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.

Why You Need to Know About Epitalon

Epitalon can influence gene expression, extend telomere length, and produce other exciting physiological effects that have what experts call “geroprotective” results. It may be too soon to make definitive statements about epitalon but the findings so far certainly give a justification for further investigation.

Unless you have a scientific background, it’s unlikely you would have heard of epitalon, sometimes referred to as epithalon, epithalone, epithalamin, or epithalamine. If the promise indicated by certain studies on its anti-aging properties prove to be true, however, this synthetic peptide may become a household name.

Research indicates that epitalon is a telomerase activator, meaning it can stimulate telomere elongation. Much of what we know about epitalon comes from the work of Dr. Vladimir Khavinson and other researchers at the St. Petersburg Institute of Bioregulation and Gerontology in Russia where it’s being developed as an anti-aging drug.

In this article, we’ll define what epitalon is and explore what scientists have discovered about its potential anti-aging benefits. But before delving into why scientists are so excited about the effect of epitalon on telomeres, let’s cover some basics about telomeres themselves.

The Link Between Telomeres and Aging

Telomeres cap the ends of our chromosomes and protect our genetic code during cell division. Each chromosome contains the genetic information necessary to keep all the cells in our body healthy and functioning at peak capacity. During cell division, those genes must be copied exactly so that the newly created cells have that same essential information. However, the process of replication always leaves off a small section from the ends of the DNA strands. That’s where telomeres come in. They’re placed at the ends to ensure no vital data gets left behind. Therefore, each time a cell divides, the telomeres capping its chromosomes get shorter. This makes telomere length the limiting factor for cellular division: when they become too short, the cell they’re attached to ceases to divide and enters senescence.

Studies indicate shortened telomeres may cause several adverse consequences of aging and age-related diseases, including increased oxidative stress, cancer, and overall mortality. Some experts have gone so far as to hypothesize that the shortening of telomeres may drive the entire aging process.

Understandably, this has drawn attention to telomere elongation as a possible method for preserving good health as we grow older. Stem cells—a subset of cells within the body with the ability to develop into different cells types (and in some instances, to repair injured tissues)—contain an enzyme called telomerase that keeps telomeres long, allowing those cells to replicate an infinite number of times.

Research indicates that providing the body with supplemental telomerase can indeed be an effective anti-aging treatment, however, it may have seriously deleterious side effects. That’s because cancer cells, like stem cells, rely on telomerase to maintain a ceaseless rate of replication. Experts in the field of gerontology, the multidisciplinary study of aging and the problems that can accompany it, have raised concerns that the use of exogenous telomerase could spur the development of cancer.

Epitalon may offer a way to lengthen telomeres without the same risks associated with the use of supplemental telomerase.

What Is Epitalon?

The discovery of epitalon, a tetrapeptide with the amino acid sequence Ala-Glu-Asp-Gly, was a direct result of efforts to develop safe and effective methods for offsetting adverse effects of aging.

Scientists know that gene expression varies significantly with age, though there are numerous and conflicting explanations for why that might be. A simple and persuasive one goes like this: gene expression acts as a timer for the human life cycle. During our youth, we express genes that allow us to grow. During middle-age, we express genes meant to keep us healthy. And when we reach old age, we begin to express genes that cause our cells to shut down.

Gene expression, on a cellular level, describes the translation of our DNA into proteins, the signaling mechanisms of the body. In the 1970s, Dr. Vladimir Anisimov, of the Department  of Carcinogenesis and Oncogerontology, N.N. Petrov Research Institute of Oncology in St. Petersburg, and a frequent collaborator of Dr. Khavinson, began investigating the role of short peptides, which he ultimately learned function as epigenetic signals that both promote and repress the expression of whole categories of genes.

These short peptides, strings of fewer than 10 amino acids, can regulate the chemistry of the entire body. This capacity comes in part from the fact that their small size allows them to pass through the skin as well as through the blood-brain barrier. And unlike larger proteins, they tend to pass through the digestive tract intact.

In a review that synthesized a few decades of data, Anisimov shared the results of his investigation of the roles of small peptides isolated from different organs and tissues, such as the thymus gland and the pineal gland, on the mechanisms of aging. As part of his research, Anisimov also developed analogues of those peptide bioregulators, such as synthetic tetrapeptide epitalon.

The terms “epithalamin” and “epithalamine” typically refer to extracted peptide preparations, while “epitalon,” “epithalon,” and “epithalone” refer to synthetic peptide preparations. As epitalon has been shown to reproduce the effects of epithalamin, we will use that term throughout unless further specificity is required for clarity.

The long-term use of certain peptide preparations led to significantly increased longevity (mean lifespan increases between 20% and 40%) as well as a slower rate of age-associated alterations to biomarkers linked to physical and mental decline. Anisimov’s work also showed lower rates of spontaneous tumor incidence in subjects who received epitalon treatment, indicating that it has carcinogenic effects.

We’ll dig into the specifics of some pioneering animal and human studies on epitalon in the following section, but first, let’s discuss why Anismov focused on the thymus and pineal gland.

How the Thymus and Pineal Gland Affect Your Health

The main function of the thymus, a gland in the upper region of the chest, is to teach the immune cells to differentiate between invading pathogens and the cells of the body. As we age, the size of the thymus decreases, which some have suggested could be the root cause of age-related decreases to immune function, resulting in higher incidences of infections and autoimmune diseases.

In the 1980s, the Slavic researchers whom we have to thank for the bulk of our knowledge about short peptides were focused on the possibilities of a thymic peptide bioregulator  called thymalin which they found could spur the thymus to re-grow, thus enhancing immune function. The use of thymalin also resulted in other desirable anti-aging benefits, such as:

Studies consistently linked thymalin treatment to decreased mortality rates too.

However, the heyday of thymalin was short-lived. In the early 1990s, researchers began focusing on the role the pineal gland plays in the aging process, specifically, its ability to modulate functions of the neuroendocrine and immune systems, which have been shown to decease with age.

Located in a region of the brain called the epithalamus, the pineal gland regulates the body’s sleep/wake cycle, a crucial task that involves the secretion of a hormone called melatonin. A significant moment in the progression of research in this field occurred when researchers used syngeneic transplantation to place pineal glands from young mice into the thymus of older mice, resulting in a prolonged lifespan. Concurrently, researchers were examining the effects of various pineal peptides. One such compound, epithalamin, was found to be a complex peptide bioregulator that could reduce the rate of cellular aging, leading to increased longevity.

Epithalamin, like thymalin, is a short peptide composed of a string of four amino acids. However, studies showed that it could increase longevity more consistently than thymalin, that it suppressed cancer growth, and that it even had a more pronounced effect on thymic growth.

In the early 2000s, excitement about epitalon increased even more when scientists found it could activate telomerase, leading to the regrowth of telomeres. It has now become the most-studied short peptide.

11 Essential Facts Everyone Should Know About Epitalon

Important Findings About the Benefits of Epitalon

The effects of epitalon have been examined in a variety of contexts: in vitro studies, animal studies, and human studies. Findings in all three realms have clearly and consistently indicated pronounced anti-aging benefits.

In Vitro Studies

The most significant work being done in vitro has to do with the effect of epitalon on telomerase activity. According to a 2003 study with Khavinson as the lead author, the addition of epitalon to a human somatic cell that did not naturally produce telomerase induced enzymatic telomerase activity, resulting in telomere elongation. They concluded that these findings indicate “the possibility of prolonging life span of a cell population and of the whole organism.”

In 2016, a St. Petersburg-based research team found that epitalon produced telomere elongation significant enough to allow cells to exceed the Hayflick limit, which describes the typical lifespan for a human cell.

Animal Studies

In 1998, Anisimov and Khavinson collaborated on a study that, as described in an article published by the The Longevity Research Institute (LRI), examined the effect of epithalamin, a pineal peptide preparation, on the lifespan of fruit flies, mice, and rats. They found that epithalamin led to a median lifespan extension of between 14% and 32% longer than control subjects. Interestingly, they also found indications that epithalamin decreased cancer risk.

The LRI article cited above shares further key findings from other studies on epithalamin. Female rats between the ages of 16 and 18 months receiving daily doses of 0.1 milligrams of pineal peptide extract had a 10% longer lifespan than control subjects per a study published in Experimentelle Pathologie. When the dose was increased to 0.5 milligrams, the rats lived 25% longer than controls. Female mice given a 0.5-milligram dose of epithalamin daily lived 31% longer than controls and had 50% fewer tumors, according to another study Anisimov and Khavinson worked on.

In 2002, a team from the Department of Medical Biology and Genetics, I. P. Pavlov St. Petersburg State Medical University collaborated with Anisimov and Khavinson to examine the effects of epitalon on chromosome aberrations related to aging. They found that the incidence of such aberrations decreased by between 17.9% and 30% compared to age-matched controls. The team concluded that these results point to an “antimutagenic effect,” which they hypothesize could be the source of epitalon’s geroprotective abilities. It’s worth noting, too, that the changes observed were consistent with increased telomere length.

Some skeptics have suggested that the lifespan extension benefits associated with various anti-aging treatments, such as epithalamin and epitalon, can more accurately be attributed to incidental food intake changes related to the way such treatments affect appetite. And indeed, fasting has been shown to have an impressive effect on lifespan.

In the case of epitalon specifically, studies with standardized food consumption have yielded the same findings related to longevity.

Take, for example a study published in Biogerontology in 2003Anisimov, Khavinson, and a team of seven other researchers from the Department of Carcinogenesis and Oncogerontology at the NN Petrov Research Institute of Oncology in St. Petersburg looked at the effects of epitalon on body weight, food consumption, and lifespan in female Swiss SHR mice. The researchers subcutaneously injected the mice in the treatment group with 1.0 microgram/mouse of epitalon on five consecutive days each month. The control group received saline injections on the same schedule. The results showed a 12.3% extension of maximum lifespan in comparison to the control group with no changes to food consumption or body weight.

Epitalon has been linked to benefits that, while relevant to those interested in remaining healthy and vital while they age, can be quite valuable for individuals of all ages.

A study published in the Archives of Gerontology and Geriatrics in 2007 looked at the antioxidant properties of epitalon. The authors (Khavinson and two other Russian researchers) found that epitalon produced impressive antioxidant effects, and perhaps even more crucially, simultaneously stimulated the expression of additional antioxidant enzymes such as ceruloplasmin, glutathione peroxidase, glutathione-S-transferase, and superoxide dismutase (SOD). All in all, this translates to a major fortification of the body’s antioxidant defense system.

Anisimov joined forces with a team of scientists from the Koret School of Veterinary Medicine at the Hebrew University of Jerusalem in Rehovot, Israel to examine the effect of epitalon on cancer growth. To do so, they injected 0.1-microgram doses of epitalon 5 times each week. They found this treatment decreased the number of malignant tumors and prevented the development of metastases. The long-term exposure to epitalon involved in the treatment protocol produced no adverse side effects.

Human Studies

Human studies have also yielded promising results. A randomized, controlled trial co-authored by Khavinson and a researcher named Vyacheslav G. Morozov and published in Neuroendocrinology Letters enrolled 94 women between the ages of 66 and 94, all of whom lived at the War Veterans Home in St. Petersburg. Participants were randomly assigned to one of four groups: the first received a placebo, the second a thymus extract called thymalin, the third epithalamin, and the fourth both thymalin and epithalamin.

Over the course of the six year study, 81.8% of the patients in the control group died, while only 41.7% of patients in the thymalin group and 45.8% of those in the epithalamin group, both of which received treatment for 2 years, died. And only a stunningly slight 20.0% of those in the group who received both epithalamin and thymalin for the full 6 years had died by the study’s conclusion. Further, the authors noted that participants who received epithalamin had lower rates of ischemic heart disease as well as improved levels of key biomarkers such as cortisol and insulin.

In 2006, Khavinson collaborated with lead author O.V. Korkushko of the Institute of Gerontology at the Academy of Medical Sciences of Ukraine in Kiev on a randomized clinical study done with human subjects. They set out to examine the effect of “pineal gland peptide preparation”—epithalamin—on elderly patients with accelerated aging of the cardiovascular system, and  found that long-term treatment with 50-milligram injections of epithalamin every 6 months for a duration of 12 years lead to decreased cardiovascular aging as well as decreased overall functional age. Epithalamin also improved participants’ exercise tolerance. Furthermore, mortality in the group that received epithalamin was 28% lower than in the control group.

In a review titled “Peptides, Genome, and Aging,” Khavinson states that treatment with both epitalon and epithalamin resulted in increased telomere lengths in the blood cells of patients between 60 and 65 years of age as well as 75 and 80 years of age. The efficacy of the two treatments proved to be equal.

As was the case for research done with animal subjects, human trials pointed to epitalon benefits desirable for individuals of all ages.

A 2011 collaboration between Korkushko, Khavinson, and two other researchers examined the effects of epitalon on elderly coronary patients. The team found that long-term treatment—meaning six courses over 3 years—resulted in numerous benefits, including:

  • Slowed rate of cardiovascular aging
  • Prevention of age-related declines to physical endurance
  • Rebalanced melatonin production and circadian rhythm
  • Normalized carbohydrate and fat metabolism

Patients also had lower rates of mortality than those in the control group who received basic therapy but no epitalon.

A 2013 study looked at the influence of epitalon on chromosome aberrations in pulmonary tuberculosis patients, as this disease is classified as one stemming from a genetic predisposition. Genome stability, or rather, instability, is one marker that can assist with the early detection of pulmonary tuberculosis. The researchers hoped that epitalon would have a corrective effect on the genome variability linked to the disease. Epitalon proved to have a potent protective effect—it reduced the frequency of aberrant cells for all subjects. However, it did not have a significant effect on chromosomal fragility that was already present.

Conclusion

The work of Dr. Vladimir Khavinson and other researchers, primarily based in Russia and Ukraine, indicate that epitalon has immense promise as an anti-aging drug. This promise has to do with epitalon’s ability to influence gene expression, extend telomere length, and other exciting physiological effects that have what experts call “geroprotective” results.

Little research has yet been conducted on epitalon by researchers without ties to Russian institutions, so it may be too soon to make definitive statements about epitalon but the findings so far certainly give a justification for further investigation.

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.

How to Memorize Amino Acids: Your Study Hack for Acing the MCATs

How to memorize amino acids: 6 creative mnemonics for memorizing the different amino acid classifications, including charged, polar, nonpolar, essential, nonessential, and aromatic.

Whether you’re studying to pass the MCATs (future medical students) or the PCATs (future pharmacists), you’re going to need to summon extensive knowledge of the 20 main amino acids relevant to human health. We have a few mnemonics that can help you ace your upcoming exam. Read on to learn how to memorize amino acids.

The Use of Mnemonics for Memory

Mnemonic devices are memory aids, and can be anything from a rhyme, a song (like the alphabet song), or any other trick to remember a set of information for whatever reason. Researchers have confirmed that mnemonic strategies help improve memory in those with mild cognitive impairment by literally reshaping the brain network to support superior memory.

Some examples of mnemonics include the way people remember the order of colors in the rainbow: Red, Orange, Yellow, Green, Blue, Indigo, and Violet, which can be recalled by thinking of a man named ROY G. BIV, or by remembering the phrase “Rainbows Over Your Great Big Island Vista.”

The mnemonic for order of operations is PEMDAS or “Please Excuse My Dear Aunt Sally”: Parentheses, Exponents, Multiplication and Division, and Addition and Subtraction. Same with remembering the order of the plants that revolve around our sun: Mercury, Venus, Earth, Mars, Jupiter, Saturn, Uranus, and Neptune can be remembered with the phrase, “My Very Educated Mother Just Served Us Noodles.”

These sorts of mnemonic devices might only need to take up space in your head until you’ve fully retained the information, or these devices may serve you for the rest of your life, like remembering the clockwise order of North, East, South, and West by forever thinking, “Never Eat Soggy Waffles.” As nonsensical as it may be, it’s helpful!

How to memorize Amino Acids

How to Memorize Amino Acids: 6 Mnemonic Devices

Without further ado, here are the tricks for how to memorize 20 amino acids. MCATs are notoriously difficult and stressful, so if you can help yourself file away the information you need on the aminos in general, like which are polar and nonpolar, which are essential and nonessential, plus their structures and which have electrically charged side chains, you’re that much closer to passing your exam.

Fundamentals First

Let’s start with the structure of amino acids, as that is what classifies them each so distinctly.

1. Amino Acid Structures

Amino acids all have the same basic structure, with a hydrogen atom and three functional groups of molecules attached to a central atom. They start with a carbon atom at the center and are joined by an amino or amine group (~NH3+), a hydrogen atom, and a carboxyl group (~COOH). The final side chain is the one that makes each amino different: the R group is the variable group that makes each structure distinct.

The way to remember their collective structure is CORN, an acronym for the carboxyl group (CO), R group (R), and amino group (N).

When it comes to L- vs. D- amino acids, the difference is the direction that they rotate. For the L- or left-moving amino acids, starting with the carboxyl group (CO) the next structure that moves to the top will be the R group (R), and then the amino group (N). D- aminos move in the opposite direction showing you carboxyl, then amino, then the R group. The order stays the same, it’s just a matter of whether the molecule rotates right or left.

CORN is easier to keep in mind than the non-word CONR for remembering which groups in what order surround the central carbon atom.

All 20 Amino Acids: Charged, Polar, and Nonpolar

Read on for ways to remember which amino acids are hydrophilic (polar) and which are hydrophobic (nonpolar), as well as a trick for remembering the basic (positively charged) and acidic (negatively charged) aminos. All 20 amino acids can be sorted into the three categories: charged, polar, and nonpolar.

2. Charged Amino Acids

In organic chemistry, of the 20 common amino acids, five have side chains that are able to be charged, two negatively and three positively.

  • Negatively charged amino acids: Glutamate or glutamic acid (Glu, E) and aspartate or aspartic acid (Asp, D). These are the two acidic amino acids (hence the word “acid” in their names). Here’s a good place to note that aspartate and glutamate are identical to asparagine (Asn, N) and glutamine (Gln, Q) except that the first two have negatively charged oxygen molecules attached to them, while the latter two have an amino group with nitrogen contained within. When you notice the “n” in each of their three-letter codes, think of nitrogen, and that may help you differentiate between them.
  • Positively charged amino acids: Arginine (Arg, R), histidine (His, H), and lysine (Lys, K). These are also the three basic amino acids.

To remember these five we suggest the phrase: “Dragons Eat Knights Riding Horses.” It’s based on their one-letter codes D, E, K, R, and H. As far as which one-letter code goes to which amino, we suggest you employ flashcards for memorizing the letter abbreviations, because as you can see, they don’t necessarily contain the letter to which they’re assigned.

3. Polar Amino Acids (Hydrophilic)

Polar amino acids are so classified because they contain side chains that prefer to reside in water environments (hydrophilic). Histidine, lysine, and arginine (the positively charged aminos) are also considered polar. The rest include: asparagine (Asn, N), aspartate (Asp, D), serine (Ser, S), glutamine (Gln, Q), threonine (Thr, T), glutamate (Glu, E), and tyrosine (Tyr, Y).

One way to remember these is by their one-letter codes: “Santa’s Team Darns New Quilts Every Year.”

4. Nonpolar Amino Acids (Hydrophobic)

The nonpolar, hydrophobic amino acids are:

  • Alanine (Ala, A)
  • Phenylalanine (Phe, F)
  • Glycine (Gly, G)
  • Proline (Pro, P)
  • Isoleucine (Ile)
  • Tryptophan (Trp, W)
  • Leucine (Leu, L)
  • Isoleucine (Ile, I)
  • Valine (Val, V)
  • Methionine (Met, M)
  • Cysteine (Cys, C)

Here’s a handy way to remember these 10 nonpolar aminos: “Grandma Always Visits London In May For Winston Churchill’s Party.” Winston Churchill was born November 30, 1874, but as the prime minister during World War II, you might imagine he’d have a party each year on May 8th, which is Victory in Europe Day, celebrating the formal surrender of the Nazis to the Allies. This is a mnemonic device that could help you on any upcoming history exams too!

Aromatic, Essential, and Nonessential Amino Acids

There are a few more classifications that might be useful to know on MCAT amino acids questions: which amino acids are aromatic and which are considered essential vs. nonessential.

5. Essential Amino Acids

The essential amino acids are the ones we need to get from our food, because they cannot be produced independently inside the body. They include:

  • Histidine
  • Leucine
  • Isoleucine
  • Lysine
  • Methionine
  • Phenylalanine
  • Threonine
  • Tryptophan
  • Valine

The best mnemonic device for this one is not based on the one-letter codes, but instead on the first letter of each amino: PVT. T.M. HILL. Just think of Private T.M. Hill as one of the brave soldiers who returned from war and happily celebrates each May with Winston Churchill.

6. Nonessential Amino Acids

Here are the remaining 11 amino acids that our bodies can synthesize independently:

  • Alanine
  • Arginine
  • Asparagine
  • Aspartic acid
  • Cysteine
  • Glutamic acid
  • Glutamine
  • Glycine
  • Proline
  • Serine
  • Tyrosine

You can use the first letter of each one as a mnemonic: “Ah, Almost All Girls Go Crazy After Getting Taken Prom Shopping.” If you think the guys go as crazy as the girls, feel free to sub in one G-word for the other.

Memorable Aminos

Now you have six mnemonic tools for how to memorize the amino acids in preparation for your exams. There’s always more information to learn (for example, the three aromatic amino acids), but these memory tricks can help you lay the groundwork for a pre-med education that’s only just beginning. Best of luck!

When Is a Nutrient an Antinutrient?

Antinutrients, like phytates, oxalates, and glucosinolates, are components of food or dietary nutrients that interfere with absorption of other nutrients. In this article, we’ll cover the latest findings on how antinutrients affect your health so you can separate fact from fiction as you continue seeing news coverage on this hot topic.

If you’re interested in optimizing your diet, you’ve likely encountered the word antinutrients before. Certain experts have raised concerns about antinutrients, components of food or dietary nutrients that interfere with the absorption of other nutrients. Different antinutrients, such as phytates, oxalates, and glucosinolates can be found in various types of food, including fruits, veggies, legumes, dairy, and meat.

At this time, the long-term impact of antinutrients on human health has yet to be fully sussed out. Research has shown that while antinutrients can cause health problems, they can also bring health benefits. The majority opinion among health authorities at this time is that the advantages of eating foods containing antinutrients outweigh the adverse effects of forgoing those foods altogether.

Read on to learn more about antinutrients and how they affect your health so you can separate fact from fiction as you continue seeing news coverage on this hot topic.

What Are Antinutrients?

The answer to the question of what antinutrients are can be found in the name itself: while the term nutrients describes substances that provide the raw materials plants and animals (humans included) need to thrive, antinutrients prevent them from absorbing and utilizing those substances. In short, they block the absorption of nutrients. Antinutrients occur naturally in a variety of both plant-based and animal-based foods.

The purpose of those found in plants, like lectins, is to prevent bacterial infections and protect against consumption by predators, as an article published in Plant Physiology outlines. To illustrate that idea, consider the case of the nightshade family of vegetables, which includes potatoes, tomatoes, peppers, and eggplants. All nightshade vegetables contain solanine and chaconine, antinutrients intended to deter animals and humans alike from consuming them as they can make you sick when ingested in large doses.

A common health concern raised by those worried about antinutrient consumption is that ingesting high amounts can result in nutrient deficiencies, particularly for individuals adhering to diets that classify certain foods as off-limits, particularly vegan or vegetarian diets organized around legumes and grains. Another worry is that they may increase intestinal permeability, resulting in a health condition referred to as leaky gut.

Fact-Checking Concerns About 7 Antinutrients

As described above, antinutrients impede the body’s ability to absorb essential nutrients such as vitamins, minerals, amino acids, and so on. While this clearly has the potential to be problematic, the evidence so far indicates that it’s unlikely to cause issues in the absence of overall malnutrition or dietary imbalances. Furthermore, studies show that in certain circumstances, antinutrients can actually enhance a person’s health—for instance, tannins found in tea can decrease cancer risk and phytic acid can lower cholesterol and triglyceride levels.

In the sections below, we’ll delve into the details of common concerns raised about seven of the most significant antinutrient groups:

  1. Lectins
  2. Phytates
  3. Oxalates
  4. Tannins and other flavonoids
  5. Glucosinolates
  6. Enzyme inhibitors
  7. Saponins

1. Lectins

Lectins can be found in all plants but in particularly high concentrations in seeds, legumes (most notably kidney beans), and whole grains as they tend to cluster in the parts of seeds that go on to become leaves after sprouting occurs.

In the popular consciousness, lectins have entered into the same category as gluten: a poorly understood substance widely believed to be, somehow, bad.

Going “lectin-free,” in the way you might go gluten-free, is posited as a way to prevent leaky gut syndrome. The theory is that when you eat foods that contain high amounts of lectin, the lectin proteins bind to cells in the walls of the digestive tract where they then create minute punctures that allow the contents of the gut to leak into the bloodstream. In high amounts, lectins may also prevent the proper absorption of certain nutrients, including calcium, iron, phosphorus, and zinc.

According to a literature review published in the American Journal of Clinical Nutrition, some lectins do have “deleterious nutritional effects.” The review also notes that dietary exposure to lectins appears to be widespread. However, the authors could not decisively determine whether lectins caused noticeable health issues.

A separate article states that due to the “ubiquitous” presence of lectins in plants, we all ingest them daily in “appreciable amounts”—unless, of course, you’re taking steps to avoid them. The article goes on to explain that it is the ability of lectins to remain intact in the digestive tract that allows them to cause damage to its lining, though the effects it notes do not include the development of leaky gut, but rather:

  • Loss of gut epithelial cells
  • Damage to the membranes of the epithelium
  • Impaired digestion and absorption of nutrients
  • Disruption to balance of bacterial flora and immune state of the gut

Before you begin to panic about the logistical challenges of avoiding lectins, remember that researchers have yet to find conclusive evidence that consuming lectin-containing foods produces damage significant enough to impact the well-being of individuals who are otherwise in good health.

Phytates

Also called phytic acid, these antinutrients can be found in many of the same foods as lectins—think legumes such as lentils, nuts, seeds, whole grains, and pseudocereals like quinoa. Their purpose for the foods that contain them is to provide the phosphorous necessary for the growing plant.

Studies show that phytates interfere with the absorption of certain minerals and trace elements, including calcium, iron, magnesium, and zinc, by binding to those micronutrients during digestion.

However, an article published in Molecular Nutrition & Food Research notes that dietary phytates also have beneficial effects such as decreasing the likelihood of kidney stone formation and keeping blood sugar and blood lipid levels in the healthy range. The authors note, too, that phytates appear to have antioxidant and possibly anticancerogenic properties.

So, it seems that the phytate content of a food should certainly not be a cause for concern and may even be a boon to your health.

Oxalates

Oxalates, or oxalic acid, can be commonly found in nuts and seeds as well as in leafy greens, fruits, vegetables (particularly rhubarb), and cocoa. Oxalates bind to minerals to form calcium oxalate or iron oxalate. This makes it much more challenging for the body to absorb those minerals.

A review published in the American Journal of Clinical Nutrition compared the absorbability of calcium from spinach, which contains oxalates, to that of calcium from milk, which does not, and found that the absorption from milk was always higher. The mean absorption for milk was 27.6% while spinach achieved a mere 5.1%.

In some instances, oxalates have also been linked to an elevated risk of kidney stone formation, though thanks to the high nutritional value of oxalate-containing foods, physicians no longer universally recommend low-oxalate diets to those with kidney stones. In other words, there’s no need to try to avoid oxalate-rich foods due to this possible side effect. Most people will harm their health more by avoiding these healthful foods than by ingesting the oxalates they contain.

Tannins and Other Flavonoids

You may be confused to see flavonoids on this list, as this group of naturally occurring polyphenols (which include tannins) have often been discussed as nutraceuticals because of their antioxidant properties. However, these compounds, like the other antinutrients, chelate or bind with minerals such as iron and zinc and reduce the absorption of these nutrients.

For instance, the tannins found in tea, coffee, fruit skins, and legumes have been linked to decreases in iron absorption. Yet they have also been shown to have anticarcinogenic activity and to inhibit the growth of fungi, bacteria, and viruses.

One way to think about tannins, as an article published in Trends in Food Science and Technology aptly put it, is as “a double-edged sword.” It appears, however, that consuming small quantities of tannins will allow you to access their benefits, while larger amounts are needed before the threshold for adverse effects is crossed.

Glucosinolates

These antinutrients are found in high amounts in cruciferous vegetables like broccoli, Brussels sprouts, and cabbage. Like tannins and the rest of the flavonoid family, you may be more familiar with glucosinolates as a desirable phytonutrient.

Yet the same compounds renowned for their ability to help prevent cancer also impede iodine absorption, which can lead to an iodine deficiency and impaired thyroid function. Individuals whose diets contain insufficient amounts of iodine or who have hypothyroidism (underactive thyroid) are most at risk for this issue.

There’s also some indication of an association between a greater intake of glucosinolates and a higher risk of type 2 diabetes. Studies so far, such as this one from 2018, have all been population-based, making it too early to say whether there’s a causal relationship at work.

Enzyme Inhibitors

This category of antinutrients includes protease, amylase, and lipase inhibitors, all of which impact the body’s ability to digest and absorb macronutrients. They can be found in a wide swathe of the plant kingdom, including legumes, seeds, and whole grains.

A protease is an enzyme (the -ase ending in chemistry denotes an enzyme) that helps break down proteins, amylase is an enzyme that breaks down certain carbohydrates, and lipase is an enzyme that breaks down lipids (fats). If the enzyme is “inhibited,” it is prevented from breaking down the macronutrient and making it available for absorption. Therefore, protease inhibitors make the body less able to digest protein, amylase inhibitors do the same for carbohydrates, and lipase inhibitors do so for fat.

Food sources of protease inhibitors include beans and other legumes, cucumbers, radishes, broccoli, spinach, potatoes, and egg whites, which contain a trypsin inhibitor along with avidin, which interferes with biotin absorption.

Interestingly, both amylase and amylase inhibitors are touted as having health benefits. Natural dietary sources of amylase include raw fruits and vegetables, along with sprouted seeds, nuts, legumes and whole grains. Amylase inhibitors are found in Garcinia cambogia, guar, inulin, Rosmarinic acid, and other plant foods.

Lipase inhibitors, as already noted, interfere with the enzymes we use to process fats. Lipase inhibitors do not discriminate between fats, meaning absorption of good fats like omega-3 can be compromised. However, they can also be beneficial in that they protect the body from absorbing harmful fats. For that reason, the FDA approved a prescription lipase inhibitor called Orlistat that can increase weight-loss results by allowing fats to pass through your system unprocessed. Orlistat can also beneficially lower total cholesterol and low-density lipoprotein, return blood pressure levels to the healthy range, and regulate fasting glucose and insulin concentrations.

Saponins

Saponins are perhaps best known for their ability to produce soapy foam when shaken with water. They can be found in a range of legumes and whole grains and can interfere with normal nutrient absorption. Per an article published in the International Journal of Nutrition and Food Sciences, they may also inhibit the actions of various digestive enzymes in the same manner as the substances discussed in the preceding section, thereby decreasing protein digestibility.

However, that same article notes that there’s evidence saponins lower cholesterol. An article published in the Journal of Medicinal Food went even further, describing saponins as “health-promoting components” and praising them for their ability to decrease your risk of cancer.

Other Antinutrients You May Encounter

In addition to the seven antinutrients discussed above, you may see references to other antinutrients. Keep in mind that what findings exist about their impact on human health likely show the same complicated and contradictory results. With that said, here are several other antinutrients as well as some food sources for each:

  • Allicin and mustard oil: Alliums like chives, leeks, onions, scallions, shallots, and garlic
  • Alpha-amylase inhibitors: Whole grains, legumes, the skins of various nuts, and the leaves of the stevia plant
  • Calcitriol, solanine, nicotine: Nightshade vegetables like eggplant, peppers, tomatoes as well as goji berries
  • Goitrogens: Cruciferous vegetables, soybeans, and peanuts
  • Oligosaccharides: Wheat, legumes, asparagus, and alliums
  • Salicylates: Berries and other fruits like apricots as well as some herbs and spices including cayenne, ginger, and turmeric
  • Uric acid: Primarily animal-based foods like meat (particularly organ meat), eggs, and dairy as well as legumes and some vegetables

14 Common Antinutrients and the Foods You'll Find Them In

How Antinutrients Affect Your Health

It’s challenging to speak generally about the health effects of antinutrients since they depend on an individual’s metabolism, how the food is cooked and prepared, and the presence of any food sensitivities, nutrient deficiencies, or health conditions.

Keep in mind, too, that many dietary substances can act as antinutrients under certain circumstances.  For example, alcohol, when consumed in excess, interferes with the bioavailability of zinc and the B vitamins.

Also, the antinutrient only impairs the absorption of nutrients that are co-ingested in the meal. For example, a phytate-rich snack of raw almonds won’t affect the absorption of iron from a steak consumed later in the day.

There are many other strategies to “neutralize” the antinutrients found in foods. Many culinary techniques such as soaking, fermenting, and sprouting (and, of course, cooking) of beans and seeds are common approaches that increase the palatability and nutrient availability.

In a balanced, omnivorous diet, antinutrients present no problem, and the benefits they confer, such as antioxidant properties and removal of toxic metals, far outweigh any impact on mineral balance.

Vegetarian or vegan diets, on the other hand, may involve the combination of low intake of iron, zinc, and calcium and a high consumption of grains that contain phytates and other antinutrients. The result of this combination can be dietary deficiencies in minerals that, over time, lead to a deficiency. These mineral imbalances result in impaired immune function, anemia, and poor bone health, among other symptoms.

That said, there’s some indication, like this study done in 2012, that the bodies of individuals adhering to such diets may adapt over time to the continued presence of antinutrients by becoming more efficient at metabolizing minerals such as iron and zinc.

Individuals with an elevated risk of developing conditions linked to mineral deficiencies, such as osteoporosis or anemia with iron deficiency may wish to consult a dietitian or nutritionist to develop an eating approach designed to improve mineral absorption. Such a strategy might be to reduce antinutrients, but that’s certainly not the only method. You might instead strategically time intake of foods with high antinutrient content, such as tea, to avoid impeding mineral absorption, or plan to take a high-quality calcium supplement after consuming a legume dish high in phytates.

It’s also worth noting that antinutrients can largely be minimized by food processing and by genetic engineering. In countries with less industrialized agricultural systems, antinutrients have presented nutritional problems, but in the United States, most diets contain micronutrients in amounts well above the minimal requirement.

Interestingly, the tendency to put more and more focus on the benefits of unprocessed fruit, vegetables and grains, increases the likelihood that antinutrients could undermine a well-intended dietary plan.

As established in the last section, antinutrients often have health benefits of their own. While it’s true that phytates interfere with calcium absorption, they also manage the body’s rate of digestion, forestalling blood sugar spikes. Because antinutrients can be quite good for you, most experts do not recommend that you avoid consuming them entirely.  As long as you eat foods with a high antinutrient content in the context of a nutritious, varied diet, there’s very little risk involved.

Conclusion

So, should you worry about  antinutrients? The simple answer is that they don’t need to be a problem if care is taken in preparing foods and timing the ingestion of raw foods and snacks apart from mineral-dense meals or dietary supplements. Certain foods will likely contain some antinutrients no matter how you process and prepare them, however, the nutrients found in those foods will typically have a more pronounced effect than the antinutrients. By eating a wide assortment of foods each day, and taking care not to eat meals centered on a large portion of a food source of antinutrients, you should be able to offset any potential adverse effects of antinutrients.

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.