Category Archives: Non-Essential Amino Acids

How Many Amino Acids are there – 20, 22, or 200?

For a while it was thought that there were only 20 amino acids, and many websites still reflect this today, but in fact, a couple of new aminos were discovered making a total of 22 amino acids. But how many amino acids are there really?

The real question is how many amino acids exist beyond the 22 we know of SO FAR, and what about other types of amino acids? The reality is that amino acids, which are the basic building blocks of the body, are in abundance within the body. They are sources of energy such as carbohydrates and fats, except that amino acids contain nitrogen (N); because of this they play a role in forming muscles, tissues, organs, skin, and even hair.

There are 20 amino acids in the our standard genetic code, and the additional 2 aminos are outside this realm. These are comprised of the amino acids selenocysteine and pyrrolysine. These amino acids were discovered only about three decades and two decades ago respectively.

Nine essential amino acids act as the precursors to neurotransmitters in the brain and enzymes that help with bodily functions like digestion. These  amino acids are essential for health, and regulate the body’s metabolic processes. There are hormones that are made up of amino acids, antibodies too, so they affect the immune system. Plus they transport oxygen and nutrients in the body.

How Many Kinds of Amino Acids are there?

Different amino acids have different functions. How many amino acids, types, or kinds that exist depend on whether they are:

Essential – 9
Non-essential – 13

How Many Essential Amino Acids Are There?

How many amino acids are “essential” (meaning you must get them from food)? They are listed as: histidine, leucine, isoleucine, lysine, methionine, phenylalanine, threonine, tryptophan, valine.

Several essential amino acids are available in supplement mixes as BCAAs, or branch chain amino acids. The specific aminos included are often leucine, isoleucine, and valine. You can get BCAA powders from Beamzen.

How Many Amino Acids are Non-Essential

How many amino acids are “non-essential” (meaning your body makes them)? These are listed as: arginine, alanine, asparagine, aspartate (aspartic acid), cysteine, glutamate (glutamic acid), glutamine, glycine, proline, serine, tyrosine (interchangeable with phenylalanine), selenocysteine, and pyrrolysine. Although pyrrolysine is not used by humans.

Semi-Essential Amino Acids

However, how many amino acids from one of the above groups are actually conditional or “semi-essential” amino acids? These are: arginine, cysteine, glycine, glutamine, proline, serine, tyrosine.

There are 22 Amino Acids

These above are the 20 more well-known amino acids; however, just how many amino acids exist actually are counted as being over 200 in numbers, but the 22 proteinogenic amino acids are the ones that are commonly known.

These more commonly known aminos can be found in food (all meat such as beef, pork, chicken, seafood, and even eggs are excellent sources of all 22 amino acids). They can also be bought as amino acid supplements individually or as a complex of many in balanced forms for their health benefits.

But haven’t we missed some? What about ornithine and citrulline? Just as phenylalanine and tyrosine are interchangeable, so are ornithine, citrulline, and arginine. Although they have different chemical structures, they have similar benefits and effects on the body and can be interchanged in the diet. For example, both arginine and citrulline act to increase nitric oxide in the body.

How many amino acids have you had in your diet today?

Recommended Daily Intakes for Essential Aminos

Here are the recommended daily intakes in milligrams per kilogram of body weight. These recommendations are made by the World Health Organization. Here is an in depth guide from the WHO on the calculations behind the recommended daily intakes.

  • Valine: 26mg per kg
  • Tyrptophan: 4mg per kg
  • Threonine: 15mg per kg
  • Phenylalanine and Tyrosine: 25mg per kg
  • Methionine and Cysteine: 15mg per kg
  • Lysine: 30mg per kg
  • Leucine: 39mg per kg
  • Isoleucine: 29mg per kg
  • Histidine: 10mg per kg

Reference:

http://aminoacidstudies.org/#sthash.51ThyP74.dpuf
Wikipedia’s Table of Amino Acids

GABA: New Treatment To Improve Recovery After Stroke

Can adjusting the levels of the amino acid GABA improve post-stroke recovery? Results are positive in this animal study, which has led to new hope for stroke patients.

Stroke is a leading cause of death worldwide. And even if the stroke victim survives, the disturbance in the brain’s blood supply—the stroke—can cause brain damage. While some people can and do make a near-complete recovery, many are left with disabilities such as the inability to understand or to speak, or the inability to move limbs on one side of the body.

This damage is often so severe that one third of stroke survivors are confined to nursing homes or institutions.

A Clarkson, B Huang, et al, researchers at the Department of Neurology, The David Geffen School of Medicine at UCLA, LA, USA, hoped to improve post-stroke recovery with drugs. They knew that, depending on the severity of the brain damage, the brain can repair itself after a stroke. The neurons in the brain re-map cognitive functions using non-damaged brain tissue.

The amino acid GABA is critical for this re-mapping process in the brain. GABA is the main neurotransmitter, which means it transmits the signals within the brain. GABA is actually synthesized in the brain, from the amino acid glutamate.

In this animal study, the researchers wanted to examine the brain’s ability to re-map if GABA levels were adjusted.

GABA studied in stroke trial

In this animal study, the researchers analyzed data from post-stroke mice. Stroke caused an increase in extrasynaptic GABA transmission. But when the GABA levels were decreased, the brains showed earlier, and more robust, motor recovery.

The researchers reported that timing is crucial when adjusting GABA levels. It can actually cause more brain damage if done too early. With the mice, the researchers found that delaying treatment until 3 days after stroke improved recovery.

The researchers concluded that targeting GABA helps the brain re-map its neural pathways, which enhances motor recovery. Targeting GABA is therefore a possible treatment in post-stroke recovery.

My personal experience with GABA

I love taking a GABA supplement and the benefits it proposes. It enhances my cognitive function and ensures that my brain is in optimal health. This study is more supporting evidence that brain supplements can be life changing to people all across the globe.

 

 

Sources:

http://www.ncbi.nlm.nih.gov/pubmed/21048709

Amino Acid: Glutamate in Stroke Treatment

Preventing brain damage after stroke is the primary goal for stroke treatment. Understanding the balance of brain chemicals—which include amino acids like glutamate (salt/ester of glutamic acid)—can help scientists develop new, successful treatments for stroke. 

Stroke is the second leading cause of death worldwide. This dangerous condition occurs when the supply of blood to the brain is disturbed. With ischemic strokes, blood supply is decreased (possibly by a blood clot), and rapidly leads to loss of brain function. Stroke can lead to permanent brain damage, when the neurons in the brain are destroyed.

Neurons are nerve cells which transmit information in our central nervous system, which includes our brain. Neuroprotection is the name for treatments which prevent, or slow, the progression of stroke by preventing the loss of neurons. It is also used to treat other central nervous system disorders, including neurodegenerative diseases, traumatic brain injury, and spinal cord injury.

Dr. Myron Ginsberg published an interesting review on ischemic stroke in Neuropharmacology. Dr. Ginsberg, from the Department of Neurology, University of Miami Miller School of Medicine, in Miami, Florida, covered many experimental neuroprotective treatments, including glutamate antagonism.

The role of glutamate role in treatment for stroke

The amino acid glutamate—sometimes known as or associated with glutamic acid—is one of our brain’s our main excitatory neurotransmitters. Glutamate is involved in cognitive functions such as learning and memory.  But with stroke, excess glutamate can accumulate in the brain. This allows calcium ions to enter the cells. This process is called excitotoxicity, and it causes neuron damage and brain cell death.

Glutamate and other excitatory amino acids interact with receptor-classes, such as N-methyl-D-aspartate (NMDA). Animal studies suggest that treatments which block NMDA receptors could be successful in preventing brain damage after stroke, but only with very early administration. Human trials have not yet been completed.

As further research continues into the role of neurotransmitting amino acids and stroke, it’s possible that a successful neuroprotective treatment using glutamate could be developed.

Sources:

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2631228/?report=classic

Phenylalanine for Pain Relief and Other Health Benefits

Phenylalanine is an essential amino acid, in which “essential” means you must get it through your diet or supplementation since your body cannot produce it on its own. Phenylalanine also is known as nature’s pain reliever. 

Interestingly, Phenylalanine is used in psychotropic drugs such as morphine, codeine, papaverine, and even mescaline because it is such an effective pain reliever.

Phenylalanine: How is it used in the body as a pain reliever?

Phenylalanine is one of the three aromatic amino acids, which include the other two, Tyrosine and Tryptophan. Phenylalanine is also the precursor for Tyrosine, and like Tyrosine, Phenylalanine is the precursor in the human body of catecholamines, which include dopamine, epinephrine, norepinephrine, and tryamine.

Dr. Winston Greene at DC Nutrition explains what catecholamines are and why we need phenylalanine, and how much: “Phenylalanine is a precursor of the neurotransmitters called catecholamines, which are adrenalin-like substances. … is highly concentrated in the human brain and plasma. … and requires biopterin, iron, niacin, vitamin B6, copper and vitamin C. An average adult ingests 5 g of phenylalanine per day and may optimally need up to 8 g daily.”

Phenylalanine essential amino acid comes from food and levels affect pain relief

You can get Phenylalanine from protein foods such as beef, chicken, fish, eggs, dairy products, and wheat germ. Dr. Greene shows that not only is this amino acid good as a pain reliever, but also that it is low in people who ingest caffeine. Interestingly, depressed people often seek out stimulants like caffeine drinks as a “pick me up” but may be doing themselves further harm since Dr. Greene says they’d found that “about 10 percent of depressed patients have low plasma Phenylalanine, and phenylalanine is an effective treatment in these cases.”

When someone gets an infection, however, Phenylalanine levels increase in the body to help aid any pain that might be associated with it, again acting as nature’s pain reliever. This amino is used in “premenstrual syndrome and Parkinson’s may enhance the effects of acupuncture and electric transcutaneous nerve stimulation (TENS). Phenylalanine and tyrosine, like L-dopa, produce a catecholamine effect. Phenylalanine is better absorbed than tyrosine and may cause fewer headaches.”

The bottom line is that Phenylalanine can be a great natural source for pain relief for numerous problems from infection to PMS to diseases such as Parkinsons. The health benefits are numerous, but always be sure to check with your doctor prior to any supplementation or changes to your diet when working to include this amazing amino acid for pain relief.

Reference:

http://www.biology.arizona.edu/biochemistry/problem_sets/aa/aromatic.html

http://www.dcnutrition.com/AminoAcids/Detail.CFM?

Can threonine-encoding alleles reduce triglyceride levels?

High levels of triglycerides and triglyceride-rich lipoproteins are significant risk factors for cardiovascular diseases. Prevention plans to lower risk include reducing dietary total and saturated fat, but since lifestyle and genetics also play significant roles in developing heart diseases, researchers at the University of Minnesota examined the genetic variations in fatty acid binding proteins and lipid metabolism. Fatty acid binding protein 2 (FABP2) relates absorption and transportation of long chain fatty acids in the intestine. At codon 54 of FABP2, a DNA variation occurs where amino acid alanine is substituted with threonine in the protein. 

This allele of threonine at codon 54 (Thr54) can transport a greater amount of fatty acids than alanine, across the intestine into the plasma. Recent studies have found that the threonine allele have higher fasting plasma triglycerides than alanine variants.

Researchers Steven McColley, Angeliki Georgopoulos, Lindsay Young, Mindy Kurzer, Bruce Redmon and Susan Raatz hypothesize that a high-fat diet would reduce triglyceride-rich lipoproteins (TRL) and the threonine-encoding allele (Thr54) would respond by changing the transportation rate. Lipoproteins are the biochemical compounds containing both proteins and lipids that help transport fat inside and outside cells. One of their main functions is to emulsify fat molecules.

The effect of threonine-encoding alleles on triglyceride-rich lipoproteins

For the crossover study, the researchers used 16 healthy postmenopausal women as participants. The participants would undergo three different 8-week isoenergetic diet treatments: high fat, low fat, and low fat plus n-3 fatty acids.

The high fat treatment consisted of a diet where 40% of energy consumed is fat, the low fat treatment consisted of a diet where 20% of energy consumed is fat, and the low-fat plus n-3 fatty acids consisted of a diet where 20% of energy consumed is fat plus 3% as omega-3 fatty acids.

The treatments were assigned in a random order with a regular diet given 6-12 weeks between conditions. Blood samples were collected throughout the process to evaluate triglyceride levels and DNA analysis.

After assessing the data, researchers McColley et al. found that carriers of the Thr54 allele had significantly lower plasma triglycerides, chylomicron triglycerides, very low density lipoprotein and chylomicron remnant triglycerides after taking part in a high-fat diet. Participants with the Ala54 allele (alanine) did not demonstrate significant changes from baseline with any of the diets.

Source:

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3156623/

Part 1: Eating Insects for Your Daily Amino Acids?

Pull up a chair and have a plate of bugs for breakfast?! Although this is not unrealistic or uncommon in most of the world, entomophagy (eating insects for food) brings a feeling of disgust for many in western societies, and a sourpuss face along with it! But eating insects is common to animals (insectivores), even other insects, as well as humans, and for good reasons.

Eating insects of many kinds brings to light the simple fact that they are full of protein and nutrition, and help sustain life. Vitamins, minerals, monounsaturated and polyunsaturated fats, oleic acid, and amino acids are only part of the full story.

In fact, bugs may wind up being a part of the human diet in the future, as it is currently in many countries, and has been prehistorically commonplace for hominids, hominins (human line), throughout time.

The big questions about eating insects include…

What amino acids are present in bugs and are they available to the human body? Exactly what nutritional content is covered for human requirements by consuming edible insects? Eating insects may be good for you, but do they taste good?

According to my daughter, who went to Peru with my mom and some friends and ate a large white grub that is a common to the area for consumption, it tasted lovely, just like an almond. She said, “It tasted good!” However, she also nearly gagged and spit it out. Why? The texture was “too mushy,” she said. The last thing she was thinking about was the amino acid content of the grub! *smiles*

Eating insects raw, such as her raw grub from Peru, are not always necessary. Most people around the world eat them raw as well as roasted, baked, smoked, fried, boiled in salted water, and dried or sun-dried. Of course, most Americans have heard of chocolate covered ants or grasshoppers as a delicacy dessert (or given as a joke, although is a serious meal in other countries). Each method of preparation makes eating insects a different experience, taste, texture, and can be the difference between it tasting good or wanting to spit it out on the ground from whence it came.

Who wants to eat bugs anyway? Lots of people, especially considering they are as easy to scavenge as they are to grow and raise for food, and is easier than gardening or raising small livestock. It is also cheaper than buying food at the grocery store, although bugs-on-a-stick (or loose) of many varieties can be purchased at local markets in many countries, like is often seen in China or Thailand.

The fact is that many grubs, larvae, grasshoppers, caterpillars, termites, palm weevils, mealworms, and other bugs are packed with nutrition such as potassium, calcium, sodium, magnesium, phosphorous, zinc, manganese, and copper according to the FAO. Eating insects can also supply you with necessary iron and amino acids like lysine, things that vegans and vegetarians are often deficient in.

CONTININUE READING Part 2: Eating Insects for Your Daily Amino Acids?

Reference:

http://link.springer.com/article/10.1007%2FBF00805837

http://www.organicvaluerecovery.com/studies/studies_nutrient_content_of_insects.htm

http://www.fao.org/docrep/018/i3253e/i3253e06.pdf

Asparagine is important for normal brain development

News-Medical.net — Asparagine, found in foods such as meat, eggs, and dairy products, was until now considered non-essential because it is produced naturally by the body. Researchers at the University of Montreal and its affiliated CHU Sainte-Justine Hospital found that the amino acid is essential for normal brain development. This is not the case for other organs. “

The cells of the body can do without it because they use asparagine provided through diet. Asparagine, however, is not well transported to the brain via the blood-brain barrier,” said senior co-author of the study Dr. Jacques Michaud, who found that brain cells depend on the local synthesis of asparagine to function properly. First co-author José-Mario Capo-Chichi and colleague Grant Mitchell also made major contributions to the study.

Glutamine Deprivation May Slow Pancreatic Cancer

Tumor growth in pancreatic cancer patients may be slowed using glutamine. Glutamine is an amino acid, which is one of the building blocks of proteins. Although it is typically considered a non-essential amino acid (meaning the body may make it on its own), glutamine is technically a conditionally essential amino acid. The term “essential” means that it must be gotten through the diet, so this amino acid is—in certain circumstances—acquired via intake of food.

Glutamine, which is the most abundant amino acid in the human body, plays a role in cancer tumor growth; so depriving the cancer cells of glutamine may hold the key to slowing the spread of cancer of the pancreas, a study shows.

Study on pancreatic tumor growth and glutamine

At the Division of Genomic Stability and DNA Repair, Department of Radiation Oncology (part of the Dana-Farber Cancer Institute) in Boston, Massachusetts, a group of researchers and doctors, J Son, CA Lyssiotis, et al., have investigated just how the amino acid glutamine is involved with the KRAS-regulated metabolic pathway, which is part of the cause of tumor growth within the pancreas itself.

The researchers studied the metabolism of cancer cells and glutamine dependencies since, unlike normal cells, the cells within cancer tumors maintain their own type of metabolism. They said that “an increased use of the amino acid glutamine to fuel anabolic processes. Indeed, the spectrum of glutamine-dependent tumors and the mechanisms whereby glutamine supports cancer metabolism remain areas of active investigation.”

Because human pancreatic cells use a non-standard pathway, which identifies ductal adenocarcinoma (PDAC) cells, most cells use “glutamate dehydrogenase (GLUD1) to convert glutamine-derived glutamate.” What this means is that the PDAC cells “are strongly dependent … as glutamine deprivation or genetic inhibition of any enzyme in this pathway leads to [a] series of reactions [that] results in a pronounced suppression of PDAC growth in vitro and in vivo.”

The scientists established that because the glutamine metabolism is reprogrammed and “mediated by oncogenic KRAS, the signature genetic alteration in PDAC [represses] key metabolic enzymes in this pathway.”

With the PDAC pathway and pancreatic cells being dispensable, the glutamine in normal cells then becomes a possible new therapeutic approach in treating pancreatic tumors in humans. Hopefully more will be forthcoming on this new technique in the near future.

Reference:

http://www.ncbi.nlm.nih.gov/pubmed/23535601

Chronic Liver Disease Shows Amino Acid-Sulphur Deficiency

Turns out that your liver can benefit from the sulphur-containing amino acids methionine and cysteine. Health benefits of amino acids such as these are excellent, but this is especially true for those with liver disease. As it turns out, those with chronic liver disease actually show a pattern of sulphur deficiency, so both cysteine and methionine may help with this.

Advanced liver disease and methionine / cysteine amino acids

In advanced or chronic liver disease, the metabolism of the sulphur-containing aminos, such as methionine and cysteine, are is impaired (no difference in the amino acid taurine, however).

In a study by P Almasio, G Bianchi, et al., at the Clinica Medica R, Università di Palermo, in Italy, the researchers published their discoveries based on 60 people who had chronic liver disease. The results show a pattern of amino acid deficiency in these patients.

10 of the subjects were used a control because they were healthy, but the other 50 patients had chronic liver disease, which was proven via biopsy.

The breakdown of their liver disease impairments

Hypermethioninemia (an extreme amount of methionine) was present in only these cases:

10 cases compensated cirrhosis
10 cases decompensated cirrhosis

Plus there were:

30 cases chronic hepatitis

The results of this clinical trial showed cysteine, a metabolite of methionine metabolism, was “markedly reduced in patients with compensated chronic liver disease, while in advanced cirrhosis its concentration was within the normal range.”

Methionine is an essential amino acid, which means you can only get it through diet, particularly protein foods such as meats (chicken, beef, pork, lamb, plus fish and eggs). Also, cysteine is a non-essential amino acid, which means the body can produce this amino acid on its own. No differences were observed (in plasma levels) for the amino acid taurine between groups.

What was observed was how sulfur-containing amino acid metabolism was deranged and “possibly located at various steps along the trans-sulphuration pathway, is also present in mild forms of chronic liver disease.”

What this means is that a key marker for those with chronic liver disease is that sulphur-containing amino acids are deficient. This can be true for people suffering from decompensated cirrhosis), or hepatitis.

The study did not explain whether supplementing intake with cysteine or methionine would affect the—chronic liver disease–patients in a positive way or not, but it is good to know that both of these amino acids are in ample amounts when associated with healthy livers, yet levels are abnormal in diseased livers.

Reference:

http://www.ncbi.nlm.nih.gov/pubmed/8025302

Prevent Prostate Cancer with Three Amino Acids?

Three specific amino acids may aid in the prevention of prostate cancer according to a study. The three aminos include methionine, phenylalanine, and tyrosine. During protein synthesis by the body, the amino acids tyrosine, methionine, and phenylalanine are utilized. Restriction of these amino acids depends on glucose metabolism, which when altered aids in cell death of cancer cells within human prostate cancer, and may aid in preventing prostate cancer.

Study linking amino acids and prostate cancer prevention

YM Fu, H Lin, et al., did a study at the Department of Pharmaceutical Sciences at Washington State University said that it is selective amino acid restriction of tyrosine and phenylalanine, plus methionine or glutamine that target mitochondria in cells that are linked to prostate cancer cell death.

Glucose metabolism modulation is tied to the process and “crucial switches connecting metabolism and these signaling molecules to cell survival during amino acid restriction” become target factors preventing prostate cancer, say the researchers.

Second study on prostate cancer and amino acids

Another study by YS Kim from Washington State University showed an identification of molecular targets regarding specific amino acid dependency and how it modulates specific kinds of prostate cancer cells. To find out how the amino acids can prevent prostate cancer, they investigated if restriction of tyrosine, phenylalanine, and methionine could inhibit the growth and metastasis of prostate cancer.

Kim progressed outward in this field of research because of the “underlying the anticancer activity of tyrosine/phenylalanine and methionine restriction. This is especially important research since there still is no satisfactory drug for treatment of androgen-independent, metastatic human prostate cancer.”

Even though further research is needed regarding the amino acids phenylalanine, tyrosine, and methionine for prostate cancer prevention, it has expanded avenues for antimetastatic, anti-invasive, apoptosis-based therapies for the preventing prostate cancer.

Prostate cancer, being one of the major cancers that kill men in the North American continent, is the reason why males should be regularly screened for this deadly disease.

Reference:

http://www.ncbi.nlm.nih.gov/pubmed/20432447

http://prevention.cancer.gov/funding/recently-funded/ca04004/1R01CA101035-01A1