EPI LIFE COACH articles

Betaine is a derivative of the nutrient choline; in other words, choline is a “precursor” to betaine and must be present for betaine to be synthesized in the human body.
YEAR 2017
DATE Friday, March 03
TOPIC Vitamins
AUTHOR Dr. Carlos Orozco (BSc, MSc, ND, MD, PhD, FPAMS)

Betaine is a derivative of the nutrient choline; in other words, choline is a “precursor” to betaine and must be present for betaine to be synthesized in the human body. Betaine is created by choline in combination with three methyl radicals and glycine, an aminoacid. Therefore, Betaine is known as trimethylglycine (TMG) and the human body is able to synthesized it. It’s involved in liver function, cellular reproduction, and helping make carnitine. It also helps the body metabolize an amino acid called homocysteine.
Just like some B vitamins, including folate andvitamin B12, betaine is considered to be a “methyl donor.” This means it aids in liver function, detoxification and cellular functioning within the body. It’s most crucial role is to help the body process fats.

Probably the most extensively researched benefit of betaine is its use to convert homocysteine in the blood to methionine. Homocysteine is an amino acid that is produced by the body naturally. Amino acids are the building blocks of all the proteins in the body. Although amino acids are critical compounds needed for many body functions, studies show that high levels of the amino acid homocysteine can be harmful to blood vessels, potentially leading to the development of plaque buildup and the condition called atherosclerosis (clogged arteries).(1) (2)

Betaine Deficiency
A betaine deficiency is not thought to be common in western nations, mostly because betaine is present in high amounts in wheat products, which are a staple in most people’s diets. Although it’s not directly due to low betaine intake, diets low in betaine may contribute to high homocysteine in the blood. High homocysteine levels in the blood may be elevated for many reasons, mainly epigeneticsdue to environmental factors, diet and life style.

The biggest threat to consuming low betaine levels is experiencing symptoms related to high homocysteine in the blood. This is seen most often in either older populations above 50, those who have suffered from alcoholism, or in children who have genetic conditions that lead to high homocysteine. Although this condition is rare, severely elevated levels of homocysteine can cause developmental delay, osteoporosis (thin bones), visual abnormalities, formation of blood clots, and narrowing and hardening of blood vessels. (3)

References:

  1. Alfthan G, Tapani K, Nissinen K, et al. (2004) The effect of low doses of betaine on plasma homocysteine in healthy volunteers. Br J Nutr.92:665-669.
  2. Atkinson W, Elmslie J, Lever M, Chambers ST, George PM (2008). Dietary and supplementary betaine: acute effects on plasma betaine and homocysteine concentrations under standard and postmethionine load conditions in healthy male subjects. Am J ClinNutr87(3):577-585.
  3. Angulo P, Lindor KD. Treatment of nonalcoholic fatty liver: present and emerging therapies. Semin Liver Dis. 2001;21(1):81-88.
  4. Barak AJ, Beckenhauer HC, Badkhsh S, Tuma DJ. The effect of betaine in reversing alcoholic steatosis. Alcohol ClinExp Res. 1997;21(6):1100-1102.
  5. Barak AJ, Beckenhauer HC, Tuma DJ. (1995) Betaine, ethanol, and the liver: a review. Alcohol. 1996; 13(4): 395-398.
  6. Boushey CJ, et al. A quantitative assessment of plasma homocysteine as a risk factor for vascular disease. Probable benefits of increasing folic acid intakes. JAMA. Oct 4,; 274(13): 1049-1057.
  7. Eikelboom JW, Lonn E, Genest J, Hankey G, Yusuf S. Homocyst(e)ine and cardiovascular disease: a critical review of the epidemiologic evidence. Ann Intern Med. 1999;131:363-375.
  8. Hanje AJ, Fortune B, Song M, Hill D, McClain C. The use of selected nutrition supplements and complementary and alternative medicine in liver disease. NutrClinPract. 2006 Jun;21(3):255-272. Review.

EPI LIFE COACH articles

Vitamin C is required for the synthesis of collagen, an important structural component of blood vessels, tendons, ligaments, and bone. Vitamin C also plays an important role in the synthesis of the neurotransmitter, norepinephrine.
YEAR 2017
DATE Friday, March 03
TOPIC Vitamin
AUTHOR Dr. Carlos Orozco (BSc, MSc, ND, MD, PhD, FPAMS)

Vitamin C, also known as ascorbic acid, is a water-soluble vitamin. Unlike most mammals, humans do not have the ability to make their own vitamin C. Therefore, we must obtain vitamin C through our diet.

Biological Function
Vitamin C is required for the synthesis of collagen, an important structural component of blood vessels, tendons, ligaments, and bone. Vitamin C also plays an important role in the synthesis of the neurotransmitter, norepinephrine. Neurotransmitters are critical to brain function and are known to affect mood. In addition, vitamin C is required for the synthesis of carnitine, a small molecule that is essential for the transport of fat to cellular organelles called mitochondria, for conversion to energy (1). Recent research also suggests that vitamin C is involved in the metabolism of cholesterol to bile acids, which may have implications for blood cholesterol levels and the incidence of gallstones (2).
Vitamin C is also a highly effective antioxidant. Even in small amounts vitamin C can protect indispensable molecules in the body, such as proteins, lipids (fats), carbohydrates, and nucleic acids (DNA RNA) from damage by free radicals and reactive oxygen species that can be generated during normal metabolism as well as through exposure to toxins and
pollutants (e.g. smoking). Vitamin C may also be able to regenerate other antioxidants such as vitamin E (1).

Signs and Symptoms of Deficiency
Scurvy
Severe vitamin C deficiency has been known for many centuries as the potentially fatal disease, scurvy. By the late 1700’s the British navy was aware that scurvy could be cured by eating oranges or lemons, even though vitamin C would not be isolated until the early 1930’s. Symptoms of scurvy include bleeding and bruising easily, hair and tooth loss, joint pain and swelling. Such symptoms appear to be related to the weakening of blood vessels, connective tissue, and bone, which contain collagen. Early symptoms of scurvy such as fatigue may result from diminished levels of carnitine, needed to derive energy from fat, or decreased synthesis of the neurotransmitter norepinephrine (see Function). Scurvy is rare in developed countries because it can be prevented by as little as 10 mg of vitamin C daily (2). However, recent cases have occurred in children and the elderly on very restricted diets (4,5).

References:

  1. Brody T. Nutritional Biochemistry. 2nd ed. San Diego: Academic Press; 1999.
  2. Shane B. Folic acid, vitamin B-12, and vitamin B-6. In: Stipanuk M, ed. Biochemical and Physiological Aspects of Human Nutrition. Philadelphia: W.B. Saunders Co.; 2000:483-518.
  3. Baik HW, Russell RM. Vitamin B12 deficiency in the elderly. Annu Rev Nutr. 1999;19:357-377. (PubMed).
  4. Herbert V. Vitamin B-12. In: Ziegler EE, Filer LJ, eds. Present Knowledge in Nutrition. 7th ed. WashingtonD.C.: ILSI Press; 1996:191-205.
  5. Food and Nutrition Board, Institute of Medicine. Vitamin B12. Dietary Reference Intakes: Thiamin, Riboflavin, Niacin, Vitamin B-6, Vitamin B-12, Pantothenic Acid, Biotin, and Choline.
  6. WashingtonD.C.: NationalAcademy Press; 1998:306-356. (National Academy Press).
  7. Ho C, Kauwell GP, Bailey LB. Practitioners’ guide to meeting the vitamin B-12 recommended dietary allowance for people aged 51 years and older. J Am Diet Assoc. 1999;99(6):725-727. (PubMed).
  8. Weir DG, Scott JM. Vitamin B-12 “Cobalamin”. In: Shils M, ed. Nutrition in Health and Disease. 9th ed. Baltimore: Williams & Wilkins; 1999:447-458.
  9. Homocysteine Lowering Trialists’ Collaboration. Lowering blood homocysteine with folic acid based supplements: meta-analysis of randomised trials. Homocysteine Lowering Trialists’ Collaboration. BMJ. 1998;316(7135):894-898. (PubMed).
  10. Quinlivan EP, McPartlin J, McNulty H, et al. Importance of both folic acid and vitamin B12 in reduction of risk of vascular disease. Lancet. 2002;359(9302):227-228. (PubMed).
  11. Stabler SP, Lindenbaum J, Allen RH. Vitamin B-12 deficiency in the elderly: current dilemmas. Am J ClinNutr. 1997;66(4):741-749. (PubMed).
  12. Fenech M. Micronucleus frequency in human lymphocytes is related to plasma vitamin B12 and homocysteine. Mutat Res. 1999;428(1-2):299-304. (PubMed).
  13. Wu K, Helzlsouer KJ, Comstock GW, Hoffman SC, Nadeau MR, Selhub J. A prospective study on folate, B12, and pyridoxal 5′-phosphate (B6) and breast cancer. Cancer Epidemiol Biomarkers Prev. 1999;8(3):209-217. (PubMed).
  14. Eskes TK. Open or closed? A world of difference: a history of homocysteine research. Nutr Rev. 1998;56(8):236-244. (PubMed).
  15. Mills JL, Scott JM, Kirke PN, et al. Homocysteine and neural tube defects. J Nutr. 1996;126(3):756S-760S. (PubMed).

EPI LIFE COACH articles

This vitamin must be hydrolyzed from protein in order to be active. Hydrolysis occurs in the stomach by gastric acids or the intestines by trypsin digestion following consumption of animal meat.
YEAR 2017
DATE Friday, March 03
TOPIC Vitamins
AUTHOR Dr. Carlos Orozco (BSc, MSc, ND, MD, PhD, FPAMS)

Cobalamin is more commonly known as vitamin B12. Vitamin B12 is composed of a complex tetrapyrrol ring structure (corrin ring) and a cobalt ion in the center. Vitamin B12 is synthesized exclusively by microorganisms and is found in the liver of animals bound to protein as methycobalamin or 5′-deoxyadenosylcobalamin.

Ciano covalamine
The vitamin must be hydrolyzed from protein in order to be active. Hydrolysis occurs in the stomach by gastric acids or the intestines by trypsin digestion following consumption of animal meat. The vitamin is then bound by intrinsic factor, a protein secreted by parietal cells of the stomach, and carried to the ileum where it is absorbed. Following absorption the vitamin is transported to the liver in the blood bound to transcobalamin II.

Biological Function of Vitamin B12
Vitamin B12 plays a major role in the biosynthesis of nucleic acids, DNA, protein and blood cells, the maintenance of the bone marrow, the gut mucosa, epithelial cells and lipids, the myelination of nerve and brain fibers.

Vitamin B12 and Homocysteine Metabolism S-adenosylhomocysteine is formed during S-adenosylmethionine-dependent methylation reactions, and the hydrolysis of S-adenosylhomocysteine results in homocysteine. Homocysteine may be remethylated to form methionine by a folate-dependent reaction that is catalyzed by methionine synthase, a vitamin B12-dependent enzyme. Alternately, homocysteine may be metabolized to cysteine in reactions catalyzed by two vitamin B6-dependent enzymes.

Signs, symptoms, and health problems associated with vitamin B12 deficiency
Deficiency of vitamin B12 occurs as a result of an inability to absorb vitamin B12 from food and also occurs in strict vegetarians who do not consume any foods that come from animals [9]. As a general rule, most individuals who develop a vitamin B12 deficiency have an underlying stomach or intestinal disorder that limits the absorption of vitamin B12 [10]. Sometimes the only symptom of these intestinal disorders is subtly reduced cognitive function resulting from early vitamin B12 deficiency. Anemia and dementia follow later [1,11].

Characteristic signs and symptoms include anemia, fatigue, weakness, constipation, loss of appetite, and weight loss [1,3,12].
Deficiency also can lead to neurological changes such as numbness and tingling in the hands and feet [7,13].
Additional symptoms of vitamin B12 deficiency are difficulty in maintaining balance, depression, confusion, dementia, poor memory, and soreness of the mouth or tongue [14].
Signs of vitamin B12 deficiency in infancy include failure to thrive, movement disorders, delayed development, and megaloblasticanemia (15).

EPI LIFE COACH articles

Biotin is a water-soluble vitamin, generally classified as a B-complex vitamin. After the initial discovery of biotin, nearly forty years of research were required to establish it as a vitamin.
YEAR 2017
DATE Friday, March 03
TOPIC Vitamins
AUTHOR Dr. Carlos Orozco (BSc, MSc, ND, MD, PhD, FPAMS)

Biotin is a water-soluble vitamin, generally classified as a B-complex vitamin. After the initial discovery of biotin, nearly forty years of research were required to establish it as a vitamin (1). Biotin is required by all organisms but can only be synthesized by bacteria, yeasts, molds, algae, and some plant species (2).

Biological Function
In its physiologically active form biotin is attached at the active site of four important enzymes, known as carboxylases (3). Each carboxylase catalyzes an essential metabolic reaction.

Enzyme cofactor
Acetyl-CoA carboxylase catalyzes the binding of bicarbonate to acetyl-CoA to form malonyl-CoA. Malonyl-CoA is required for the synthesis of fatty acids.
Pyruvate carboxylase is a critical enzyme in gluconeogenesis, the formation of glucose from sources other than carbohydrates, for example, amino acids and fats.
Methylcrotonyl-CoA carboxyla se catalyzes an essential step in the metabolism of leucine, an indispensable (essential) amino acid.
Propionyl-CoA carboxylase catalyzes essential steps in the metabolism of amino acids, cholesterol, and odd chain fatty acids (fatty acids with an odd number of carbon molecules) (4).

Histone biotinylation
Histones are proteins that bind to DNA and package it into compact structures to form chromosomes. The compact packaging of DNA must be relaxed somewhat for DNA replication and transcription to occur. Modification of histones through the attachment of acetyl or methyl groups (acetylation or methylation) has been shown to affect the structure of histones, thereby affecting replication and transcription of DNA. The attachment of biotin to another molecule, such as a protein, is known as “biotinylation”. The enzyme biotinidase has recently been shown to catalyze the biotinylation of histones, suggesting that biotin may play a role in DNA replication and transcription (5,6).

Signs and Symptoms of Deficiency
Although biotin deficiency is very rare, the human requirement for dietary biotin has been demonstrated in two different situations: prolonged intravenous feeding without biotin supplementation and consumption of raw egg white for a prolonged period (many weeks to years). Avidin is a protein found in egg white, which binds biotin and prevents its absorption. Cooking egg white denatures avidin, rendering it susceptible to digestion, and unable to prevent the absorption of dietary biotin (7).

Symptoms of overt biotin deficiency include hair loss and a scaly red rash around the eyes, nose, mouth, and genital area. Neurologic symptoms in adults have included depression, lethargy, hallucination, and numbness and tingling of the extremities. The characteristic facial rash, together with an unusual facial fat distribution, have been termed the “biotin deficient face” by some experts (7). Individuals with hereditary disorders of biotin metabolism resulting in functional biotin deficiency have evidence of impaired immune system function, including increased susceptibility to bacterial and fungal infections (8).

References:

  1. Food and Nutrition Board, Institute of Medicine. Biotin. Dietary Reference Intakes: Thiamin, Riboflavin, Niacin, Vitamin B-6, Vitamin B-12, Pantothenic Acid, Biotin, and Choline. Washington, D.C.: NationalAcademy Press; 1998:374-389. (National Academy Press).
  2. Mock DM. Biotin. In: Ziegler EE, Filer LJ, eds. Present Knowledge in Nutrition. 7th ed. WashingtonD.C.: ILSI Press; 1996:220-236.
  3. Chapman-Smith A, Cronan JE, Jr. Molecular biology of biotin attachment to proteins. J Nutr. 1999;129(2S Suppl):477S-484S. (PubMed).
  4. Zempleni J, Mock DM. Biotin biochemistry and human requirements. 1999; volume 10: pages 128-138. J Nutr. Biochem. 1999;10:128-138.
  5. Hymes J, Wolf B. Human biotinidase isn’t just for recycling biotin. J Nutr. 1999;129(2S Suppl):485S-489S. (PubMed).
  6. Zempleni J, Mock DM. Marginal biotin deficiency is teratogenic. ProcSocExpBiol Med. 2000;223(1):14-21. (PubMed).
  7. Mock DM. Biotin. In: Shils M, Olson JA, Shike M, Ross AC, eds. Nutrition in Health and Disease. 9th ed. Baltimore: Williams & Wilkins; 1999:459-466.
  8. Baumgartner ER, Suormala T. Inherited defects of biotin metabolism. Biofactors. 1999;10(2-3):287-290.

EPI LIFE COACH articles

Folate coenzymes act as acceptors and donors of one-carbon units in a variety of reactions critical to the metabolism of nucleic acids and amino acids.
YEAR 2017
DATE Friday, March 03
TOPIC Vitamins
AUTHOR Dr. Carlos Orozco (BSc, MSc, ND, MD, PhD, FPAMS)

Biological Function of Folic Acid
One-carbon metabolism
The only function of folate coenzymes in the body appears to be mediating the transfer of one-carbon units (2). Folate coenzymes act as acceptors and donors of one-carbon units in a variety of reactions critical to the metabolism of nucleic acids and amino acids (3).

Nucleic acid metabolism
Folate coenzymes play a vital role in DNA metabolism through two different pathways.1) The synthesis of DNA from its precursors is dependent on folate coenzymes. 2) A folate coenzyme is required for the synthesis of methionine, and methionine is required for the synthesis of S-adenosylmethionine (SAM). SAM is a methyl group (one-carbon unit) donor used in many biological methylation reactions, including the methylation of a number of sites within DNA and RNA. Methylation of DNA may be important in cancer prevention.

Amino acid metabolism
Folate coenzymes are required for the metabolism of several important amino acids. The synthesis of methionine from homocysteine requires a folate coenzyme as well as a vitamin B12 dependent enzyme. Thus, folate deficiency can result in decreased synthesis of methionine and a build up of homocysteine. Increased levels of homocysteine may be a risk factor for heart disease, as well as several other chronic diseases.

Signs and Symptoms of Deficiency
Folate deficiency occurs in a number of situations. For example, low dietary intake and diminished absorption, as in alcoholism, can result in a decreased supply of folate. Certain conditions like pregnancy or cancer result in increased rates of cell division and metabolism, leading to an increase in the body’s demand for folate (5). Several medications may also contribute to deficiency.

References:

  1. Food and Nutrition Board, Institute of Medicine. Folic Acid. Dietary Reference Intakes: Thiamin, Riboflavin, Niacin, Vitamin B-6, Vitamin B-12, Pantothenic Acid, Biotin, and Choline. Washington, D.C.: NationalAcademy Press; 1998:193-305. (National Academy Press).
  2. Choi SW, Mason JB. Folate and carcinogenesis: an integrated scheme. J Nutr. 2000;130(2):129-132. (PubMed).
  3. Bailey LB, Gregory JF, 3rd. Folate metabolism and requirements. J Nutr. 1999;129(4):779-782. (PubMed).
  4. Gerhard GT, Duell PB. Homocysteine and atherosclerosis. CurrOpinLipidol. 1999;10(5):417-428. (PubMed).
  5. Herbert V. Folic acid. In: Shils M, Olson JA, Shike M, Ross AC, eds. Nutrition in Health and Disease. 9th ed. Baltimore:

EPI LIFE COACH articles

The terms folic acid and folate are often used interchangeably for this water-soluble B-complex vitamin.
YEAR 2017
DATE Friday, March 03
TOPIC Vitamins
AUTHOR Dr. Carlos Orozco (BSc, MSc, ND, MD, PhD, FPAMS)

The terms folic acid and folate are often used interchangeably for this water-soluble B-complex vitamin. Folic acid, the most stable form, occurs rarely in foods or the human body, but is the form most often used in vitamin supplements and fortified foods. Naturally occurring folates exist in many chemical forms. Folates are found in foods as well as in metabolically active forms, in the human body (1). In the following discussion forms found in food or the body will be referred to as “folates”, while the form found in supplements or fortified foods will be referred to as “folic acid”.

EPI LIFE COACH articles

Vitamin B6 must be obtained from the diet because humans cannot synthesize it, and the coenzyme, PLP plays a vital role in the function of approximately 100 enzymes that catalyze essential chemical reactions in the human body.
YEAR 2017
DATE Friday, March 03
TOPIC Vitamins
AUTHOR Dr. Carlos Orozco (BSc, MSc, ND, MD, PhD, FPAMS)

Vitamin B6 is a water-soluble vitamin that exists in three major chemical forms: pyridoxine, pyridoxal, and pyridoxamine [1,2].
Pyridoxal, pyridoxamine and pyridoxine are collectively known as vitamin B6. All three compounds are efficiently converted to the biologically active form of vitamin B6, pyridoxal phosphate. This conversion is catalyzed by the ATP requiring enzyme, pyridoxal kinase.
Pyridoxal phosphate functions as a cofactor in enzymes involved in transamination reactions required for the synthesis and catabolism of the amino acids as well as in glycogenolysis as a cofactor for glycogen phosphorylase.

Biological Function of Vitamin B6
Vitamin B6 must be obtained from the diet because humans cannot synthesize it, and the coenzyme, PLP plays a vital role in the function of approximately 100 enzymes that catalyze essential chemical reactions in the human body (1, 2). For example, PLP functions as a coenzyme for glycogen phosphorylase, an enzyme that catalyzes the release of glucose stored in the muscle as glycogen. Much of the PLP in the human body is found in muscle bound to glycogen phosphorylase. PLP is also a coenzyme for reactions used to generate glucose from amino acids, a process known as gluconeogenesis.

Pyridoxal phosphate inhibits angiogenesis and down regulates the activity of RNA polymerase, reverse transcriptase and DNA polymerase.
Vitamin B6, through its involvement in protein metabolism and cellular growth, is important to the immune system. It helps maintain the health of lymphoid organs (thymus, spleen, and lymph nodes) that make white blood cells. Animal studies show that a vitamin B6 deficiency can decrease antibody production and suppress the immune response. Vitamin B6 also helps maintain blood glucose (sugar) within a normal range by releasing glucose from glycogen. When caloric intake is low the body needs vitamin B6 to help convert stored carbohydrate or other nutrients to glucose to maintain normal blood sugar levels. While a shortage of vitamin B6 will limit these functions, supplements of this vitamin do not enhance them in well-nourished individuals (1, 8-10).

Signs and Symptoms of Deficiency of Vitamin B6
Clinical signs of vitamin B6 deficiency are rarely seen however, Vitamin B6 deficiency can occur in individuals with poor quality diets that are deficient in many nutrients. Symptoms occur during later stages of deficiency, when intake has been very low for an extended time. Signs of vitamin B6 deficiency include dermatitis, glossitis, depression, confusion, and convulsions (1,11). Vitamin B6 deficiency also can cause anemia (1,12,14) abdominal distress, abnormal electroencephalogram, acne, anorexia, autoimmune diseases.

References:

  1. Leklem JE. Vitamin B6. In: Shils ME, Olson JA, Shike M, Ross AC, ed. Modern Nutrition in Health and Disease. 9th ed. Baltimore: Williams and Wilkins, 1999: 413-421.
  2. Bender DA. Vitamin B6 requirements and recommendations. Eur J ClinNutr 1989 ;43:289-309. [PubMed abstract].
  3. Gerster H. The importance of vitamin B6 for development of the infant. Human medical and animal experiment studies. Z Ernahrungswiss 1996; 35:309-17. [PubMed abstract].
  4. Bender DA. Novel functions of vitamin B6. ProcNutrSoc 1994; 53:625-30. [PubMed abstract].
  5. Chandra R and Sudhakaran L. Regulation of immune responses by Vitamin B6. NY AcadSci 1990; 585:404-423. [PubMed abstract].
  6. Trakatellis A, Dimitriadou A, Trakatelli M. Pyridoxine deficiency: New approaches in immunosuppression and chemotherapy. Postgrad Med J 1997; 73:617-22. [PubMed abstract].
  7. Shibata K, Mushiage M, Kondo T, Hayakawa T, Tsuge H. Effects of vitamin B6 deficiency on the conversion ratio of tryptophan to niacin. BiosciBiotechnolBiochem 1995; 59:2060-3.
    [PubMed abstract].
  8. Leyland DM and Beynon RJ. The expression of glycogen phosphorylase in normal and dystrophic muscle. Biochem J 1991; 278:113-7. [PubMed abstract].
  9. Oka T, Komori N, Kuwahata M, Suzuki I, Okada M, Natori Y. Effect of vitamin B6 deficiency on the expression of glycogen phosphorylase mRNA in rat liver and skeletal muscle. Experientia 1994; 50:127-9. [PubMed abstract].
  10. Okada M, Ishikawa K, Watanabe K. Effect of vitamin B6 deficiency on glycogen metabolism in the skeletal muscle, heart, and liver of rats. J NutrSciVitaminol (Tokyo) 1991; 37:349-57. [PubMed abstract].
  11. U.S. Department of Agriculture, Agricultural Research Service,1999. USDA Nutrient Database for Standard Reference, Release 13. Nutrient Data Lab Home Page, http://www.nal.usda.gov/fnic/foodcomp.
  12. Institute of Medicine. Food and Nutrition Board. Dietary Reference Intakes: Thiamin, riboflavin, niacin, vitamin B6, folate, vitamin B12, pantothenic acid, biotin, and choline. NationalAcademy Press. Washington, DC, 1998.
  13. Alaimo K, McDowell M, Briefel R, Bischof A, Caughman C, Loria C, and Johnson C. Dietary intake of vitamins, minerals, and fiber of persons ages 2 months and over in the United States: Third National Health and Nutrition Examination survey, Phase 1, 1988-91. Hyattsville, MD: U.S. Department of Health and Human Services; Center for Disease Control and Prevention; NationalCenter for Health Statistics, 1994:1-28.
  14. Combs G. The Vitamins: Fundamental aspects in nutrition and health. San Diego, California: Academic Press, Inc., 1992; 311-328.

EPI LIFE COACH articles

Pantothenic acid, also known as vitamin B5, as well as the "anti-stress vitamin" is part of the B group vitamins and classified as a water-soluble vitamin. This nutrient can be manufactured in the body by the intestinal flora.
YEAR 2017
DATE Friday, March 03
TOPIC Vitamins
AUTHOR Dr. Carlos Orozco (BSc, MSc, ND, MD, PhD, FPAMS)

Pantothenic acid, also known as vitamin B5, as well as the “anti-stress vitamin” is part of the B group vitamins and classified as a water-soluble vitamin. This nutrient can be manufactured in the body by the intestinal flora.

Biological Function of Vitamin B5
Pantothenic acid is involved in the synthesis of acetylcholine, antibody production, cholesterol, cortisone, coenzyme A, fibroblast multiplication, steroid hormone production, lipid metabolism, protein metabolism; it reduces arthritic pain and maintains normal uric acid levels. Vitamin B5 is also helpful to fight wrinkles as well as the graying of the hair.
Pantothenic acid, also known as vitamin B5, is essential to all forms of life (1). Pantothenic acid is found throughout living cells in the form of coenzyme A (CoA), a vital coenzyme in numerous chemical reactions (2).

Pantothenic acid is a component of coenzyme A (CoA), an essential coenzyme in a variety of reactions that sustain life. CoA is required for chemical reactions that generate energy from food (fat, carbohydrates, and proteins). The synthesis of essential fats, cholesterol, and steroid hormones requires CoA, as does the synthesis of the neurotransmitter, acetylcholine, and the hormone, melatonin. Heme, a component of hemoglobin, requires a CoA-containing compound for its synthesis. Metabolism of a number of drugs and toxins by the liver requires CoA (3).
Coenzyme A was named for its role in acetylation reactions. Most acetylated proteins in the body have been modified by the addition of an acetate group that was donated by CoA. Protein acetylation affects the 3-dimensional structure of proteins, potentially altering their function, the activity of peptide hormones, and appears to play a role in cell division and DNA replication. Protein acetylation also affects gene expression byfacilitating the transcription of mRNA. A number of proteins are also modified by the attachment of long-chain fatty acids donated by CoA. These modifications are known as protein acylation, and appear to play a central role in cell signaling (1).

Acyl-carrier protein
The acyl-carrier protein requires pantothenic acid in the form of 4′-phosphopantetheine for its activity as an enzyme (1, 4). Both CoA and the acyl-carrier protein are required for the synthesis of fatty acids. Fatty acids are a component of some lipids, which are fat molecules essential for normal physiological function. Among these essential fats are sphingolipids, which are a component of the myelin sheath that enhances nerve transmission, and phospholipids in cell membranes.

Signs and Symptoms of Deficiency in vitamin B5
With Vitamin B5 in short supply symptoms like fatigue, headaches, nausea, tingling in the hands, depression, personality changes and cardiac instability have been reported.
Naturally occurring pantothenic acid deficiency in humans is very rare and has been observed only in cases of severe malnutrition. World War II prisoners in the Phillipines, Burma, and Japan experienced numbness and painful burning and tingling in their feet, which was relieved specifically by pantothenic acid (1). Pantothenic acid deficiency in humans has been induced experimentally by administering a pantothenic acid antagonist together with a pantothenic acid deficient diet. Participants in this experiment complained of headache, fatigue, insomnia, intestinal disturbances, and numbness and tingling of their hands and feet (5). In a more recent study, participants fed only a pantothenic acid free diet did not develop clinical signs of deficiency, though some appeared listless and complained of fatigue (6). Homopantothenate is a pantothenic acid antagonist with cholinergic effects (similar to those of the neurotransmitter, acetylcholine). It was used in Japan to enhance mental function, especially in Alzheimer’s disease. A rare side effect was the development of hepatic encephalopathy, a condition of abnormal brain function resulting from the failure of the liver to eliminate toxins. The encephalopathy was reversed by pantothenic acid supplementation suggesting, but not proving, it was due to pantothenic acid deficiency caused by the antagonist (4).

References:

  1. Plesofsky-Vig N. Pantothenic acid. In: Shils M, ed. Nutrition in Health and Disease,. 9th ed. Baltimore: Williams & Wilkins; 1999:423-432.
  2. Tahiliani AG, Beinlich CJ. Pantothenic acid in health and disease. VitamHorm. 1991;46:165-228. (PubMed).
  3. Brody T. Nutritional Biochemistry. 2nd ed. San Diego: Academic Press; 1999.
  4. Bender DA. Optimum nutrition: thiamin, biotin and pantothenate. ProcNutr Soc. 1999;58(2):427-433. (PubMed).
  5. Hodges RE, Ohlson MA, Bean WB. Pantothenic acid deficiency in man. J Clin Invest. 1958;37:1642-1657.
  6. Fry PC, Fox HM, Tao HG. Metabolic response to a pantothenic acid deficient diet in humans. J NutrSciVitaminol (Tokyo). 1976;22(4):339-346. (PubMed).

EPI LIFE COACH articles

Niacin (nicotinic acid and nicotinamide) is also known as vitamin B3. Both nicotinic acid and nicotinamide can serve as the dietary source of vitamin B3.
YEAR 2017
DATE Friday, March 03
TOPIC Vitamins
AUTHOR Dr. Carlos Orozco (BSc, MSc, ND, MD, PhD, FPAMS)

Niacin (nicotinic acid and nicotinamide) is also known as vitamin B3. Both nicotinic acid and nicotinamide can serve as the dietary source of vitamin B3.
Niacin is required for the synthesis of the active forms of vitamin B3, nicotinamide adenine dinucleotide (NAD+) and nicotinamide adenine dinucleotide phosphate (NADP+). Both NAD+ and NADP+ function as cofactors for numerous dehydrogenase reactions e.g., lactate and malate dehydrogenases.
Niacin is not a true vitamin in the strictest definition since it can be derived from the amino acid L-tryptophan, but this conversion is inefficient and requires the presence of thiamine, pyridoxine, and riboflavin.

Biological Function of Vitamin B3
Niacin functions in the release of energy from carbohydrates, fats, and proteins. Niacin is also involved in the synthesis of protein, fat, and pentoses needed for nucleic acid formation.

Niacin is a major constituent of the coenzyme nicotinamide adenine dinucleotide (NAD) and nicotinamide adenine dinucleotide phosphate (NADP). These compounds function to remove hydrogen atoms during biological reactions. Niacin functions as a component of the coenzymes nicotinamide adenine dinucleotide (NAD) and nicotinamide adenine dinucleotide phosphate (NADP). These enzymes are involved in respiration where they act as hydrogen acceptors. They are essential in the reactions involved in the release of energy from carbohydrates, fats, and proteins.

Oxidation-reduction (redox) reactions
Living organisms derive most of their energy from oxidation-reduction (redox) reactions, which are processes involving the transfer of electrons. As many as 200 enzymes require the niacin coenzymes, NAD and NADP, mainly to accept or donate electrons for redox reactions. NAD functions most often in reactions involving the degradation (catabolism) of carbohydrates, fats, proteins, and alcohol to produce energy. NADP functions more often in biosynthetic (anabolic) reactions, such as in the synthesis of fatty acids and cholesterol (1, 2).

Signs and Symptoms of Deficiency
Pellagra, dermatitis, muscular weakness, general fatigue, anorexia, indigestion, insomnia, irritability, stress, depression, excessive blood cholesterol, autoimmune diseases, gastrointestinal upsets, inflammation of the mouth and digestive track. Memory loss, glossitis, confusion, hyper pigmentation, malignant carcinoid tumor, stomatitis, nausea and vomiting.

References

  1. Food and Nutrition Board, Institute of Medicine. Riboflavin. Dietary Reference Intakes: Thiamin, Riboflavin, Niacin, Vitamin B-6, Vitamin B-12, Pantothenic Acid, Biotin, and Choline.
  2. WashingtonD.C.: NationalAcademy Press; 1998:87-122. (National Academy Press).
  3. Brody T. Nutritional Biochemistry. 2nd ed. San Diego: Academic Press; 1999

EPI LIFE COACH articles

Riboflavin is also known as vitamin B2. Riboflavin is the precursor for the coenzymes, flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD).
YEAR 2017
DATE Friday, March 03
TOPIC Vitamins
AUTHOR Dr. Carlos Orozco (BSc, MSc, ND, MD, PhD, FPAMS)

Riboflavin is also known as vitamin B2. Riboflavin is the precursor for the coenzymes, flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD).

FAD
The enzymes that require FMN or FAD as cofactors are termed flavoproteins. Several flavoproteins also contain metal ions and are termed metalloflavoproteins. Both classes of enzymes are involved in a wide range of redox reactions, e.g. succinate dehydrogenase and xanthine oxidase. During the course of the enzymatic reactions involving the flavoproteins the reduced forms of FMN and FAD are formed, FMNH2 and FADH2, respectively.

Biological Function of Vitamin B2:
Riboflavin (vitamin B2) is manufactured in the body by the intestinal flora and is easily absorbed, although very small quantities are stored, so there is a constant need for this vitamin. It activates vitamin B6 and folate, it acts as a coenzyme in the respiratory enzymatic system, as mentioned above, it is an important constituent of flavoproteins i.e. its role in the Krebs cycle from Fumarate to Oxaloacetate. It also plays a major role in the growth and development of the fetus as well as in the maintenance of the mucosal and epithelial tissues.

Oxidation-reduction (redox) reactions
Living organisms derive most of their energy from oxidation-reduction (redox) reactions, which are processes involving the transfer of electrons. Flavin coenzymes participate in

redox reactions in numerous metabolic pathways (3). Flavins are critical for the metabolism of carbohydrates, fats, and proteins. FAD is part of the electron transport (respiratory) chain, which is central to energy production. In conjunction with cytochrome P-450, flavins also participate in the metabolism of drugs and toxins (4).

Antioxidant functions
Glutathione reductase is an FAD-dependent enzyme that participates in the redox cycle of glutathione. The glutathione redox cycle plays a major role in protecting organisms from reactive oxygen species, such as hydroperoxides.

Glutathione reductase requires FAD to regenerate two molecules of reduced glutathione from oxidized glutathione. Riboflavin deficiency has been associated with increased oxidative stress (4). Measurement of glutathione reductase activity in red blood cells is commonly used to assess riboflavin nutritional status (5).
Xanthine oxidase, another FAD-dependent enzyme, catalyzes the oxidation of hypoxanthine and xanthine to uric acid. Uric acid is one of the most effective water-soluble antioxidants in the blood. Riboflavin deficiency can result in decreased xanthine oxidase activity, reducing blood uric acid levels (6).
Glutathione peroxidase, a selenium-containing enzyme, requires two molecules of reduced glutathione to break down hydroperoxides (seediagram).

References

  1. Tanphaichitr V. Thiamin. In: Shils M, ed. Nutrition in Health and Disease. 9th ed. Baltimore: Williams & Wilkins; 1999:381-389.
  2. Rindi G. Thiamin. In: Ziegler EE, Filer LJ, eds. Present Knowledge in Nutrition. 7th ed. WashingtonD.C.: ILSI Press; 1996:160-166.
  3. Brody T. Nutritional Biochemistry. 2nd ed. San Diego: Academic Press; 1999.
  4. Bender DA. Optimum nutrition: thiamin, biotin and pantothenate. ProcNutr Soc. 1999;58(2):427-433. (PubMed).
  5. Todd K, Butterworth RF. Mechanisms of selective neuronal cell death due to thiamine deficiency. Ann N Y Acad Sci. 1999;893:404-411. (PubMed).
  6. Krishna S, Taylor AM, Supanaranond W, et al. Thiamine deficiency and malaria in adults from southeast Asia. Lancet. 1999;353(9152):546-549. (PubMed)