, is to regulate blood glucose concentrations.

Basal Insulin Secretion

A very comprehensive article published in the Clinical Biochemist Reviews establishes the healthy basal level of insulin secretion when the body’s in a fasting state as 0.25 to 1.5 units of insulin per hour. In healthy individuals, basal secretion maintains fasting insulin concentrations in the bloodstream of between 3 and 15 mlU/L. This allows for insulin-dependent entry of glucose into the cells of the body, prevents excessive breakdown of triglycerides, and minimizes glucogenesis, all of which ensures that blood sugar levels remain stable.

Glucose-Stimulated Insulin Secretion

When all is operating as it should, glucose-stimulated insulin secretion occurs in two distinct phases. The first phase is a rapid response, resulting in insulin secretion within one minute of glucose entering the bloodstream. This phase peaks in 3 to 5 minutes and only lasts for about 10 minutes.

The second phase has a slower onset. It’s not apparent until 10 minutes after glucose reaches the bloodstream (at which point the first phase will be over, or close to over). The phase involves continuous secretion of insulin for the duration of the time that blood sugar levels remain elevated. The amount of insulin secreted is proportional to the concentration of glucose in the bloodstream.

The first phase involves insulin that has already been synthesized and stored, while the second phase requires the use of newly synthesized insulin.

The Release of Insulin in Response to a Meal

The neat and tidy insulin responses described above only occur in laboratory settings. In the real world, the secretion of insulin stimulated by food intake proves far more difficult to predict due to the multitude of variables involved, such as:

  • Presence of specific nutrients, including amino acids
  • Physical makeup of the foods
  • Rate of gastric emptying
  • Speed of gastrointestinal motility

Furthermore, neural input as well as other digestive hormones such as incretin affect insulin response.

Specific nutrients produce distinct insulin responses. For instance, non-esterified fatty acids (NEFA),  which may come directly from high-fat foods or from the synthesis of excess carbohydrates, lead to increased output of glucose and reduce insulin sensitivity. There’s some indication, too, that they alter glucose-stimulated insulin secretion—in the short-term, elevated levels of NEFA in the blood have been linked to increased glucose-stimulated insulin secretion, but chronically high levels of NEFA result in decreased glucose-stimulated insulin secretion as well as decreased insulin synthesis.

The Role of Insulin Receptors

First described by scientists in 1971, insulin receptors contain special proteins called insulin responsive substrates (IRS) that mediate the effects of insulin on the body’s cells.

Four distinct IRS proteins have been identified and named (rather prosaically): IRS 1, IRS 2, IRS 3, and IRS 4.

IRS 1 controls most actions of insulin in the skeletal muscle cells. IRS 2 handles the liver as well as peripheral insulin signals and the development of pancreatic beta cells. The roles of IRS 3 and 4 remain somewhat more mysterious. IRS 3 can be found in fat cells as well as in beta cells and in the liver, while IRS 4 appear in the thymus, brain, and kidneys.

How Insulin Functions on a Cellular Level

The primary functions of insulin in the body’s cells have to do with the metabolism of carbohydrates, fats, and amino acids from protein as well as the transcription and translation of mRNA.

  • Carbohydrates: Insulin contributes to carbohydrate metabolism at many points during the process. It facilitates the diffusion of glucose from carbohydrates into fat and muscle cells, signals the presence of an abundance of intracellular energy, and more.
  • Fats: Insulin instigates the synthesis of fatty acids in adipose tissue (fat) as well as in the liver and in the mammary glands during lactation. It also affects the metabolism of phospholipids.
  • Protein: Insulin stimulates protein synthesis throughout the body. It also contributes to the transcription of mRNA as well as aiding translation of mRNA into ribosomal proteins.

In a big-picture sense, insulin’s role has to do with the regulation of the body’s cellular energy supply and the balance of micronutrients. When the body is in a fed, as opposed to fasting, state, insulin orchestrates the anabolic processes that lead to muscle growth (so long as a sufficient quantity of amino acids are available), tissue healing, and more. Insulin signals an abundance of energy, indicating to the body that it can halt the breakdown of fat stores and instead carry out fat synthesis.

How Does Insulin Function in the Body?

How to Enhance Insulin Function

Aside from the nutritional strategy of minimizing large spikes in blood glucose, the most effective way to enhance insulin function is to stay physically active.

It makes sense that insulin is an important factor in making sure the body is properly fueled for physical activity. Insulin helps deliver glucose from the blood into the muscle cell. Once in the muscle, glucose is metabolized to produce energy to support physical exertion. Insulin also stores excess glucose as glycogen so that it can be used for energy at a later time.

Dietary protein and amino acids can also stimulate insulin release. Consuming a balance of carbohydrate and protein during exercise has been proven to stimulate more insulin than carbohydrate alone, resulting in faster delivery of glucose to working muscles.

Insulin is also needed to optimize recovery of muscles from a hard workout. Immediately after exercise, the muscle is primed to replenish fuel stores like glycogen and to rebuild and repair muscle proteins. During this period, insulin accelerates the rate at which glycogen and protein synthesis proceeds, up to 2 to 3 times the normal rate as long as carbohydrate and protein are ingested and made available.

Insulin likes to do these jobs, and can carry them out quite efficiently. However, for individuals who live sedentary lifestyles, the muscles use very little stored fuel, resulting in an abundance of excess fuels, carbohydrates, fats, and amino acids in circulation. The good news is, just a single bout of exercise can wake up the insulin receptors and enhance their sensitivity and functioning.  This helps rebalance the body’s energy utilization and storage processes.

Tips for Enhancing Insulin Function

Conclusion

In summary, insulin is an amazing hormone dedicated to ensuring that the food we eat is properly routed to where it is needed and when it is needed. A poor diet high in processed carbohydrates, excess energy intake, and lack of physical activity all tax the ability of insulin to do its job properly.

The overproduction of insulin, as it tries to overcome these challenges, has led to an interpretation that insulin in some way contributes to metabolic dysfunction and health complications. While it’s true that abnormal insulin levels as well as changes to the body’s ability to detect the presence of insulin can lead to the development of adverse health conditions such as diabetes, metabolic syndrome, polycystic ovary syndrome, and even cancer, insulin itself is not to blame.

Rather, the true instigating factors in the development of these conditions can be traced back to a person’s genes, lifestyle choices, environment, or a combination of all the above. By supplying your body with a properly balanced diet and prioritizing physical activity as much as your other commitments and overall health allow, you can build a foundation for proper insulin function that will keep this crucial hormone operating as a “good guy, not a “bad” one.

Pulled and Torn Calf Muscle Recovery Time: How to Heal Your Lower Leg

This article has details on how to rest the injured area, how long it takes for pulled or torn calf muscle recovery time, and how to strengthen the back of the lower leg to avoid reinjury going forward.

Anything from a calf strain to an outright muscle tear can hobble you, interrupting your ability to walk, to work out, and to enjoy your daily life. This article has details on how to rest the injured area, how long it takes for pulled or torn calf muscle recovery time, and how to strengthen the back of the lower leg to avoid reinjury going forward.

The Calf Muscle and Lower Leg

In human anatomy, the calf muscle is located on the back of the lower leg. It consists of two distinct muscles, the larger gastrocnemius muscle, which creates the visible bulge on the back of the leg, and the soleus muscle, a flatter muscle that lies beneath the gastrocnemius muscle.

The calf is attached via the Achilles tendon to the heel of the foot. The calf muscle allows us to flex the ankle and the knee, and to run, jump, and rise to our tippy toes. It’s an integral part of daily movement.

Calf Muscle Injuries

There are many degrees of calf muscle injury. Here’s a breakdown of the different soft tissue injuries that could be causing calf pain.

  • Calf muscle strain: Straining the calf muscle involves a tearing of the calf muscle fibers. Muscle strains can exist along a spectrum from mild cases of light pain and soreness to severe cases of complete tear.
  • Pulled calf muscle: Another name for a calf muscle strain, a pulled calf muscle is caused by “pulling” or overstretching the muscle beyond its natural limits.
  • Calf muscle tear: Any strain involves some measure of tearing, but the more serious ones are partial or complete tears that may require surgery to fix.
  • Calf muscle rupture: A complete tear is also known as a rupture, which impairs the ability to walk and may display a lump under the skin if the calf collapses.
  • Calf muscle myositis: Another culprit that can cause calf pain is myositis, a rare inflammation of the muscle that can occur due to infections or autoimmune disorders.
  • Calf muscle cancer: This is another rare condition, but in cases of cancer, it is possible for a tumor (sarcoma) to form in the calf muscle or for other cancerous growths to spread to the calf (metastasis).

Pulled or torn calf muscle recovery time.

Pulled or Torn Calf Muscle Recovery Time

A pulled or torn calf muscle can be a brief concern, a mild injury resulting from a one-time accident or overstrain. It’s a common sports injury, familiar to many athletes and runners, but one strain that is not properly healed can become a long-term chronic injury that is more likely to become reinjured multiple times. Chronic calf injuries could possibly lead to a complete calf tear and immobility. The treatment options and recovery times differ depending on severity.

Pulled Calf Muscle Recovery Time

A milder pulled calf injury may come with symptoms like redness, bruising, mild swelling, and an inability to stand up on the ball of your foot. Depending on the severity of the injury, these types of sprains can usually be treated at home with RICE and other healing aids. RICE stands for:

  • Rest: If sharp pain makes it difficult for you to walk normally, stay off your feet or use the aid of a cane or crutch to give your body time to heal.
  • Ice: An ice pack or a cold compress applied to the area for 10 minutes at a time, every hour or so in the first few days, can help reduce inflammation and swelling, plus ease pain.
  • Compression: A leg wrap can also help reduce swelling and increase your mobility while you heal.
  • Elevation: Prop up your leg above the level of your heart to help reduce swelling and pain.

Other options for at-home treatment include a heating pad to help draw blood to the area after the first few days (just be sure not to fall asleep with the pad on as it could cause skin burns or exacerbate swelling). You might also try over-the-counter anti-inflammatories like ibuprofen—just be sure to take them as directed. For more natural aids, consider taking an amino acid supplement to increase the supply of raw materials needed to mend muscle fiber: all nine essential amino acids.

The recovery time for a mild calf injury is a few days to a week. You may only have to take special care to treat the injury in the first day or two. So long as you don’t reinjure the area by resuming vigorous physical activity too soon, your body will take care of the rest. In more severe cases it could take a month to 6 weeks to fully heal an injured calf muscle, so just be sure to listen to your body before resuming sports activities.

Torn Calf Muscle Recovery Time

Symptoms of a torn calf that don’t improve after a few days or start to worsen could be a sign of a more severe tear or a gastrocnemius muscle rupture. Also known as “tennis leg,” calf ruptures may require surgical intervention and/or physical therapy. Prompt treatment should be sought if you suspect the injury won’t improve with at-home care, as some injuries could handicap the affected leg for the rest of your life.

Keep in mind that around 30% of people who have one calf muscle strain end up experiencing repeated injuries because they’re not fully healed before returning to strenuous activity. This is especially true for athletes who demand the same movements from their bodies over and over again. Also keep in mind that it’s possible to herniate the muscle of a calf, prompting repeated and chronic injury.

The recovery time for a fully torn calf muscle will be longer than a simple strain and will depend on the treatment option you choose with your doctor or physical therapist, plus other factors like your age and general fitness level. Once you are healed, it’s important to restrengthen your calf to avoid future injuries.

How to Prevent a Torn Calf Muscle

Here are some stretches and strengthening exercises you can use to help minimize the risk of calf injury and hopefully prevent future sprains and injuries.

  • Warm up and stretch for at least 5 minutes before engaging in exercise or sport, and set aside time for a cool-down period of stretching to prevent cramping.
  • Use a chair stretch to loosen up your hamstrings. It’s important to stretch your whole leg and body before working out, as every bit of the body is connected to the rest, and tension in one area could cause an injury in another.
  • Wall stretches allow you to focus on loosening up the back of the leg from heel to hip.
  • The floor or supine stretch helps condition your leg muscles for the prevention of injury.
  • A standing calf stretch is not only targeted for calf strength but can also be easily done just about anywhere throughout the day.
  • Supplement with amino acids to help support muscle recovery and repair with a full host of the building blocks of new protein synthesis.

Proper stretching helps prevent injury and strengthens the stability of your knee, improving your physical performance and protecting other areas of the leg from getting hurt. For more specific medical advice or help with your technique, consult with a doctor or qualified physiotherapist.

Long-Term Calf Recovery

Calf injuries are relatively common in sports medicine and physiotherapy and can quickly become debilitating if they keep you from walking. Be extra cautious as you heal these injuries to reduce recovery time. And be sure to consume the right amount of amino acid nutrition to build new muscle fibers. The faster you heal, the better chance you have to return to your full range of motion and make instances of further injury less likely.

T-Lymphocytes: How Your T-Cells Save Your Life

You may have heard vaguely about the importance of T-lymphocyte or T-cells in your immune system, but how do they function? Find out how closely linked amino acids like glutamine, methionine, and leucine are to your immune system response and the utilization of T-lymphocyte cells to fight diseases and cancer.

You may have heard vaguely about the importance of T-lymphocyte or T-cells in your immune system, but how do they function? And what do they have to do with amino acids? We break down the science so that if ever you hear your T-cells are too high or too low, you’ll know what the doctor is talking about.

What Are T-Lymphocytes?

A lymphocyte is a type of white blood cell, and each white blood cell has a specific role to play in the body’s immune function. Like all blood cells, T-lymphocytes come from haematopoietic stem cells, which are stem cells in our bone marrow. They work to fight infections and various types of cancer cells in an adaptive immune system, also referred to as an acquired immune system. Our adaptive immunity uses T-cells and B-cells (B-lymphocytes, also derived from bone marrow) to battle organisms and intracellular pathogens that slip through the frontlines of our bodies’ defenses.

T-cells work in cell-mediated immunity. While we’re born with other innate immune cells like dendritic cells, basophils, neutrophils, and macrophages (which are also deployed in emergency immune responses), T-cells and B-cells launch a more sophisticated and targeted attack.

Both T-cells and B-cells are specialized cells that we earn by surviving in our environments. These cells tend to live longer than innate immune cells, and they are also the cells that allow for vaccinations to work due to their ability to learn, adapt, and grow stronger.

B-cells mature in our bone marrow, whereas T-cells travel first to the thymus gland and become thymocytes, which is where they get their “T,” and continue to mature and differentiate. Our thymus glands shrink as we age, making T-cell expansion more and more vital as we grow older.

Immunotherapy treatments for multiple forms of cancer, including cancers of the bloodstream like lymphoma and leukemia, rely on T-cells. T-cells are less likely than B-cells to mutate into liquid cancers like chronic lymphocytic leukemia or B-cell lymphoma, and T-cells can also be engineered into chimeric antigen receptors, able to identify specific proteins on tumor cell membranes for a surgical strike against cancer.

Types of T-Lymphocytes

There are two major types of T-cells: helper T-cells, which stimulate B-cells to create antibodies, and killer T-cells, which mercilessly strike out any compromised or infected cell they find.

Taking advantage of this ability to target cells, researchers have developed anti-cancer drugs to enhance this form of autoimmunity against cancers like melanoma and lung cancer, disrupting the surface marker evasions these cells employ to sneak into the body and activating the surface receptors of T-cells to focus them on cancer elimination.

Further T-cell specifications break down into five types of T-cells.

  • CD4+ T-Cells: These helper cells activate when they discover MHC Class II molecules (major histocompatibility complex) on the cell surface of antigen presenting cells (APCs). They stimulate B-cells to become plasma cells and memory B-cells, activate innate macrophages and cytotoxic T-cells, and rapidly divide while secreting cytokines (small proteins) to alert the immune system’s response.
  • CD8+ T-Cells: CD8+ cytotoxic T-cells (CTLs) cause lysis (cell wall disintegration) in antigenic tumor and virus-infected cells.
  • Memory T-cells: Naive T-cells upon activation differentiate into either CD4+ or CD8+ effector function cells, or memory T-cells. Memory T-cells are long-living, and therefore have the ability to “remember” encountered pathogens and quickly expand into CD4+ or CD8+ in large numbers when they encounter them again.
  • Natural Killer T-Cells: Most T-cells function after recognizing MHC molecules (MHC-I or -II) via T-cell receptors (TCRs), but these natural killer cells are able to bind to other foreign antigen cells without that stimulation, and proceed to kill them by inserting perforin-containing granules through the cell walls (perforin is a protein that creates lesion-like pores in cell membranes).
  • Regulatory T-cells: Regulatory T-cells are present to check the immune system and help prevent the development of autoimmune diseases and allergies to common environmental realities like molds, pollen, or pet dander.

What Are T-Lymphocytes?

Amino Acids and the Immune Response

Thymic, or T-cell activation, is closely linked to our amino acids. Most of our lymphocytes, including T-cells, move through the lymph nodes and other lymphatic organs like the tonsils and spleen, but they can’t do so unaided. There are amino acids necessary for this immune response.

Glutamine

Glutamine is a nonessential hydrophilic amino acid that is coupled with naive T-cell activation and linked to the amino acid transporter ASCT2. Researchers have found that inflammatory T-cell responses rely on amino acid transporter ASCT2 and come with a rapid glutamine uptake. Though it’s still not largely understood, it’s nevertheless clear that glutamine plays a role in the immune response necessary to defeat deadly pathogens.

Methionine

Methionine is an essential amino acid that researchers have identified as necessary for the synthesis of new proteins and muscle and for the methylation of RNA and DNA, which drives T-cell proliferation and differentiation. Essential amino acids are those our bodies cannot make independently, and so must be consumed in the proper amount via food sources or supplementation.

Leucine

Again, the amino acid transporters that are tasked with the uptake of essential amino acids like leucine are attached to the development, maintenance, and activation of T-lymphocytes. This 2017 review looked at LAT1 (L-leucine transporter) along with ASCT2 (L-glutamine transporter) and GAT-1 (γ-aminobutyric acid transporter-1) and found that they are important for the fate decisions and determinations of memory T-cells and other lymphocytes. The researchers also suggested that manipulation of the amino acid transporter-mTORC1 axis could help manage inflammatory and autoimmune diseases tied to T-cell-based immune responses.

What Interrupts T-Lymphocyte Function?

T- and B-lymphocytes work hand-in-hand to fight disease and infection, but sometimes they are forced out of order in circumstances of illness. Doctors can often use a blood count of overall lymphocyte content to determine whether or not there is something afflicting your immune system. If your lymphocyte count is too high or too low it could indicate the following diseases and disorders.

Low Lymphocyte Count

A low lymphocyte count is known as lymphocytopenia, and can arise if your body isn’t producing sufficient lymphocytes, if the lymphocytes you do produce are being destroyed, or if they are trapped in places like your spleen or lymph nodes. With a lower lymphocyte count you are more at risk of developing infections, and that low count is often associated with the following conditions:

  • Influenza
  • HIV/AIDS
  • Undernutrition
  • Steroid usage
  • Radiation therapy and chemo drugs for cancer
  • Cancers like Hodgkin’s lymphoma
  • Autoimmune diseases like lupus
  • Inherited conditions like DiGeorge or Wiskott-Aldrich syndrome

High Lymphocyte Count

A high lymphocyte count, called lymphocytosis, is also an indication that your immune system is under attack from an overwhelming disease or illness, such as the following:

Amino Acids and The Immune Response

Taking Care of Your T-Cells

Without T-lymphocyte cells standing as the second line of defense against diseases, viruses, and cancer cells, our immune systems would collapse. Scientists are hard at work not only trying to understand the utilization pathways of these cells, but also striving to improve their numbers and recruit them in the battle to cure cancer. Closely tied to the movement and usage of our amino acids, T-cells are the special ops team keeping each of us alive.

Breaking Down the Organic Acid Test, Step by Step

By measuring levels of over 70 metabolites, the organic acid test allows individuals to better understand their overall health. The OAT can help identify the underlying causes of frustrating health issues, thereby forming the foundation for the creation of a highly individualized treatment plan.

The Organic Acid Test (OAT) measures a range of metabolic markers—over 70 in total—to provide insight into a person’s health. By providing an accurate evaluation of intestinal yeast and bacteria, fungus, mold, oxalates, metabolites, neurotransmitters, vitamins, minerals, and antioxidants, the test offers insight into your body’s energy production and detoxification capacity.

In recent years, the test has gained quite a following among experts in the functional medicine world. It’s a simple, noninvasive urine test that can yield a wealth of valuable information for individuals with chronic illnesses, neurological conditions, and other health concerns. The OAT can also be useful for those who simply wish to gain a better understanding of their overall health and identify nutrient deficiencies as well as genetic factors that may need to be strategically addressed. The OAT can provide cellular-level wisdom about the underlying causes of frustrations like low energy levels, recurrent abdominal pain, and more.

Before explaining how organic acid testing works in more detail, however, let’s take a moment to go over some basics about organic acids themselves.

Quick Facts About Organic Acids

Organic acids, in short, are organic, acidic chemical byproducts of the body’s metabolic processes that get excreted in the urine. Many organic acids are generated by the bacteria and other microorganisms that populate the digestive tract.

The chemical makeup of organic acids always includes carbon and hydrogen molecules, and sometimes contains oxygen, phosphorus, nitrogen, and sulfur molecules too.

The names of the organic acids can be used as clues to their composition. Most of their names use the suffix “ic”—for example, lactic acid. The letters before the suffix indicate its conjugate base—each organic acid has one or more—which ends with the suffix “ate.” So, going back to our example, you can deduce that the conjugate base of lactic acid is lactate. While this all sounds, and is, highly technical, it’s helpful to know, as it’s common to see the name of the organic acid—lactic acid—and the name of its conjugate base—lactate—used interchangeably.

What Does the Organic Acid Test Measure?

As touched on in the introduction, the organic acid test measures levels of over 70 biomarkers that provide information about the state of a multitude of metabolic pathways throughout the body. Abnormal organic acid levels indicate the presence of metabolic dysfunction arising from underlying causes such as:

  • Nutritional deficiencies
  • Exposure to toxins
  • Neuroendocrine malfunction
  • Enzyme deficits
  • Overgrowth of intestinal bacteria

Scientists use either gas or liquid chromatography in combination with mass spectrometry to measure organic acid levels. In most cases, they look at levels in a urine sample, as organic acids tend to be far more concentrated in urine than in other bodily fluids—they can be found at 100 times the concentrations seen in blood, for instance. More than 1,000 organic acids can be detected in a single urine sample.

When organic acid levels fall below the optimal range, the body’s ability to carry out essential functions becomes compromised. And when they rise too high, that can be harmful too—it may, for example, lead to metabolic acidosis.

The OAT can not only detect organic acid abnormalities and their underlying causes, but it can also help you determine the best course of treatment, which might involve some or all of the following elements:

  • Dietary changes
  • Targeted supplementation
  • Detoxification practices

Should You Take the Organic Acid Test?

Historically, the organic acid test was performed primarily in hospital settings as a means of assessing genetic metabolic defects in children. However, as new markers have been introduced, its applications have expanded. The test can now reveal health issues stemming from non-genetic factors, meaning more individuals can benefit from the information it provides.

Studies have shown correlations between abnormal organic acid levels and chronic conditions including fatigue and kidney disease as well as neurological disorders like autism. Based on the findings of the OAT, dietary interventions and targeted supplementation can be used to bring about significant clinical improvements.

The OAT can also be a relatively inexpensive way for individuals to try to suss out the root cause of health issues. It can give a more in-depth perspective than conventional bloodwork offers. Individuals dealing with sleep disturbances, mood disorders, skin issues, gastrointestinal problems and more can all garner helpful information from the OAT.

If You're Dealing with One or More of These Issues, Consider Taking the OAT

Breaking Down the 12 Sections of the Organic Acid Test

The organic acid test evaluates biomarkers relevant to a range of health issues. The test itself is divided into 12 sections:

  1. Intestinal microbial overgrowth
  2. Oxalate metabolism
  3. Glycolytic cell metabolism
  4. Krebs cell metabolites
  5. Amino acid metabolites
  6. Neurotransmitter metabolities
  7. Pyrimidine metabolites
  8. Ketone and fatty acid metabolites
  9. Nutritional markers
  10. Indicators of detoxification
  11. Mineral metabolism
  12. Fluid intake and hydration levels

Now, we’ll go section by section, discuss what exactly is being measured and how those measurements shed light on your overall health and wellness.

1. Intestinal Microbial Overgrowth

The first section of the OAT looks at markers indicating the presence of yeast and fungi, such as:

  • Candida
  • Mold
  • Clostridia

If multiple markers are elevated, that’s quite concerning. Overgrowths of fungi and yeast can interrupt immune function and digestion. They can also create imbalances in the production of stress hormones.

Elevated markers in this section often correlate to conditions such as:

2. Oxalate Metabolites

High levels of oxalates, one of the most acidic of the organic acids, can be quite damaging. The structure of oxalate crystals involves sharp edges that can damage the tissues of the body, resulting in pain, inflammation, and oxidative stress.

The location where oxalate crystals form determines the symptoms associated with the presence. Some locations they can develop include:

  • Joints
  • Organs
  • Blood vessels
  • Muscles
  • Glands

Elevated oxalate levels can be a factor in chronic joint pain, kidney stones, and other health problems.

Often, high oxalic acid levels result from deficiencies in vitamin B6 as well as heavy consumption of foods rich in oxalates. Many of those foods are quite nutritious, such as:

  • Spinach
  • Beets
  • Wheat bran
  • Berries
  • Almonds

Correcting elevated oxalic acid levels will likely involve both increasing vitamin B6 intake as well as decreasing intake of foods high in oxalates.

3. Glycolytic Cycle Metabolites

During a process called the glycolytic cycle, or glycolysis, the body generates lactic and pyruvic acid from glucose (sugar) in order to give us energy.

Elevated levels of lactic or pyruvic acid indicate that a person’s metabolism has become overly reliant on sugar and is underutilizing fat. This results from mitochondrial dysfunction, which may stem from exposure to environmental toxins such as mold.

Other potential causes of high levels of glycolytic cycle metabolites include:

  • Intense exercise
  • Shock
  • Bacterial overgrowth
  • Anemia
  • Oxidative stress

4. Krebs Cycle Metabolites

The Krebs, or citric acid, cycle is comprised of a series of chemical reactions in the mitochondria. Similar to glycolysis, this process produces energy. Elevated levels or unnaturally low levels of Krebs cycle metabolites also indicate mitochondrial dysfunction, often stemming from deficiencies in various nutrients and enzymes that are vital to the health of your mitochondria.

For instance, abnormally high low levels of sunnic can be a sign of a vitamin B2 or coenzyme Q10 (CoQ10) deficiency, while extremely low levels of sunnic point to possible deficiencies of two branched-chain amino acids, leucine and isoleucine.

5. Amino Acid Metabolites

This section of the OAT measures levels of three amino acid metabolites: 3-Methylglutaric acid, 3-Hydroxyglutaric acid, and 3-Methylglutaconic acid.

When these measurements are high, that’s a sign of both impaired mitochondrial function as well as poor metabolism and absorption of amino acids. Typically, those imbalances will produce gut inflammation.

If amino acid metabolite levels are high, but glycolytic and Krebs cycle metabolites are normal, that indicates metabolic difficulties specifically with the breakdown of protein and the absorption of the amino acids it contains.

6. Neurotransmitter Metabolites

This section of the test has the greatest relevance for individuals dealing with insomnia, ADHD, autism, and mood disorders such as anxiety and depression. It measures levels of metabolites for phenylalanine and tyrosine—HVA and VMA—as well three metabolites for tryptophan—5-HIAA, quinolinic acid, and kynurenic acid.

High levels of stress can have a seriously adverse effect on phenylalanine and tyrosine metabolites, as does exposure to lead. Additional factors related to abnormal levels of these metabolites include:

  • Vitamin C deficiency
  • Low copper levels
  • Bacterial overgrowth

Abnormal levels of tryptophan metabolites can be a sign of issues such as:

  • Serotonin deficiency
  • Neurological inflammation
  • Microbial infection
  • Degeneration of the central nervous system
  • Inappropriate tryptophan supplementation
  • Exposure to phthalates
  • Vitamin B6 deficiencies
  • Overactive immune system
  • High cortisol levels

7. Pyrimidine Metabolites

Levels of pyrimidine metabolites (uracil and thymine) reflect how well the body is metabolizing folate.

A body deficient in folate (vitamin B9) has high uracil levels. Other causes of high uracil levels include mutations to the MTHFR homozygous gene and issues with methylation.

Individuals on extremely high-carbohydrate diets, as well as alcoholics, can become deficient in vitamin B1, leading to high levels of thymine, a physiological state linked to inflammatory diseases and cancer.

8. Ketone and Fatty Acid Metabolites

The eight ketone and fatty acid metabolites measured by this section of the OAT provide valuable information about fat metabolism.

Individuals on low-carbohydrate diets, such as the ketogenic diet, will have elevated levels of these markers as an innate feature of that eating approach. In individuals not adhering to such a dietary protocol, elevated levels indicate impaired absorption of fats.

Often, the underlying cause of such an issue is gut inflammation. It can also indicate widespread oxidative stress.

9. Nutritional Markers

This can be one of the most important sections of the OAT, as it can pinpoint nutritional deficiencies that may cause both physical and mental health conditions. It does this by measuring the byproducts generated when nutritional deficiencies set in.

For instance, elevated levels of methylmalonic acid correlate to a vitamin B12 deficiency, which might be caused by pernicious anemia, small intestinal bacterial overgrowth (SIBO), or simply malabsorption.

Some of the nutritional deficiencies that can be flagged by this section include:

  • Vitamin B12
  • Other B vitamins
  • Vitamin C
  • CoQ10
  • N-Acetylcysteine
  • Biotin (vitamin H)

10. Indicators of Detoxification

This section yields crucial information about your body’s capacity for detoxification. One way it does this is by measuring levels of an essential antioxidant called glutathione. It’s common for chronic health issues to deplete the body’s glutathione supply.

High levels of pyroglutamic acid, a metabolite of glutathione, indicate that the body has an insufficient supply, typically due to overuse. Underlying causes such as infections and exposure to environmental toxins can demand more glutathione than the body can generate.

High levels of orotic acid, another significant marker of detoxification, indicate the presence of excess ammonia in the body. Ammonia toxicity has a pronounced effect on brain tissue, producing symptoms like:

  • Anxiety
  • Headaches
  • Difficulty concentrating

While genetic issues account for some instances of poor ammonia metabolism, it can also be caused by viral infections, poor liver or kidney function, and gut dysbiosis and other gastrointestinal issues.

11. Mineral Metabolism

This section measures levels of phosphoric acid, which provides a view of the body’s supply of vitamin D and calcium—vital for the growth and maintenance of your bones.

Low levels of phosphoric acid point to a deficiency, which might stem from:

  • Poor phosphate intake
  • Impaired production of digestive juices
  • Deficiency of vitamin K2
  • Deficiency of magnesium

High levels of phosphoric acid might mean that a person has been exposed to toxic levels of lead, or that they’re getting too many phosphates in their diet (often from high consumption of processed foods). It can also result from inappropriate vitamin D supplementation.

12. Creatine Levels

The final section of the OAT measures creatine, which shows how dilute a person’s urine is. This, in turn, provides information about fluid intake and hydration.

High levels of creatine tend to result from dehydration, but may also be caused by excessive exercise, inappropriate creatine supplementation, or a urinary tract infection. If creatine levels exceed 300, kidney problems are indicated.

What's Covered by Each Section of the Organic Acid Test?

How to Perform an Organic Acids Test

It’s now possible to perform an OAT test at home using mail-order kits that come with comprehensive instructions and all the necessary materials. Most ask that you collect urine immediately after waking and prior to the consumption of any food or beverages.

It’s also important to follow instructions relating to foods that contain compounds with the potential to produce false positives for certain biomarkers. Typically, you would need to avoid eating these foods 2 days prior to the collection of your urine sample.

Some foods known to cause problems include:

  • Apples
  • Cranberries
  • Grapes and raisins
  • Pears

You may also need to refrain from taking certain supplements, including echinacea and reishi mushrooms, for at least 12 hours leading up to urine sample collection.

Conclusion

By measuring levels of over 70 metabolites, the organic acid test allows individuals to better understand their overall health. The test looks at metabolites related to:

  • Detoxification
  • Fatty acid metabolism
  • Oxalate levels
  • Mitochondrial function
  • Neurotransmitter levels
  • Vitamin and antioxidant levels
  • Yeast and bacterial overgrowth

The test can help individuals identify the underlying causes of frustrating health issues, thereby forming the foundation for the creation of a highly individualized treatment plan.

Kidney Pain After Drinking Alcohol: How Worried Should You Be?

What causes kidney pain after drinking alcohol? How dangerous is kidney pain and does it require a trip to the doctor? We have the details on how alcohol affects your kidneys, and what health conditions may arise from excessive drinking.

The most detrimental effect of alcohol overconsumption, aside from any personal or psychological problems that arise, is the impact alcohol has on our detox organs: the liver and the kidneys. Imbibing a harmful substance like alcohol regularly overtaxes these organs with the effort of clearing out the poison, opening us up to certain risk factors associated with alcohol abuse. Heavy drinkers or those who engage in binge drinking are doing even more harm than those who drink in moderation, and alcohol abuse could lead to serious kidney problems. If you experience kidney pain after drinking alcohol, we have the information you need on the possible causes.

How the Kidneys Function and Where They Are Located

Our kidneys are part of the system known as the urinary tract, which also includes our bladders and ureters. Kidney health is essential for filtering toxins and waste out of our blood and transferring those substances to our urine for elimination from the body. The kidneys also keep our electrolyte and fluid levels balanced, and they are directly impacted by the excessive intake of alcohol.

Our kidneys are vital to our survival, and luckily they are one of many paired organs and parts our bodies have, like our eyes, ears, testes/ovaries, lungs, limbs, adrenal glands, and more. What’s fortunate about that is it’s quite possible to live with only one kidney, a fact that allows healthy, living people to donate one of their kidney organs to save the life of someone who has lost the use of both.

The kidneys are about the size of our fists and are located below the rib cage on either side of our spines. Kidney pain may be experienced as back pain, but if there is kidney damage resulting from alcohol use, other symptoms may occur. We review the symptoms of kidney damage and kidney failure further along in this article, but first let’s discuss how alcohol interacts with the kidneys.

Alcohol’s Effect on the Kidneys

According to the National Kidney Foundation, alcohol harms the kidneys in the following ways.

  • Interruption of function: High blood alcohol levels can cause changes in the function of the kidneys, interrupting the prime objective of these organs, which is filtering the blood.
  • Interference with fluid levels: Another principle role of the kidneys is fluid regulation, and alcohol as a diuretic forces frequent urination and causes dehydration and possible kidney stone formation (more information on kidney stones below).
  • Elevated blood pressure: Consumption of alcohol frequently causes high blood pressure, which increases the risk of kidney disease and other cardiovascular health problems.
  • Interrelated liver damage: Chronic alcohol consumption can cause liver disease and liver failure, disrupting the rate of blood flow between it and the kidneys and detrimentally impacting all of them.

Some of these impacts won’t be felt until they cause you pain, or lead to other health conditions with recognizable symptoms. If you suspect you’ve overdone it on alcoholic beverages, seek medical advice before being prompted by severe pain: your doctor may be able to detect the early signs of kidney stressors before they cause irreversible damage.

Alcohol's Effect on the Kidneys

Kidney Pain After Drinking Alcohol: Symptoms

Here is a list of symptoms that may indicate there is something wrong with your kidneys. Seek medical advice for a specific diagnosis if you experience:

  • Stabbing or dull pain in your mid-lower back (on either or both sides)
  • Pain between the buttocks
  • Chills
  • Fever
  • Unexplained fatigue
  • Loss of appetite
  • Headache
  • Nausea
  • Vomiting
  • Trouble sleeping
  • Worsening kidney-area pain after sleeping
  • Painful urination
  • Blood in urine

Kidney Pain After Drinking Alcohol: Possible Causes

Here are some of the potential causes of alcohol-related kidney pain.

1. Dehydration

Because alcohol is a diuretic, it can cause severe dehydration when over-consumed, and in fact dehydration is one of the biggest culprits in causing the symptoms of a hangover (like headache). When we drink alcohol in excess, it overrides our kidneys in the area of water retention and balance, not only flushing more water than necessary out of our systems, but also the vitamins, salts, and electrolytes we need along with that water. This is why many a hangover recovery involves drinking a sports drink full of electrolytes or (more problematically) a hair-of-the-dog cure in the form of a spicy Bloody Mary.

Extreme dehydration can cause palpable kidney pain. Water is the best cure for dehydration, while sugary drinks should be avoided after a hard night of drinking. In severe cases, you may need to visit a doctor for an IV fluid.

2. Kidney Stones

When worrying about how alcohol affects the kidneys, many wonder, “Can alcohol cause kidney stones?” Dehydration can, and excessive alcohol consumption quickly induces dehydration.

When there isn’t enough fluid available to filter out certain substances like calcium or uric acid through urine, those substances will deposit in the kidneys and form into stones. Not only can alcohol contribute to the formation of the stones, but if you have kidney stones already, extreme dehydration can also cause them to move, resulting in kidney pain and (if they’re small enough to pass without medical intervention) pain throughout your urinary tract.

If you suspect you have kidney stones, increase your water consumption and consult with a medical professional for assistance and possible medication to help break them up. According to the Mayo Clinic, kidney stone diagnoses may involve blood tests, urine tests, imaging tests, and tests on any passed stone to analyze its content in the hopes that such information will help prevent future stones from forming.

3. Hydronephrosis

Hydronephrosis is a condition characterized by one (or two) swollen kidneys, filled with urine due to an obstruction or blockage of the urinary tract. This could be caused by kidney stones, and may present with flank pain or an inability to urinate.

This condition requires immediate medical attention, and treatment may involve antibiotics if the blockage is caused by a kidney infection instead of kidney stones.

4. Kidney Infection

A kidney infection can come about due to a number of causes, including bacteria that enters through the urethra and bladder, and then moves up to one (or both) kidneys. This would be a UTI (urinary tract infection), and drinking alcohol can worsen the severity of a UTI.

A UTI can be a minor infection, but if it travels to and takes hold in the kidneys, it can cause lasting kidney damage and even kidney failure if it isn’t treated successfully in time. It’s important not to hesitate in seeking advice from a health care professional, and it may be advisable to abstain from drinking if you have a UTI, and definitely if you are taking antibiotics to treat a UTI or any other infection.

5. Liver or Kidney Disease

Liver disease and kidney disease are conditions that can be caused by long-term alcohol abuse, sometimes as part of end-stage alcoholism and death. While it’s not a concern after one night of binge drinking, if you habitually over-imbibe, the damages can accumulate in the liver and cause fatty liver disease or scarring that leads to cirrhosis. Once the liver becomes compromised, the blood flow to the kidneys is interrupted, instigating a domino effect of vital organ damage and possible shutdown.

Should kidney disease develop, it could be due to alcohol or other contributing health conditions that alcohol exacerbates, including high blood sugar, type 2 diabetes, and high blood pressure. Chronic kidney disease can lead to kidney failure, which, like liver failure, can sometimes only be reversed by organ transplantation.

Don’t Kid Around with Kidney Function

Excessive drinking can lead to very painful and serious health consequences, and while there are natural ways to support your kidney health with a kidney flush diet, as Benjamin Franklin once pointed out, “an ounce of prevention is worth a pound of cure.”

The best thing you can do to prevent kidney damage caused by heavy drinking is to detox from alcohol and either quit drinking entirely or drink only in moderation. Swapping hard liquor drinks for low-alcohol beer and wine can help you avoid drinking too much alcohol, as can making sure you stay adequately hydrated. Drink a glass of water for every alcoholic drink to help balance out the amount of alcohol consumed. If you do drink, be sure to drink responsibly, for the sake of your kidneys and your quality of life.

Pancreatin: Uses, Side Effects and Potential Drug Interactions

Pancreatin, a mixture of the digestive enzymes amylase, lipase, and protease, has a well-established history of use as a treatment for pancreatic insufficiency and other conditions that impact pancreatic function and fat digestion. It’s important to follow the dosing instructions provided by your doctor or on the product label to avoid side effects and unforeseen drug interactions.

Pancreatin, also called pancrelipase and pancreatic enzymes, is a mixture of digestive enzymes used to supplement the body’s natural supply of such enzymes. Under normal circumstances, the pancreas produces all the digestive enzymes necessary for breaking down fats, proteins, and carbohydrates from the food you eat. However, certain conditions—including cystic fibrosis, chronic pancreatitis, and pancreatic cancer—can impede the pancreas’s ability to carry out that vital function, resulting in malabsorption.

Here’s what you should know about what pancreatin is and how it works, the conditions it’s been shown to effectively treat, side effects associated with its use, and potential drug interactions.

What Is Pancreatin?

To prevent malabsorption and ensure full, efficient digestion, three essential enzymes are needed: amylase, lipase, and protease. Most pancreatin products are made using enzymes extracted from the pancreases of pigs—you may see these termed porcine pancreatic extract or porcine pancreatic enzymes. In some cases, the pancreatic enzymes come from the pancreases of cows—the key term to look for here is bovine.

The medical use of pancreatin dates back to the 1800s at least. It now appears on the World Health Organization (WHO)’s List of Essential Medicines, which evaluates the effectiveness, safety, and cost-effectiveness of various medicines, then determines which should be considered essential to health care systems around the globe. Pancreatin is currently available both by prescription and as a supplement—in 2019, more than one million prescriptions were written in the United States alone.

5 Questions About Pancreatin, Answered

4 Proven Uses for Pancreatin

Studies support the use of pancreatin for a number of medical conditions, all of which somehow affect either the pancreas or fat digestion.

1. Pancreatic Insufficiency

The most common use for pancreatin is to treat digestive problems related to disorders of the pancreas. This is sometimes referred to as pancreatic insufficiency.

According to an article published in BMC Medicine in 2017, the most common causes of pancreatic insufficiency are:

  • Chronic pancreatitis
  • Cystic fibrosis
  • History of extensive necrotizing acute pancreatitis
  • Pancreatitis (swelling of the pancreas)
  • Pancreas removal

Researchers have conclusively determined that taking pancreatin improves the absorption of fat and protein and raises energy levels.

Pancreatic enzyme treatments historically had varying levels of efficacy, but since the Food and Drug Administration (FDA) put regulations in place for all prescription formulations in 2010, they have become quite reliable. Studies show they can treat abdominal pain, malnutrition, steatorrhea (pale, oily, foul-smelling stools), and weight loss, and that they may even be able to improve an individual’s overall quality of life.

2. Nonalcoholic Fatty Liver Disease

Nonalcoholic fatty liver disease (NAFLD) is a condition characterized by the accumulation of fat in the livers of individuals who drink little or no alcohol. In some cases, this condition develops after individuals have the pancreas removed. Studies indicate that taking pancreatin may help to treat or prevent NAFLD in those individuals.

Findings published in the Journal of Hepato-Biliary-Pancreatic Sciences showed that treatment with pancreatin could significantly improve liver fat levels among patients who developed NAFLD after having their pancreases removed. Analysis also revealed improvements to liver function, digestion, and blood levels of proteins, albumin, and cholesterol.

3. HIV/AIDS

Individuals with HIV and AIDS sometimes have difficulty digesting fat. Preliminary findings indicate that taking pancreatin might improve fat digestion for those individuals.

According to a retrospective analysis published in HIV Medicine, 104 out of 233 patients showed signs of pancreatic insufficiency. Pancreatin proved to be an effective treatment for symptoms of pancreatic insufficiency, such as steatorrhea, in a majority of patients.

4. Pancreatic Cancer

Issues with digestion can occur for certain individuals with pancreatic cancer, resulting in unwanted weight loss. According to some studies, pancreatin can lead to beneficial weight gain for individuals with pancreatic cancer. Other studies, however, were unable to locate any evidence that pancreatin leads to weight gain, improved nutritional status, or increased rates of survival for pancreatic cancer patients.

These divergences may be because pancreatin only helps individuals with underlying pancreatic enzyme issues, which can be difficult to differentiate from the physiological manifestations of pancreatic cancer as well as the side effects of pancreatic cancer treatments.

The Pancreatic Cancer Action Network (PanCAN) recommends that patients experiencing signs of pancreatic insufficiency discuss the use of pancreatin with their medical team. Those symptoms include:

  • Indigestion
  • Stomach cramps after eating
  • Gas
  • Frequent, loose stools
  • Weight loss

Best Practices for Taking Pancreatin

When discussing the use of pancreatin with your doctor, be sure to disclose if you have allergies to pork proteins. If you have any other allergies, asthma, or gout, that’s also important information for your doctor to have.

The FDA has classified pancreatin in pregnancy category C, meaning it’s possible it may have an adverse effect on a fetus, but the potential benefits might outweigh the risks. Pregnant women should be sure to seek medical advice about possible side effects from a trusted source before taking pancreatin. Since it’s also possible pancreatin can pass into breast milk, nursing mothers should do the same.

General Dosing Recommendations

Be sure to follow the instructions given by your doctor or provided on the label for the pancreatin product you chose. If your doctor adjusts your dose, stick to that dosage and be sure to discuss any desired changes with your doctor rather than trying them out on your own.

That said, scientific research on the use of pancreatin can be used to extrapolate some general guidelines, which vary based on the targeted condition.

For pancreatic insufficiency, doses are measured in units of lipase—one of the enzymes in pancreatin that’s required for proper metabolism. A typical starting dose would be between 500 and 1,000 lipase units per kilogram (kg) of body weight, taken with each meal. The high end of the range would be 2,500 lipase units/kg at each meal. Amounts in excess of that should only be taken if a physician has deemed it medically necessary.

For NAFLD, the most studied option is a specific, delayed-release prescription pancreatic enzyme drug that’s sold in the United States under the brand name Creon. Research supports the use of a daily 1,800-milligram dose for a duration of 6-12 months.

Expert Tips to Minimize Side Effects and Maximize Results

Experts advise always taking pancreatin with food (either meal or snack will work), in part because doing so mimics the way the body naturally releases endogenous pancreatic enzymes. It’s advisable to drink an entire glass of water with your dose of pancreatin too.

Always take pancreatin tablets whole. Do not pulverize the tablets, break them into pieces, or chew them. Swallow each tablet promptly and avoid holding it in your mouth, as that may cause irritation to the sensitive tissues there.

Plan ahead to avoid running out of this important medication—call in for a prescription refill before you take your last dose. If you do miss a dose, take that dose as soon as you realize you missed one. If it’s nearly time to take your next dose, refrain from making up the dose missed previously. Never take a double dose.

If you’re using prescription pancreatin, keep in mind that changes to the brand, strength, or type may affect the dose you take. Be sure to speak with your doctor or pharmacist about any questions you have related to medication changes.

Pancreatin does not need to be refrigerated. It should be stored at room temperature in a cool, dry location.

Unless instructed to do so by your prescribing physician, do not take any other digestive enzymes while using pancreatin. You should also refrain from taking antacid medications both an hour before and an hour after each dose of pancreatin.

5 Expert Tips to Get the Most from Pancreatin

Watch for These Possible Side Effects of Pancreatin

The FDA has determined the oral use of pancreatin to be “likely safe” when supervised by a health care provider. That said, it can cause side effects.

Common side effects include:

  • Dizziness
  • Changes to blood sugar levels (both increases and decreases)
  • Stomach pain
  • Gas
  • Unusual bowel movements
  • Nausea
  • Minor skin rash

However, the FDA has categorized taking pancreatin in doses that exceed those prescribed by your doctor as possibly unsafe, in part because it appears doing so makes you more likely to develop a rare bowel disorder.

If you experience more severe side effects, you should contact your doctor immediately. Watch for:

  • Intense nausea
  • Vomiting
  • Joint pain and swelling
  • Pronounced changes to baseline symptoms

If you show signs of an allergic reaction, you should seek immediate medical help by calling 9-1-1 or going to the emergency department at the nearest hospital. Indicators of an allergic reaction include:

  • Labored breathing
  • Facial swelling
  • Swelling of the lips, tongue, or throat
  • Hives

What You Should Know About Pancreatin Side Effects

Be Aware of These Potential Drug Interactions

As is true of nearly every bioactive substance you ingest, it’s possible for pancreatin to interact with other prescription and over-the-counter medicines as well as vitamins, supplements, and herbal products. If you’re taking prescription pancreatin, be sure to discuss with your doctor all other medicines, vitamins, or supplements you currently take.

One drug that’s known to interact poorly with pancreatin is acarbose (sold under the brand names Precose and Prandase). This drug helps to treat type 2 diabetes by slowing the rate at which the body metabolizes food. Because pancreatin helps the body break food down more efficiently, it can decrease the efficacy of acarbose.

Conclusion

Pancreatin is a mixture of digestive enzymes—specifically, amylase, lipase, and protease. It has a well-established history of use as a treatment for pancreatic insufficiency, a condition that can be caused by cystic fibrosis, chronic pancreatitis, and pancreatic cancer, among other health disorders.

Studies show that taking pancreatin addresses symptoms of pancreatic insufficiency such as:

  • Abdominal pain
  • Malnutrition
  • Steatorrhea (pale, oily, foul-smelling stools)
  • Weight loss

By doing so, it can significantly improve an individual’s overall quality of life.

Pancreatin is available as prescription and over the counter. It’s important to follow the dosing instructions provided by your doctor or on the label of the product you chose. If you experience severe side effects, contact your health care practitioner immediately. If you show signs of an allergic reaction, seek emergency medical attention.

Because pancreatin can interact with other medications—prescription, over-the-counter, and herbal—it’s important to speak with a doctor to avoid unforeseen interactions.

Body Repair After Quitting Drinking: How to Naturally Promote Recovery from Alcohol

What is involved in body repair after quitting drinking, and what can you do to help support recovery and detox? Find out how to minimize withdrawal symptoms and recover better from excessive alcohol use. 

Whether alcohol use has reached the level of alcohol addiction, or regular heavy drinking has simply started to take its toll, quitting alcohol is one of the healthiest decisions anyone can make to improve health and quality of life. Drinking too much alcohol can have damaging physical, psychological, and interpersonal effects that could be disastrous or even fatal, but alcohol recovery isn’t easy either. If you or a loved one has decided to be alcohol-free, the question now is how to speed up body repair after quitting drinking? How long does it take to detox from the effects of alcohol, and what can you do to minimize withdrawal symptoms and improve the body’s health? Read on for natural solutions.

The Symptoms of Alcohol Withdrawal

Depending on your personal level of alcohol dependence, withdrawal symptoms could be mild or severe. In the worst case scenarios, alcohol withdrawal syndrome can include:

  • Anxiety
  • Nausea
  • Tremors
  • Headache
  • Vomiting
  • Rapid heart rate
  • Irritability
  • Confusion
  • Sweating
  • Elevated blood pressure
  • Insomnia
  • Nightmares
  • Fever
  • Seizures
  • Extreme agitation and confusion
  • Visual, auditory, and/or tactile hallucinations

These symptoms could start occurring as soon as 6 hours after your last drink and potentially last for weeks. The severest symptoms are part of delirium tremens (DT), the most dangerous level of alcohol withdrawal that should be undergone only in a hospital or rehab setting as part of a substance abuse recovery process.

The National Institute on Alcohol Abuse and Alcoholism has an online questionnaire to help you evaluate your level of alcohol use and better decide your body’s ability to quit “cold turkey” or with the aid of a treatment center. This post-acute withdrawal phase is often the hardest part, and the more recovery resources you have, the better your chances of maintaining sobriety and not relapsing the next day because the withdrawal symptoms are too overwhelming.

The Symptoms of Alcohol Withdrawal

Body Repair After Quitting Drinking: How To Minimize Withdrawal Symptoms and Recover Faster

What happens to your body when you stop drinking? Is it just one endless hangover? Will the damage done to the stomach lining, kidneys, and liver eventually reverse? Here are the areas you may notice the most dramatic side effects and recovery benefits, and how you can support your recovery after you’re done drinking alcohol.

1. Repair Skin Damage

The cartoon image of a drunk is someone hiccuping bubbles and sporting rosy cheeks and a big, red nose. Part of that picture is actually true: regular overconsumption of alcohol damages your skin, making you look older and causing tissue inflammation. There are a few reasons for this.

  • Dehydration: Because it’s a diuretic, alcohol dehydrates your skin, leading to less elastic skin that can become dry, flaky, and painful.
  • Inflammation: The facial flush that occurs when you drink isn’t the rosy glow of healthy skin but an inflammatory reaction to poison, almost like a mild allergic rash. While that inflammation will subside when you sober up, repeated inflammation to the area will damage the skin over time and leave a lasting redness. It’s also been associated with a higher risk of cancer.
  • Aging: New research indicates drinking alcohol prematurely ages your cells, including your skin cells, causing visual signs of premature aging.

Alcohol has long been associated with bad skin, including what was once known as a “drinker’s nose” or rhinophyma. Rhinophyma is not directly linked to alcohol as a cause and is in fact a form of rosacea. However, there is research showing that there’s a high prevalence of alcohol use among patients with inflammatory skin diseases, and a possible increased risk of basal cell carcinoma linked to alcohol consumption.

The conclusion: alcohol use causes skin damage and premature aging, may worsen other skin conditions, and could increase the risk of skin cancer.

The Solution

Once you quit drinking, what does your skin need most to recover? The first step is adequate, regular hydration, and perhaps a daily moisturizing facial lotion with SPF to protect against sun damage. The second step is to make sure your body has the proper supplies to regenerate new skin and tissue cells, which means amino acids for skin tightening, especially the collagen amino acids that can restore supple, youthful skin. Whether you get them from diet or supplementation, you can’t repair or regenerate new tissue without the necessary amino acids.

2. Reduce Risk of Heart Attack

Excessive alcohol consumption has a serious impact on your cardiovascular health, increasing your risk of pulmonary (lung) conditions and heart disease. Heart failure affects up to five million Americans, and the risk of heart failure is nearly doubled for those who drink heavily.

In the previously linked systematic review of studies, the risk of alcohol abuse was found to be so dangerous, the researchers’ conclusion stated that although “the current literature provides some evidence for a lower risk of heart failure with light-to-moderate consumption of alcohol […] it would be premature to recommend light-to-moderate drinking as a means to lower the risk of heart failure, given the possible risk of abuse and resulting consequences.”

For all the articles that get passed around about the benefits of drinking red wine for heart health, the risk of over-consuming alcohol is so much greater than the small amount of potential benefit from moderate consumption that it is not recommended.

The conclusion: by quitting alcohol entirely, you significantly reduce your risk for heart disease, heart attack, heart failure, and other cardiovascular and pulmonary conditions.

The Solution

According to the American Heart Association, alcohol use and abuse endangers the heart by increasing the amount of fat (triglycerides) in our bloodstreams. Once you’ve quit drinking, there are natural ways to help lower cholesterol and blood lipid levels, and aid in your body’s clean-up of these substances.

3. Reverse Liver Damage

Our livers are unique organs, able to heal from damage in ways that our hearts (for example) cannot. Because alcohol is an intoxicant, it’s up to our livers to process it in order to detox the body, which is why liver disease is a dangerous risk of chronic alcohol abuse.

Consuming large amounts of alcohol can lead to fatty liver disease, alcoholic hepatitis, cirrhosis of the liver, and ultimately liver failure and death. At a certain point the scarring on the liver is so advanced it is irreversible, but there is a large and vitally important window of time when, if you can quit drinking, you can stop the damage in its tracks and allow the liver to heal completely.

The conclusion: alcohol damages the liver, but abstaining can stop the damage and possibly allow it to be reversed.

The Solution

Once alcohol is out of your system, you can help the liver detox and repair itself in a few simple ways: by consuming a liver-flush diet, knowing which key vitamins, supplements, and amino acids aid in liver support, and avoiding intoxicants like alcohol, unnecessary drugs, or exposure to industrial chemicals and preventable diseases like hepatitis. Your liver and kidneys are the only truly natural detoxifiers you have, and in a heavy drinker they are often fatally overtaxed. By quitting alcohol, you can cure your detox organs.

4. Lose Weight and Improve Body Composition

Alcohol leads to higher fat levels in the blood, and therefore alcohol consumption is also associated with higher body weight gain, obesity, and the symptoms that can accompany excess weight like type 2 diabetes, high blood pressure, and metabolic syndrome. Alcohol itself contributes to high calorie consumption, but the calories in alcohol are empty, with no nutritional benefit. Alcohol is processed and stored just like sugar, and like a diet high in refined sugar, it’s closely associated with dangerous weight gain and obesity.

While there’s no direct correlation between the amount of alcohol consumed and the amount of weight gained due to each of us having our own individual metabolism rates, it’s nevertheless true that reducing or eliminating alcohol intake helps lead to successful weight loss and long-term weight-loss management in those with diabetes, as well as avoiding weight gain in the first place.

The conclusion: alcohol can contribute to weight gain and obesity, while abstaining can aid in weight loss.

The Solution

Once you’re sober, proper diet and exercise are still the first and foremost ways to safely lose weight and maintain a healthy body composition. You’ll also want to control for hunger cravings, especially if alcohol addiction is at play. Eating can be an addiction much like drinking, the main difference being that you have to eat every day, while those who are addicted to other substances can remove the temptation entirely. By eating nutritionally dense and filling meals full of the protein and amino acids necessary to build muscle and lose weight, you can avoid the dangers of obesity and regain your optimal fitness.

5. Support Energy and Sleep

Energy levels and proper rest are two sides of the same coin. Because alcohol acts like sugar in the body, the comedown from sobering up can lead to fatigue and energy crashes not unlike drops in blood sugar. This encourages people to overeat or return to drinking despite their best intentions to quit—it’s an effort to correct that crash and regain the rush.

On the flip side, because alcohol also interrupts the brain activity associated with rest, memory creation, and waking, it disrupts normal sleep patterns. Just as so-called “blackout drunks” can be manically active and then wake up with no memory of what they did or said, even more moderate drinkers will experience poor sleep quality due to conflicting brain activities that prevent them from entering into deep REM sleep.

The conclusion: While drinking, you sleep without getting the benefits of “dream sleep” and the neurological function it provides. When newly sober, one of the most maddening side effects can be sometimes long-lasting insomnia that further depletes already low energy levels.

The Solution

While there are sleep aids you can take to chemically induce sleep, they are not recommended for those whose sleep issues are due to coming down from a chemical alcohol dependence in the first place. There are certain natural nutrients and amino acids for insomnia you can explore, pre-bed rituals you can adopt to retrain your brain for regular sleep, and even more amino acids to help boost your daily energy as your body recalibrates to a non-toxic state.

The Amazing Attributes of Abstinence

Now you have an idea of what the body must go through to repair itself once you quit drinking, plus the various ways you can support a natural recovery. Keep in mind that alcohol’s effects don’t stop at damage to your body, and thus quitting drinking can improve even more aspects of your life: alcohol detox and abstinence can save you money, can save your relationships from the consequences of binge drinking, and can help save your overall emotional and mental health going forward.

Get the Facts About Hyperlipidemia: 4 Crucial Questions, Answered

Hyperlipidemia (high cholesterol) can stem from genetic causes, but the majority of the time, it results from lifestyle choices and environmental factors. As it causes no symptoms itself, it’s vital that health care practitioners routinely screen for this silent condition. Lifestyle changes involving diet and physical activity form part of any successful hyperlipidemia treatment plan, and the use of proven supplements can be a highly effective complementary treatment.

More frequently referred to as high cholesterol, hyperlipidemia is the medical term used to describe unusually elevated blood levels of lipids (fat molecules). Though it’s possible to inherit hyperlipidemia, most cases can be traced back to lifestyle choices and environmental factors. Hyperlipidemia itself causes no symptoms, but it does adversely impact your health—most notably by increasing your risk of developing coronary artery disease.

Read on to learn how hyperlipidemia develops, 14 risk factors for hyperlipidemia, how doctors diagnose hyperlipidemia (as well as the different types), and natural treatments for hyperlipidemia.

1. How Does Hyperlipidemia Develop?

To understand how high cholesterol develops, you must first have a basic grasp of some essential facts about cholesterol itself. Cholesterol, a type of fat made in the liver, makes vital contributions to the functioning of the human brain, development of membranes surrounding cells, production of hormones, and storage of vitamins.

In order to travel through the bloodstream, cholesterol pairs with proteins to form lipoproteins. There are two forms of lipoproteins—high-density lipoproteins (HDL) and low-density lipoproteins (LDL)—each of which carry out different functions.

  • Low-density lipoproteins (LDL): Because LDL cholesterol has been linked to the development of cardiovascular disease, it’s known as “bad cholesterol.” LDL cholesterol moves cholesterol molecules through your arteries, and when levels get too high, fatty deposits begin to build up on the walls of your arteries. This leads to atherosclerosis, the hardening or narrowing of the arteries, which in turn raises your risk of heart disease.
  • High-density lipoproteins (HDL): HDL cholesterol, or “good cholesterol,” can actually counterbalance the negative effects of LDL cholesterol. That’s because HDL transports unused cholesterol molecules back to the liver, where they can be excreted. This prevents the development of high blood cholesterol levels and the associated adverse health outcomes, such as heart attack and coronary heart disease.

If your doctor elects to perform a lipid profile, they will likely measure your triglyceride levels too. Your body stores any calories not required for immediate energy needs in the form of triglycerides. Regularly consuming more calories than necessary to fuel your body, particularly if you consume a diet high in carbohydrates, is likely to result in high triglyceride levels (technically speaking, hypertriglyceridemia).

High cholesterol levels in the blood, as touched on in our discussion of LDL cholesterol, causes deposits of fat to accumulate in the blood vessels. As these deposits grow, they can restrict blood flow through the arteries. If a deposit spontaneously breaks loose, it can create a clot that triggers a heart attack or stroke.

This makes it important to monitor and manage your cholesterol levels. For HDL cholesterol, this means keeping your levels at or above a certain threshold while for LDL cholesterol, it means making sure they do not rise too high. Optimal levels for total, HDL, and LDL cholesterol as well as triglycerides are impacted by whether or not you have heart disease, diabetes, or other conditions that put you at higher risk of developing high cholesterol.

The guidelines for each category are as follows:

  • Overall cholesterol
    • Optimal: Under 200 milligrams per deciliter (mg/dL)
    • Concerning: 200-239 mg/dL
    • High: 240 mg/dL and higher
  • HDL cholesterol
    • Optimal: 60 mg/dL and higher
    • Adequate: 50-59 mg/dL for women and 40-59 mg/dL for men
    • Low: Under 50 mg/dL for women and 40 mg/dL for men
  • LDL cholesterol:
    • Optimal for those with heart disease or diabetes: Under 70 mg/dL
    • Optimal for those at risk of heart disease: Under 100 mg/dL
    • Adequate for those with no heart disease, concerning for those with heart disease: 100-129 mg/dL
    • Concerning for those with no heart disease, high for those with heart disease: 120-159 mg/dL
    • High for those with no heart disease, very high for those with heart disease: 160-189 mg/dL
    • Very high: 190 mg/dL and higher
  • Triglycerides:
    • Optimal: Under 150 mg/dL
    • Concerning: 150-199 mg/dL
    • High: 200-499 mg/dL
    • Very high: 500 mg/dL and higher

Making Sense of Your Cholesterol Levels

2. What Factors Raise Your Risk of Hyperlipidemia?

As we covered in the last section, hyperlipidemia results from an unbalanced ratio of LDL cholesterol to HDL cholesterol. While certain types of hyperlipidemia have a genetic component (meaning it’s important for you to know if you have a family history of hyperlipidemia), most result from lifestyle choices.

According to a study published in 2017, both age and sex influence a person’s likelihood of developing high levels of LDL cholesterol or triglycerides. The cross-sectional study, which enrolled 2,000 individuals, also found correlations between hyperlipidemia and lifestyle choices such as smoking, physical inactivity, and the consumption of fatty meats. Meanwhile, individuals who ate more fruits and vegetables were less likely to develop high cholesterol.

Research points to other risk factors as well, such as having a large waist circumference and consuming excessive quantities of alcohol. There are also links between elevated cholesterol levels and several health conditions, such as: kidney disease, polycystic ovary syndrome (PCOS), and decreased thyroid activity. Certain medications affect cholesterol levels too, like steroids, progestin, retinoids, diuretics, and in some cases, beta blockers.

Other factors shown to raise your risk of developing hyperlipidemia include:

  • Sedentary lifestyle: Failing to engage in physical activity on a routine basis can skew your cholesterol levels. It appears that exercise increases production of HDL cholesterol and increases the size of LDL cholesterol molecules, rendering them less harmful.
  • Use of tobacco products: Scientists have observed that smoking cigarettes injures blood vessel walls, which increases the odds that fat will build up on them. Smoking also appears to adversely impact HDL cholesterol levels.
  • Consumption of saturated and trans fats: Studies show that regularly eating foods that contain saturated fats (for instance, fatty meats) and trans fats (commonly included in processed foods like crackers, microwave popcorn, cookies, and more), leads to higher cholesterol levels.
  • Blood sugar levels: Analysis reveals a connection between high blood sugar and high levels of very-low-density lipoprotein (VLDL), a particularly unhealthy type of cholesterol, as well as lower levels of HDL cholesterol.
  • Body fat percentage: Researchers have also found a link between how much body fat a person has and their likelihood of having hyperlipidemia.
  • Overall physiology: As you age, your liver becomes less effective at removing LDL cholesterol, making you more likely to develop hyperlipidemia.

14 Hyperlipidemia Risk Factors

3. How Do Doctors Diagnose Hyperlipidemia?

Hyperlipidemia itself causes no noticeable symptoms, which is why it’s important for doctors to routinely check cholesterol levels, particularly for individuals who have a higher risk of developing the condition.

They do this, as touched on previously, with a test called a lipid panel. This simple blood test allows doctors to measure your total cholesterol, LDL cholesterol, HDL cholesterol, and triglycerides. In order to ensure accurate results, your physician may ask that you fast for between 8 and 12 hours leading up to the blood draw.

However, recent research trends toward a consensus that fasting may not be necessary. According to a study published in JAMA Internal Medicine in 2019, fasting prior to a lipid profile produced negligible differences to total, LDL, and HDL cholesterol levels. Triglyceride levels were consistently slightly higher for participants who did not fast.

The study enrolled close to 8,300 participants, all of whom had documented cardiovascular risk. Each participant had fasting and nonfasting lipid profiles done with a minimum of 1 month’s time in between the tests. The fasting protocol used required them to abstain from eating or drinking anything except water for 8 hours before the test. By following participants for a median of 3 years, the authors were able to determine that whether or not individuals fasted prior to the lipid profile did little to impact doctors’ ability to predict their risk of future health problems. This is exciting news not only because just about everyone dreads fasting, but more significantly, because fasting can cause issues for older individuals as well as those with diabetes.

5 Different Types of Hyperlipidemia

Experts have categorized the different types of hyperlipidemia that have a genetic component based on the different fats involved in each as well as how each affects the body.

  1. Type I, hyperlipidemia familial lipoprotein lipase deficiency: This inherited condition interferes with the mechanisms by which the body breaks down fats. It can cause abdominal pain, chronic pancreatic infections, and swelling of the liver and the spleen. It’s one of the more severe types of hyperlipidemia, and tends to develop during childhood.
  2. Type IIa, familial hypercholesterolemia, and type IIb, familial combined hyperlipidemia: Both type IIa and type IIb lead to elevated levels of LDL cholesterol. As the names of these types indicate, they do have a genetic component. They’re also one of the few types that can cause visible symptoms—specifically, deposits of fat under the skin and near the eyes. Both types put individuals at increased risk of heart problems.
  3. Type III, familial dysbetalipoproteinemia: This type involves increased total cholesterol and triglyceride levels in combination with decreased HDL levels. It, too, can cause visible symptoms—orange or yellow discoloration of the palms and the development of yellowish deposits of lipids in the skin over the elbows and knees. This type also raises your risk of cardiovascular disease.
  4. Type IV, familial hypertriglyceridemia: This type is differentiated from the others by the fact that it involves elevated levels of triglycerides, not cholesterol. It has been linked to obesity, high blood glucose, and high insulin levels. Typically, this condition remains unnoticed until early adulthood.
  5. Type V, mixed familial hyperlipoproteinemia: This type is quite similar to type I, but it also involves elevated levels of VLDL cholesterol. It’s quite common among patients diagnosed with metabolic syndrome.

Hyperlipidemia without a genetic component, also known as acquired hyperlipidemia, tends to mimic the forms described above.

4. Are There Natural Treatments for Hyperlipidemia?

There are a variety of prescription drugs on the market that can decrease cholesterol and triglyceride levels, such as:

  • Statins
  • Bile-acid-bindingresins
  • Cholesterol absorption inhibitors
  • Fibrates
  • Niacin

While these drugs do effectively treat hyperlipidemia, they can cause seriously unpleasant side effects. Statins, the first option most doctors will try, have been known to cause muscle aches, digestive upset and mental cloudiness. In rare cases, they can also cause liver damage and rhabdomyolysis, a serious condition that results in intense muscle pain, liver damage, and if left untreated, kidney failure and death.

Depending on which type of hyperlipidemia you have, as well as the results of your lipid profile, it’s possible that lifestyle changes and natural cholesterol treatments will allow you to avoid the use of potentially harmful prescription drugs. And even if a drug is necessary to manage your risk of more serious health problems like a heart attack or stroke, lifestyle shifts will still be an important part of your overall treatment plan.

Here are five lifestyle changes and natural treatments that can bring your cholesterol and triglyceride levels into the healthy range.

1. Develop a Healthy Diet

There’s no one right way to eat, but there are certain science-backed elements you can use to build a healthy diet that works for you.

When it comes to lowering bad cholesterol levels and raising good ones, the fats you eat make a big difference. Saturated fats found in red meat, bacon, and sausage and trans fats found in fried and processed foods are particularly problematic. Omega-3 fatty acids, on the other hand, have a wealth of heart-health benefits. Fatty cold-water fish like salmon and mackerel contain plenty of these good fats, as do walnuts and flaxseeds.

It’s also important to consume plenty of soluble fiber, which has been shown to lower LDL cholesterol levels. Load up on fiber-rich vegetables and fruits, legumes, and oats.

2. Engage in Physical Activity

Researchers have found that your physical activity levels have a pronounced impact on your HDL cholesterol levels. The more you exercise, the better those levels will be. And the less you exercise, the lower they’ll drop.

It appears that for cholesterol-management purposes, you should shoot for 40 minutes of moderate to vigorous exercise on 3 or 4 days of the week. Aim for a minimum of 150 minutes of exercise total per week.

If you have the time necessary to try swimming laps at the pool or joining a game of pick-up basketball, that’s wonderful. But finding ways to incorporate exercise into your daily routine, like biking to work or picking up the pace when you take your dog for a walk, can also help you hit that physical activity threshold.

3. Stop Smoking

As mentioned earlier, smoking causes HDL cholesterol levels to fall and triglyceride levels to rise. Furthermore, it independently increases your risk of developing heart disease. If you’re a current smoker, no matter which type of high cholesterol you have, quitting will be an important part of your treatment plan.

As you’re almost certainly aware, it can be quite a challenge to quit. It may be helpful to talk to your doctor about strategies for doing so, like using a nicotine patch, or to seek support from others who have successfully kicked the habit.

4. Evaluate Your Weight

There can be a connection between body weight (particularly fat mass) and cholesterol levels. Research has shown that by adopting dietary strategies designed to produce sustainable weight loss, individuals were able to raise their HDL cholesterol levels and lower their LDL cholesterol levels.

Learn more about strategies for pursuing healthy weight loss here.

5. Incorporate Proven Supplements

If you’re committed to pursuing natural methods of lowering your cholesterol, you can find more in-depth advice about proven methods for doing so, as well as the rationale behind choosing a natural approach, in this article.

For our purposes, it will suffice to say that supplements can play a very important role in naturally addressing hyperlipidemia.

For instance, compelling research has revealed that taking an essential amino acid supplement can produce highly desirable results on cholesterol levels.

Studies have shown that essential amino acids, which stimulate the synthesis of the proteins that transport lipids out of the liver as well as those that flush fatty acids into safe storage areas, can lower levels of total cholesterol, LDL cholesterol, VLDL cholesterol, and triglycerides in the liver as well as the bloodstream. These results have been seen with a dosage schedule of two 11-gram doses, twice a day.

These all-natural, completely safe compounds bring benefits for your overall health and—it’s important to note—they can be combined with statins without any ill effects. In fact, they actually make them more effective, per the findings of an Italian research team.

If you’re curious about amino acid supplementation, this primer is a great place to begin.

5 Natural Ways to Address Hyperlipidemia

Conclusion

Hyperlipidemia is the medical term for high blood levels of lipids. It can stem from genetic causes, but the majority of the time, it results from behavior choices and environmental factors such as an overly sedentary lifestyle, the use of tobacco products, or excessive alcohol consumption.

As it causes no symptoms itself, it’s vital that health care practitioners routinely screen for this silent condition, which has been linked to an increased risk of cardiovascular disease.

There are a variety of prescription medications available that can be used to get cholesterol levels under control, but they can cause unpleasant side effects. And even if the benefits of using one of those drugs outweighs the risks, it’s still important to make lifestyle changes such as developing a healthy diet that facilitates lower levels of LDL cholesterol and higher levels of HDL cholesterol as well increasing physical activity. It can also be quite valuable to incorporate supplements with proven benefits for bringing cholesterol levels into a healthy range, such as essential amino acids.

Recognizing Cachexia: Unintended Weight Loss, Falling Energy Levels, Temporal Wasting and Other Signs to Look For

Treating cachexia, a frequently irreversible side effect of many major illnesses, requires a separate, multilevel approach. This is, in part, because diagnosing it can be quite tricky, as symptoms such as temporal wasting overlap with those of the underlying conditions. In addition to lifestyle-related shifts such as eating small, frequent meals, supplementing with amino acids has been shown to slow the rate of muscle mass loss as well as the fatigue caused by cachexia.

One way to think about cachexia is as the last illness. This metabolic disorder causes muscle wasting and involuntary, extreme weight loss, as well as temporal wasting. Cachexia occurs in the final states of almost every serious disease, including cancer, heart disease, HIV, and multiple sclerosis.

According to experts, approximately 9 million people around the world have cachexia. A 2016 estimate placed the number of cachexia diagnoses among individuals admitted to hospitals in the United States at 160,000 per year. Despite the staggering number of individuals affected by cachexia, doctors have historically focused on treating the underlying disease, rather than cachexia itself.

However, as we entered the twenty-tens, scientists began to examine cachexia as not just a symptom, but a condition that could itself be treated. Early studies showed that inflammation and metabolic imbalances drive cachexia, pointing the way to potential treatment approaches.

One of the challenges in treating cachexia is that it can be challenging to diagnose, particularly in the early stages when interventions are most likely to result in increased quality of life.

In this article, we’ll cover what causes cachexia, how to recognize temporal wasting and other symptoms of cachexia, and available treatments for cachexia such as targeted amino acid supplementation.

What Causes Cachexia?

Cachexia is a complex condition with no single cause. The term comes from the Greek words “kakos,” meaning bad, and “hexis,” meaning condition—and indeed, those with cachexia are in overall bad condition. This makes it challenging not only to tease out the factors that cause cachexia, but also to define the condition clinically. Though Hippocrates is widely acknowledged as the first to describe cachexia, a formal medical definition—which includes the loss of 5% or more of a person’s bodyweight over the course of a year as well as declining muscle strength—was not developed until 2006.

Scientists do know that in addition to altered levels of key bioactive substances, a primary force behind the development of cachexia is increased muscle protein breakdown which, in conjunction with decreased muscle protein synthesis, results in muscle atrophy, or muscle loss.

Other processes known to contribute to cachexia include systemic inflammation and elevated energy expenditure.

A number of factors contribute to cachexia, including the levels of these substances, the conditions that cause them, and the reaction they provoke from the body.

Who’s at Risk of Developing Cachexia?

As touched on in the introduction, cachexia commonly develops during the last stages of serious diseases. That means individuals with the following conditions are all at risk of developing cachexia as their diseases progress:

If you or a loved one has one of the conditions listed above, consider having a conversation with your doctor about preventative steps you can take to avoid cachexia and safeguard your quality of life.

9 Conditions That Put You at Risk of Developing Cachexia

Recognizing Temporal Wasting, Unintended Weight Loss, and Other Symptoms of Cachexia

Many of the symptoms of cachexia overlap with the symptoms of other conditions, including the very conditions that cause cachexia to develop. This can make it difficult to differentiate between true cachexia and other issues.

Some telltale indicators of cachexia include:

  • Muscle wasting: The core symptom of cachexia is muscle wasting. It’s important to note, however, that particularly in the early stages, individuals may be experiencing ongoing muscle loss without visibly appearing malnourished. In individuals who are overweight, this can make it even more unlikely that doctors will spot cachexia.
  • Unintentional weight loss: This refers to weight loss without conscious intent, and with the consumption of an adequate number of calories to maintain body weight or even a high enough caloric intake to result in weight gain under normal circumstances.
  • Loss of appetite: Known clinically as anorexia (and not to be confused with anorexia as an eating disorder), the loss of appetite experienced by those with cachexia is pronounced and consistent. They cease to find food appealing and lose the desire to eat it.
  • Decreased functional ability: Cachexia often results in fatigue, low energy levels, and malaise, which can make it difficult for a person to carry out daily activities. They may find even simple tasks such as brushing their teeth to be exhausting.
  • Edema: Cachexia causes protein levels in the blood to decrease, which in turn causes excess fluid to accumulate in the tissues of the body. As it builds up, it causes swelling.
  • Temporal wasting: The wasting of the temporal muscles and subcutaneous fat in the temporal region occurs with serious nutritional deficiencies and severe catabolism (meaning when muscle protein breakdown massively outpaces muscle protein synthesis).

6 Symptoms of Cachexia

Why Is It Challenging to Diagnose Cachexia?

Many of the symptoms of cachexia overlap with the symptoms of other conditions, including the very conditions that cause cachexia to develop. This can make it difficult to differentiate between true cachexia and other issues.

To further complicate matters, doctors don’t agree on the threshold at which muscle wasting becomes extensive enough to be considered cachexia. The definition of cachexia settled upon in 2008—”a complex metabolic syndrome associated with underlying illness and characterized by loss of muscle with or without loss of fat mass”—largely hinges on presence of muscle loss either in the absence of, or that outpaces, fat loss.

Even mild muscle loss, which commonly accompanies the aging process, produces some feelings of increased weakness and fatigue. It can also make it more difficult for individuals to carry out the activities of daily life.

Most experts concur that the best approach for determining when muscle wasting has become significant enough to constitute cachexia involves quantifying:

  • Loss of muscle mass
  • Change to muscle strength
  • Degree of decrease to muscle tone

In the early 2010s, some researchers proposed that imaging techniques like MRI (magnetic resonance imaging) could be valuable tools for diagnosing cachexia.

At this time, doctors continue to use a variety of criteria for diagnosing cachexia. The most common lists the following diagnostic points:

  • Inadvertent loss of over 5% of overall body weight in a span of 6 to 12 months
  • Body mass index (BMI) of under 20 for individuals younger than 65 and under 22 for individuals age 65 and older
  • Less than 10% of body mass accounted for by body fat

The Importance of Early Recognition

Because loss of muscle strength and muscle mass often occur slowly and in tandem with chronic diseases and/or the aging process, cachexia diagnoses tend to happen once widespread muscle wasting has transpired. This eliminates the best window of opportunity for halting the progression of cachexia and securing an improved long-term quality of life.

Unfortunately, the patients under the closest medical observation often fare the worst, as hospitalization can instigate or exacerbate malnourishment, which in turn furthers the progression of cachexia. When a patient’s nutrient intake declines, longer hospital stays and worse outcomes tend to follow.

Conventional medical treatment plans are not designed to encourage the recognition of early signs of muscle wasting. The more pronounced the wasting becomes, the lower the efficacy rate for interventions.

In an effort to combat this, researchers developed guidelines for a condition termed “pre-cachexia,” which are as follows:

  • Presence of an underlying chronic disease
  • Unintentional weight loss less than or equal to 5% of typical body weight during the last 6 months
  • Systemic inflammation
  • Loss of appetite and related symptoms

Hopefully, the establishment of these guidelines will lead to greater recognition of early signs of muscle wasting. Even minor changes to body mass or appetite among those with chronic diseases can be indicators that something has gone awry, and should, therefore, be taken seriously. The sooner these symptoms are noted and addressed, the better the treatment results will be.

Diagnostic Criteria for Pre-Cachexia and Cachexia

Complications Associated with Cachexia

As cachexia progresses, it can seriously impact a person’s overall health. Muscle wasting, in particular, can significantly decrease longevity. According to a 2017 study, cachexia correlates strongly with survival and has been found to contribute to 20% of cancer fatalities.

In general, complications associated with cachexia include:

  • Impaired quality of life
  • Inability to live independently
  • Compromised immunity
  • Exacerbated symptoms of underlying disease
  • Shortened lifespan

How to Treat Cachexia

Because so many separate factors coalesce to cause cachexia, treatment typically involves multiple types of therapy. While it can be tempting to believe that simply encouraging a person to eat more, or to change the foods they eat, will halt the loss of body mass caused by cachexia, that will not produce the desired results.

According to doctors, dietitians, and other experts, the following steps can be valuable parts of a cachexia treatment plan.

  • Adopt an eating approach centered on small, frequent meals. While an increased caloric intake alone will not cure cachexia, it’s vital that individuals with cachexia consume as many nutrient-dense calories as they can tolerate. Most find it preferable to eat small portions of high-calorie meals throughout the day rather than three larger meals. It can also be helpful to add nutritional supplement drinks as between-meal snacks.
  • Emphasize the social elements of eating. Even if eating itself holds little attraction, individuals with cachexia can still draw enjoyment from gathering together to eat a meal. Encouraging a person with cachexia to focus on mealtime socialization can help recalibrate the relationship to food.
  • Educate the emotional support system. As cachexia and the underlying diseases associated with it progress, patients may entirely lose the desire to eat. This can be upsetting for family and friends, who may feel strong urges to compel them to eat. It’s important to understand that eating will not halt muscle wasting and weight loss. When patients reach this stage, prioritize their overall quality of life rather than caloric intake.
  • Try appetite stimulant medications. Certain drugs—for example, dronabinol, megestrol, and glucocorticoids—can stimulate the appetite. Again, keep in mind that eating more will not change the progression of the disease. However, it can be beneficial in that patients feel more integrated into familial and social interactions, which in turn improves mental health.
  • Engage in light exercise. If a person has the energy to do so, some believe that light exercise can help build muscle mass. That said, this hypothesis has yet to be fully substantiated.

Incorporating Amino Acids into a Cachexia Treatment Plan

Researchers have found that certain nutritional interventions can help to both treat and prevent muscle wasting. Given the paramount importance of amino acids for muscle growth, it should come as no surprise that strong evidence indicates that whey protein, as well as glutamine, arginine, and leucine, can help individuals with cachexia maintain and even increase their muscle mass.

Studies support the use of whey protein to build muscle. Whey, considered to have one of the best amino acid profiles of any natural protein, provides a wealth of amino acids that play active roles in muscle synthesis, including all three branched-chain amino acids (BCAAs): leucine, isoleucine, and valine. Multiple studies have shown that supplementing with whey protein can result in increased protein synthesis. Furthermore, the increases associated with the use of whey protein are greater than those linked to the use of casein or soy. That said, it’s not uncommon for these studies to have participants enroll in an exercise program, making it somewhat unclear whether the muscle mass increases stem from the whey protein, the exercise program, or the combination of the two.

Interestingly, carnitine, an amino acid derivative, can not only stimulate muscle protein synthesis but also increase energy production, thereby alleviating the ill effects of cachexia on two levels. Several studies have found that cancer patients with cachexia tend to have low levels of carnitine, and that supplementing with 2 to 6 grams of carnitine can help reduce fatigue and increase lean body mass.

A 2006 study conducted by an Italian research team found that taking 2 grams of L-carnitine 3 times each day for a month led to an average muscle mass gain of 4.4 pounds, significantly decreased fatigue, and markedly improved quality of life. Other studies done with cancer patients also found that supplementing with carnitine led to increased muscle mass and decreased fatigue.

As you may be aware, amino acids work in concert to orchestrate myriad essential physiological functions, including protein synthesis. Thus, while certain amino acids have been shown to be uniquely beneficial for the treatment of cachexia, it appears that supplementing with well-balanced blends of multiple amino acids produces better results than supplementing with a single amino acid.

For instance, the use of leucine in combination with glutamine and arginine can bring about lean muscle mass gains in individuals with muscle wasting. A study published in The Journal of Parenteral and Enteral Nutrition showed that a mixture of leucine, glutamine, and arginine given in two divided doses each day led to an average weight gain of 5.6 pounds of lean muscle mass compared to an average weight loss of 1.5 pounds of lean mass for those taking the placebo. Study participants, all of whom had HIV and documented weight loss of at least 5% of body mass over the previous 3 months, were randomly assigned to receive the amino acid mixture or the placebo. The study authors tracked their body weights, lean body mass, and fat mass using air displacement plethysmography and computerized tomography (CT). After 8 weeks, the researchers found that supplementing with the amino acid blend could “markedly alter the course of lean tissue loss” as well as improve immune status.

Studies done with cancer patients and other populations found similar results in terms of muscle mass gains.

How to Treat Cachexia

Research supports the idea that the use of amino acids to treat cachexia should include a well-formulated blend of essential amino acids. This ensures the body has all the raw materials necessary to carry out muscle protein synthesis at the highest rate possible. Only a small amount of amino acids—say, a 3-gram dose—is needed to bring about this effect.

Conclusion

Cachexia, a frequently irreversible side effect of many major illnesses, causes severe muscle wasting. The accompanying rapid loss of muscle mass can undermine a person’s overall health and even shorten their lifespan. Diagnosing cachexia is quite tricky, as symptoms such as temporal wasting overlap with those of the underlying conditions associated with it. Furthermore, it often accompanies the end stage of those diseases.

Cachexia is complex condition, and though it is intimately intertwined with the progression of the underlying disease, treating it requires a separate, multilevel approach. In addition to lifestyle-related shifts such as eating small, frequent meals, supplementing with amino acids has been shown to slow the rate of muscle mass loss as well as the fatigue caused by cachexia.

How to Lengthen Telomeres—and Why You Should

Shortening of telomeres plays a vital role in cellular division and the aging process, which has led to intense interest in how to lengthen telomeres. Research indicates that both telomerase therapy and RNA treatments could possibly be effective interventions, however, it will likely be some time before those treatments become available to the public. In the meantime, a new study points to amino acids as a possible method for enhancing the health of your telomeres. 

“Telomeres”—have you encountered that term yet? It seems that interest in telomere length and how to lengthen telomeres is reaching somewhat of a fever pitch.

Researchers describe telomeres as the cellular equivalent of the plastic tips placed on the ends of shoelaces to prevent fraying. The material telomeres keep intact, however, is your DNA.

When a cell divides and replicates, the replication does not include the full length of the DNA strand—a small section from the ends does not get copied. Telomeres cap the ends, ensuring nothing vital gets left out of the replicated cell. Each time a cell divides, a little bit of the telomeres at its ends gets left behind. So, over time, telomeres become shorter and shorter. When they get too short, the cell they’re attached to stops replication and enters senescence. The accumulation of senescent cells in the body is thought to contribute to the development of many age-related health conditions, such as:

A wealth of research indicates linkages between length of telomeres and overall health. While some have interpolated that to mean that short telomeres indicate a short lifespan, others feel it’s more complex than that.

Here’s what you should know about telomeres, the vital role of an enzyme called telomerase, and how to lengthen telomeres (including a very accessible option).

10 Quick Facts About Telomeres

What Are Telomeres?

The word telomere is derived from Greek (as many medical terms are)—specifically, the word “telos,” which means end, and the word “meros,” which means part. Scientists suspect that short telomeres may be a contributing factor to the development of many chronic diseases, while geroscientists think it’s possible that the shortening of telomeres may drive the entire aging process.

Telomere shortening can be thought of as the lighting of a fuse attached to a cell. With each cell division, telomeres grow shorter until (to continue the metaphor) the flame gets too close to valuable genetic information, triggering cellular senescence or apoptosis (cell death).

Technically speaking, telomeres are repeated sequences of DNA that keep our chromosomes stable during cellular division and protect our genetic information. Thus, shorter telomeres correlate with an increased risk of cancer and other diseases linked to genetic malfunctions. Telomeres also regulate the cellular aging process, dictating how many times a cell can safely divide. Scientists used to believe that cells could replicate indefinitely, and research into telomeres has been a vital component of efforts to better understand cellular replication and its effect on human health.

The Science of Telomeres

Pioneering scientists Hermann Muller (who gave telomeres their name) and Barbara McClintock were the first to recognize that telomeres appeared to have a protective function. After their groundbreaking work in the 1930s, however, it would take several more decades for researchers to comprehend how telomeres functioned in relation to cellular aging.

One reason for that was the persistent assumption that cells could divide endlessly, an incorrect belief that was shattered at last in 1961 when two scientists from the Wistar Institute of Anatomy and Biology in Philadelphia, Pennsylvania discovered that cells can only divide a limited number of times. For the lung cell cultures they observed that limit appeared to be set around 40 or 50 divisions.

The next decade ushered in the work of Elizabeth Blackburn, an icon in the field of human telomere research. At Yale University in the 1970s, she became the first to identify a telomere sequence.

Another major breakthrough took place in 1998 when a research team based in Menlo Park, California found that artificially extending the length of the telomeres attached to cells could allow them to continue dividing indefinitely, thereby officially “establishing a causal relationship between telomere shortening and in vitro cellular senescence.”

Then, in 2009, Elizabeth Blackburn, Carol Greider, and Jack Szostak won a Nobel Prize for their discovery of telomerase, an enzyme that lengthens telomeres and which remains shut off in most cells after the early phases of growth.

Since then, telomeres have become a hot topic among those interested in healthy aging. “Once telomeres became popular knowledge, all sorts of people came out of the woodworks selling nutraceuticals, natural products, claiming that it was the fountain of youth,” explained Jerry Shay, a biologist at the University of Texas Southwestern Medical Center who specializes in telomeres, in an interview.

Understanding the Role of Telomerase

As touched on briefly in the preceding section, the enzyme telomerase is responsible for telomere lengthening. When it restores length to telomeres, it bestows the cells those protective caps that are correlated with a longer lifespan. Because of this, some experts in the field of geroscience believe that increasing the body’s supply of telomeres can safeguard—and even restore—the length of our telomeres. This, in turn, will help to prevent the development of age-related diseases.

While a number of different proteins contribute to telomere upkeep, telomerase carries out the most important role—it rebuilds the ends that get shortened during cellular division.

As established earlier, the cells of the body can’t replicate indefinitely. To be more precise, however, somatic cells can’t replicate like that. Stem cells, however, are immortal. To continue dividing without compromising genetic code, stem cells use telomerase to rebuild the ends of their telomeres. With perpetually long telomeres in place, they can carry on dividing, and dividing, and dividing. Telomerase keeps their telomeres at a consistent length regardless of how many times they divide, allowing them to continue with their vital work, which includes tissue growth and regeneration.

It is because ordinary, somatic cells do not use telomerase that they can only divide a limited number of times.

So, you might be thinking that supplementing with telomerase would have to be the most effective anti-aging treatment ever. And in a sense, you’d be right. But scientists worry this approach could come with serious adverse side effects. You see, there’s another type of cell that uses telomerase—cancer cells. That’s why they’re able to replicate so ruthlessly. Experts worry that if telomerase levels rise too high, that could fuel the growth of cancer.

How to Lengthen Telomeres

Because of the potential risks associated with telomerase therapy, research so far has been conducted with rodents. That said, the results have been highly encouraging.

A 2012 study published in EMBO Molecular Medicine found that the use of telomerase gene therapy in adult mice successfully extended lifespans without increasing cancer risk. They found that higher levels of telomerase translated to “remarkable beneficial effects on health and fitness, including insulin sensitivity, osteoporosis, neuromuscular coordination and several molecular biomarkers of aging.” Even more impressive, however, were the increases to lifespan—an increase of 13% for 2-year-old mice and 24% for 1-year-old mice.

While this seems to indicate telomerase therapy could be an effective anti-aging tool, allowing us to live longer, healthier lives, it’s important to remember more research is needed to corroborate those findings. There are (obviously) many differences between humans and mice, including that mice have longer telomeres than humans at baseline.

That said, the results of in-vitro, test-tube studies have also shown that adding telomerase makes it possible for cells to continue to replicate long past the point at which they would typically undergo senescence or apoptosis.

Another interesting approach to lengthening telomeres is the use of RNA therapy. Dr. John Cooke, department chair of cardiovascular sciences at Houston Methodist Research Institute, led a team in analyzing whether RNA therapy could lengthen the telomeres of human cells, albeit in test tubes.

To do so, Cook and his team harvested cells from children living with progeria, a condition that causes such rapid aging, most who have it die in their teens. Earlier studies had already established that children with progeria have markedly short telomeres.

Before the RNA treatment, the harvested cells multiplied poorly and died quickly. Once the RNA was inserted, “cells proliferated normally,” stated Cooke. “It was a dramatic improvement.“ He noted, too, that the RNA treatment rolled back other indicators of aging, like the presence of inflammatory proteins.

A More Accessible Option

While findings on the use of telomerase and RNA are certainly exciting, it’s unlikely that most people will have access to these treatments in the near future. Luckily, there’s a more accessible way you can directly impact the health of your telomeres.

Vicki Lundblad, a professor in the Molecular and Cell Biology Laboratory at the Salk Institute for Biological Sciences, led a team who identified a key protein group that helps lengthen telomere ends. Through analysis of the structure of human telomerase, Lundblad uncovered three EST proteins—known as Est1, Est2, and Est3—that make major contributions to telomerase activity. Est2, along with RNA, does the cellular heavy lifting necessary for reconstructing telomeres, while Est1 and Est3 ensure that process progresses smoothly. Both Est1 and Est3 make unique contributions. Est 1 transports telomerase to the telomeres. “Without Est1, telomerase cannot get to the ends of chromosomes, and thus telomeres shorten,” Lundblad stated.

Ongoing analysis is centered on clarifying the role of Est3. What the team knows so far is that it uses specific amino acids to interact with telomerase. When the team inactivated those amino, shorter telomeres were produced, indication that telomerase activity had been measurably impaired.

In other words, without amino acids, the body cannot utilize telomerase. Yet another reason to ensure your body always has a ready, more-than-adequate supply of essential amino acids.

Conclusion

Telomeres ensure that the cellular division process does not result in the loss of genetic material. Instead, each time your cells divide, a section of your telomeres gets left behind. When telomeres become too short, cells stop dividing and become inactive.

This has led to intense interest in how to preserve and lengthen telomeres. Research indicates that both telomerase therapy and RNA treatments could possibly be effective interventions. However, it will likely be some time before those treatments become available to the public.

In the meantime, a new study points to amino acids as a possible method for enhancing the health of your telomeres. Given the many benefits associated with amino acids, this seems like a telomere-lengthening strategy worth trying.