Amino Acid Deficiency (Essential)

What Are Essential Amino Acids?

[dropcap]A[/dropcap]mino acids are small molecules, or subunits, that link together in various combinations to make up big, complicated proteins. As such, amino acids are commonly referred to as “the building blocks” of proteins.

Q: How many amino acids are used in our body?

A: There are 20 amino acids that are used within our body to synthesize or produce our unique human proteins.  Of these amino acids,  9 are termed essential, meaning our bodies require them to live but cannot make them. Therefore, the essential amino acids must come from the food we eat, whether from plant or animal sources.

The essential amino acids include histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, and valine.

What Is Deficiency Of Essential Amino Acids In Celiac Disease and/or Gluten Sensitivity?

• Relationship between essential amino acid deficiency and metabolic needs of the body. Essential amino acid deficiency results when the level within cells is too low to meet metabolic needs of the body.

• Relationship between essential amino acid deficiency and celiac disease. Deficiency of essential amino acids is a classic symptom of celiac disease characterized by these  health effects:

1. Impaired growth and repair of body tissues,
2. Impaired maintenance of osmotic pressure in blood vessels needed to prevent leakage of fluid from blood vessels (edema),
3. Impaired performance as a carrier for many substances in the blood, and
4. Impaired neurotransmitter production and function.¹

• Relationship between essential amino acids and deficiency. Deficiency of any essential amino acid results in inefficient utilization of others. For example, the blood protein albumin, which is a marker of malnutrition, can illustrate the limiting effect of even a single amino acid deficiency on protein production that requires its presence. Albumin is formed in the liver using 585 amino acids in various sequences.

How Prevalent Is Deficiency of Essential Amino Acids In Celiac Disease and/or Gluten Sensitivity?

Essential amino acid deficiency is common in patients with untreated celiac disease.²

What Are The Symptoms Of Essential Amino Acid Deficiency?

Symptoms of essential amino acid deficiency in general include¹:

• Abdominal distention from edema – [histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, and valine].
• Agitation- [tryptophan, methionine].
• Anemia – [histidine].
• Anxiety – [tryptophan, methionine].
• Apathy- [phenylalanine].
• Appetite loss – [lysine].
• Arthritis – [histidine].
• Bloodshot eyes- [lysine].
• Bone loss – [lysine].
• Chapped lips – [lysine].
• Depression – [tryptophan, methionine].
• Dermatitis- [lysine].
• Diminished intellect – [methionine].
• Discoloration of hair (black or brown turns reddish) – [tyrosine].
• Dizziness – [lysine].
• Edema (puffiness) –  [histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, and valine as components of albumin].
• Fatigue – [isoleucine, lysine, leucine, threonine, valine].
• Flaky skin- [lysine].
• Impaired growth in children – [lysine, histadine, tryptophan, valine].
• Infertility – [lysine].
• Insomnia- [tryptophan].
• Hunger – [all].
• Nausea – [lysine].
• Paleness – [lysine].
• Poor muscle tone – [lysine].
• Susceptibility to infection – [leucine].
• Thinning hair – [methionine].
• Wasting of subcutaneous fat and muscle – [leucine, lysine].
• Weak bones leading to osteoporosis – [lysine].
• Weak teeth – [lysine].
• Weak tendons and ligaments leading to easy tears and injury – [lysine].
• Weakness – [ isoleucine, leucine, lysine, threonine].
• Weight loss – [histidine, leucine, lysine].

How Does The Body Get Essential Amino Acids?

• Essential amino acids must be obtained from food containing protein. In the small intestine, food proteins are broken down into small units called peptides by protease enzymes secreted by the pancreas.
• Peptides are then completely broken down into their constituent amino acids in the intestinal lining itself by enzymes called dipeptidases. Dipeptidase splits a double molecule peptide to yield 2 amino acids.
• Only amino acids from food, not proteins or parts of proteins (peptides), can be properly used by the body to build human proteins. Unfortunately, peptides that are able to pass through an abnormally “leaky gut,” such as in celiac disease, become foreign substances that may provoke  immune responses to them.

What Do Essential Amino Acids Do In The Body?

Histidine is required for protein production, tissue growth and repair, and in infants and young children, optimal growth.

• Histidine is the binding site for hemoglobin.
• It binds zinc in signaling proteins and regulates other essential trace elements including iron, copper, manganese, and molybdenum.
• It is also essential in forming the powerful antioxidant, super oxide dismutase, and other enzymes and compounds that involve metals.
• In another metal activity, histadine is required for the formation of metallothionein. Metallothionein is a compound that removes toxic metals such as mercury and cadmium from the body.
• Histidine is a precursor for synthesizing histamine which is a compound released by mast cells to cause inflammation when tissue is injured or in allergic and inflammatory reactions, to cause dilation of small blood vessels and smooth muscle contraction.³

Isoleucine is used to produce both glucose and ketones for energy and is required for muscle metabolism, for optimal growth in infants, and for nitrogen balance in adults.

• The vitamin biotin is required for the full and necessary breakdown of isoleucine.

Leucine is required for protein production, particularly muscle protein synthesis, and normal growth and metabolism. Leucine also inhibits the destruction of muscle proteins with consequent increased balance over time.⁴

• Leucine is a branched amino acid that works best when the other branched amino acids, isoleucine and valine, are optimally present.⁴
• The vitamin biotin is required for the full and necessary breakdown of leucine.

Lysine is required for normal growth.

• Lysine plays an essential role in the production of carnitine, an amino acid responsible for converting fatty acids into energy and helping to lower cholesterol.
• Lysine helps the body absorb calcium and decreases the amount of calcium that is lost in urine which in turn reduces the loss of bone causing osteoporosis.
• Lysine is needed to produce collagen, a protein that is the living tissue in bones and connective tissues including skin, tendon, and cartilage.
• Lysine is shown to have anti-seizure activity.
• Lysine reduces viral outbreaks of cold sores and genital herpes.

Methionine is an anti-oxidant and source of sulfur for the body such as for making collagen tissue for healthy skin, nails and hair.

• Methionine is required to make homocysteine, a transient amino acid in blood, and also for conversion to S-adenosylmethionine (SAM) a naturally-occurring compound found in almost every tissue and fluid in the body. It is involved in many important processes. SAMe plays a role in the immune system, maintains cell membranes, and helps produce and break down brain chemicals, such as serotonin, melatonin, and dopamine. It works with vitamin B12 and folate (vitamin B9). Being deficient in either vitamin B12 or folate may reduce levels of SAMe in your body.⁵
• Methionine is used in the process of detoxification to produce cysteine for the ultimate production of the body’s main detoxifier, glutathione. Glutathione is made in every cell from cysteine, glutamic acid and glycine.
• Methionine increases the levels of other amino acids that play important roles in immune function such as glutathione and taurine.
• Methionine helps to absorb the essential minerals selenium and zinc from the small intestine into the body.

Threonine is required in energy metabolism for conversion of glucose to pyruvate via the enzyme threonine dehydrogenase.

Tryptophan is required for normal growth and development, and for conversion to the brain chemicals serotonin/melatonin and to the vitamin niacin (vitamin B3).

Valine is required for protein synthesis, muscle metabolism, and in infants, normal growth.¹

How Does Essential Amino Acid Deficiency Develop In Celiac Disease and/or Gluten Sensitivity?

• Essential amino acid deficiency results from protein maldigestion due to inadequate enzyme digestion required to break off, or yield, amino acid molecules, and
• Malabsorption by damaged and inflamed/swollen villi due to immune reponse to gluten.
• Stress and chronic inflammation are added factors that increase the need for amino acids such as histadine and lysine.

Does Essential Amino Acid Deficiency Respond To Gluten-Free Diet?

Yes. Celiac disease-related amino acid deficiency quickly responds to a strict gluten free diet that contains needed amino acids.

6 Steps To Correct Essential Amino Acid Deficiency:

• [dropcap]1[/dropcap]Meet, or Exceed the RDA (Recommended Dietary Allowances) for the Essential Amino Acids per day:

[box type=”success” ]0.8 grams per kilogram of body weight for healthy adults which is 10% to 15% of daily energy intake. One gram of protein provides 4 calories of energy. If the diet contains 2000 calories then the protein portion should be at least 200 calories which is 50 grams. [/box]

• [dropcap]2[/dropcap]Diet – Include Food Sources Richest in the Essential Amino Acids  :

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Animal Sources:

Proteins from animal sources, such as meat, poultry, fish, eggs, milk, cheese, and yogurt, provide all 9 indispensable amino acids in adequate amounts. Note: Meat preparation using moist heat and acids like vinegar and lemon juice as marinade break down fibers and so help digestion.

Plant Sources:

Proteins from plants tend to be deficient in one or more of the indispensable amino acids.

Rich plant sources of protein include tree nuts, soybeans, peanuts, legumes, and seeds.¹ Keep veggies and nuts sealed and away from light.

Specific examples. Histidine is rich in rice, buckwheat, corn, potatoes, cauliflower, mushrooms, cantaloupe, bananas, and citrus fruits. Isoleucine is also rich in seaweed. Leucine is rich in milk, chicken, fish, cottage cheese, lentils, sesame, and peanuts. Threonine is rich in lentils and sesame seeds. Lysine is rich in spirulina, fenugreek seed, milk and cheeses, eggs, meat, mango, beans, squash, peas, and lentils. Tryptophan is rich in spirulina, sunflower seeds, and chocolate.[/box]

• [dropcap]3[/dropcap] Diet – Avoid  or Limit These Foods That Deplete or Interfere With Absorption:

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• Excessive fiber foods, such as seeds and whole grains, bind proteins when eaten together.
• Lactose in milk when heated binds lysine.
• Non-heated soybeans contain an enzyme (trypsinase) that interferes with protein digestion by trypsin.

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• [dropcap]4[/dropcap]Monitor Medications That Deplete or Interfere With Absorption:

Ask your doctor or pharmacist about possible interactions between amino acid supplements and medications you’re taking.

[box type=”shadow” ] Here are common medications that deplete amino acids. Ask your doctor or pharmacist about this possible adverse effect if you are taking any of the drugs listed below. Do not stop prescribed medications without supervision. This is not a complete listing.

• Beta blockers (Inderol®, Lopressor®, Corgard®, Atenolol®).[/box]

• [dropcap]5[/dropcap]Manage Nutritional Supplements to Obtain Essential Amino Acids :

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• Amino acids are readily sold without a prescription individually in tablet, capsule, powder and liquid form and can be included in a mix of various types.

Caution: Persons prescribed a low protein diet, such as those with kidney disease, should discuss taking amino acid supplements with their treating physician.

Excessive amino acids can be harmful when not needed and put an unecessary burden on the liver and kidneys. When the body has what it needs, the liver works to remove the nitrogen molecules from extra amino acids. The nitrogen is excretely mainly through the urine by the kidneys, while the rest of the molecule is used for energy or stored. This is an expensive way to get energy that should be coming from carbohydrates and fats.[/box]

• [dropcap]6[/dropcap]Other Supplements That Deplete or Interfere With Absorption:

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• Check with your pharmacist.

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Medical Research Findings On Amino Acid Deficiency In Celiac Disease and/or Gluten Sensitivity:

RESEARCH STUDY SUMMARIES

“Amino acid and peptide absorption in patients with celiac disease and dermatitis herpetiformis.” This small early study investigating absorption of dietary protein in patients with celiac disease and dermatitis herpetiformis showed that malabsorption of dietary protein is unlikely to occur in dermatitis herpetiformis but may occur and contribute to protein deficiency seen in some severe cases of adult celiac disease.

A double-lumen perfusion technique was used to study amino acid and peptide absorption in 8 normal control subjects, 13 patients with untreated adult celiac disease, and 16 patients with dermatitis herpetiformis who had varying morphological abnormalities of the small bowel. All subjects were perfused with isotonic solutions containing 10 mM glycyl-L-alanine and 10 mM glycine + 10 mM L-alanine.

Patients with adult celiac disease had impaired absorption of glycine (p < 0.01) and L-alanine (p < 0.05) from the amino acid solution compared with the control subjects. Amino acid uptake from the dipeptide solution was not significantly impaired, although four individual patients had impaired uptake of both amino acids. In contrast to these findings, very few patients with dermatitis herpetiformis had impaired amino acid absorption from either solution.

Sodium absorption was impaired from both solutions when the groups of patients with adult coeliac disease and dermatitis herpetiformis with subtotal villous atrophy and partial villous atrophy were studied, and there were patients in each group who secreted sodium and water. The impairment of sodium and water absorption provides evidence that there may be functional impairment of the jejunal mucosa in dermatitis herpetiformis as well as in adult celiac disease.⁶

“Long-term follow-up of celiac adults on gluten-free diet: prevalence and correlates of intestinal damage.” This study reporting data on long-term control of celiac disease and its correlates demonstrated that celiac disease is often poorly controlled in the majority of patients on long-term treatment with a Gluten Free Diet due to lack of adherence to strict gluten free diet. Intestinal damage at follow-up was absent in only 43.6% and EMA were present in the serum of 24.9%.

In patients with noncontrolled celiac disease, albumin protein level in long-term treatment was low and/or lower than pretreatment and correlated with the presence of intestinal damage.⁷

Sources:

1. Kathleen Mahan and Sylvia Escott-Stump, ed. Krause’s Food, Nutrition & Diet Therapy, 10th Edition. Philadelphia, PA. USA: W.B. Saunders Company, 2000. [↩] [↩] [↩] [↩]
2. Murray JA, the widening spectrum of celiac disease. American Journal of Clinical Nutrition. Mar 1999; 69(3):354-365. [↩]
3. Dictionary.com [↩]
4. Rondanelli M, Faliva M, Monteferrario F, Peroni G, Repaci E, Allieri F, Perna S. Novel insights on nutrient management of sarcopenia in elderly. Biomed Res Int. 2015;2015:524948. doi: 10.1155/2015/524948. Epub 2015 Jan 29. [↩] [↩]
5. https://umm.edu/health/medical/altmed/supplement/sadenosylmethionine [↩]
6. Silk DB, Kumar PJ, Perrett D, Clark ML, Dawson AM. Amino acid and peptide absorption in patients with coeliac disease and dermatitis herpetiformis. Gut. 1974 Jan;15(1):1-8. [↩]
7. Ciacci C, Cirillo M, Cavallaro R, Mazzacca G. Long-term follow-up of celiac adults on gluten-free diet: prevalence and correlates of intestinal damage. Digestion. 2002;66(3):178-85. [↩]