Individual differences |
Methods | Statistics | Clinical | Educational | Industrial | Professional items | World psychology |
Biological: Behavioural genetics · Evolutionary psychology · Neuroanatomy · Neurochemistry · Neuroendocrinology · Neuroscience · Psychoneuroimmunology · Physiological Psychology · Psychopharmacology (Index, Outline)
Chemical structure of L-arginine
|Systematic (IUPAC) name|
Arginine (symbol Arg or R) is an α-amino acid. The L-form is one of the 20 most common natural amino acids. In mammals, arginine is classified as a semiessential or conditionally essential amino acid, depending on the developmental stage and health status of the individual. Infants are unable to effectively synthesize arginine, making it nutritionally essential for infants. Adults, however, are able to synthesize arginine in the urea cycle.
Arginine was first isolated from a lupin seedling extract in 1886 by the Swiss chemist Ernst Schulze.
Structure[edit | edit source]
Arginine can be considered to be a basic amino acid as the part of the side chain nearest to the backbone is long, carbon-containing and hydrophobic, whereas the end of the side chain is a complex guanidinium group. With a pKa of 12.48, the guanidinium group is positively charged in neutral, acidic and even most basic environments. Because of the conjugation between the double bond and the nitrogen lone pairs, the positive charge is delocalized. This group is able to form multiple H-bonds.
Synthesis[edit | edit source]
Arginine is synthesized from citrulline by the sequential action of the cytosolic enzymes argininosuccinate synthetase (ASS) and argininosuccinate lyase (ASL). This is energetically costly, as the synthesis of each molecule of argininosuccinate requires hydrolysis of adenosine triphosphate (ATP) to adenosine monophosphate (AMP); i.e., two ATP equivalents.
Citrulline can be derived from multiple sources:
- from arginine via nitric oxide synthase (NOS);
- from ornithine via catabolism of proline or glutamine/glutamate;
- from asymmetric dimethylarginine (ADMA) via DDAH.
On a whole-body basis, synthesis of arginine occurs principally via the intestinal–renal axis, wherein epithelial cells of the small intestine, which produce citrulline primarily from glutamine and glutamate, collaborate with the proximal tubule cells of the kidney, which extract citrulline from the circulation and convert it to arginine, which is returned to the circulation. Consequently, impairment of small bowel or renal function can reduce endogenous arginine synthesis, thereby increasing the dietary requirement.
Synthesis of arginine from citrulline also occurs at a low level in many other cells, and cellular capacity for arginine synthesis can be markedly increased under circumstances that also induce iNOS. Thus, citrulline, a coproduct of the NOS-catalyzed reaction, can be recycled to arginine in a pathway known as the citrulline-NO or arginine-citrulline pathway. This is demonstrated by the fact that in many cell types, citrulline can substitute for arginine to some degree in supporting NO synthesis. However, recycling is not quantitative because citrulline accumulates along with nitrate and nitrite, the stable end-products of NO, in NO-producing cells.
Function[edit | edit source]
Arginine plays an important role in cell division, the healing of wounds, removing ammonia from the body, immune function, and the release of hormones. Arginine, taken in combination with pycnogenol or yohimbine, has also been used as a treatment for erectile dysfunction.
In proteins[edit | edit source]
The geometry, charge distribution and ability to form multiple H-bonds make arginine ideal for binding negatively charged groups. For this reason arginine prefers to be on the outside of the proteins where it can interact with the polar environment. Incorporated in proteins, arginine can also be converted to citrulline by PAD enzymes. In addition, arginine can be methylated by protein methyltransferases.
As a precursor[edit | edit source]
Arginine is the immediate precursor of NO, urea, ornithine and agmatine; is necessary for the synthesis of creatine; and can be used for the synthesis of polyamines (mainly through ornithine and to a lesser degree through agmatine), citrulline, and glutamate. For being a precursor of NO, (relaxes blood vessels), arginine is used in many conditions where vasodilation is required. The presence of asymmetric dimethylarginine (ADMA), a close relative, inhibits the nitric oxide reaction; therefore, ADMA is considered a marker for vascular disease, just as L-arginine is considered a sign of a healthy endothelium.
[edit | edit source]
Tissues culture studies have shown the suppression of viral replication when the lysine to arginine ratio in vitro favors lysine. The therapeutic consequence of this finding is unclear, but dietary arginine may affect the effectiveness of lysine supplementation.
Implication in contributing to risk of death from heart disease[edit | edit source]
A recent Johns Hopkins study testing the addition of L-arginine to standard postinfarction treatment has implicated L-arginine supplementation with an increased risk of death in patients recovering from heart attack. This study has been discussed in some detail in : "Reverse Heart Disease Now" by Stephen T Sinatra MD and James C Roberts MD, publ. Wiley 2006 ISBN 0-471-74704-1 at pp 111 -113.
Growth hormone[edit | edit source]
Prolactin[edit | edit source]
Although there haven't been thorough studies, some sources claim that arginine helps release prolactin, an estrogenic compound which is associated with lactation, and like all estrogenic compounds may curb the secretion of testosterone (citation needed). Thus some bodybuilders stay away from pure arginine, intaking only amounts naturally found in protein. Prolactin does not curb testosterone release. Prolactin increases adrenal androgen (amongst it testosterone) secretion. Ref. Kazumi Higuchi et al. Prolactin has a direct effect on adrenal androgen secretion. J Clin Endocrinol Metab. 1984;59:714-8.
Food sources[edit | edit source]
Arginine is found in chocolate, wheat germ and flour, buckwheat, granola, oatmeal, dairy products (cottage cheese, ricotta, nonfat dry milk, skim yogurt), beef (roasts, steaks), pork (Canadian bacon, ham), nuts (coconut, pecans, cashews, walnuts, almonds, Brazil nuts, hazel nuts, peanuts), seeds (pumpkin, sesame, sunflower), poultry (chicken and turkey light meat), wild game (pheasant, quail), seafood (halibut, lobster, salmon, shrimp, snails, tuna in water), chick peas, and cooked soybeans.
References[edit | edit source]
- Enzymes of arginine metabolism J Nutr. 2004 Oct; 134(10 Suppl): 2743S-2747S; PMID 15465778 Free text
- Stanislavov, R. and Nikolova. 2003. Treatment of Erectile Dysfunction with Pycnogenol and L-arginine. Journal of Sex and Marital Therapy, 29(3): 207 – 213.
- Lebret, T., Hervéa, J. M., Gornyb, P., Worcelc, M. and Botto, H. 2002. Efficacy and Safety of a Novel Combination of L-Arginine Glutamate and Yohimbine Hydrochloride: A New Oral Therapy for Erectile Dysfunction. European Urology 41(6): 608-613.
- Griffith RS, Norins AL, Kagan C. (1978). A multicentered study of lysine therapy in Herpes simplex infection. Dermatologica. 156 (5): 257-267. PMID 640102.
- Arginine Therapy in Acute Myocardial Infarction JAMA. 2006 Jan; Vol.295 #1: 58-64; PMID 16391217 Abstract
- Alba-Roth J, Müller O, Schopohl J, von Werder K (1988). Arginine stimulates growth hormone secretion by suppressing endogenous somatostatin secretion. J Clin Endocrinol Metab 67 (6): 1186-9.
- L-Arginine Supplements Nitric Oxide Scientific Studies Food Sources. URL accessed on 2007-02-20.
[edit | edit source]
|Alanine | Arginine | Asparagine | Aspartic acid | Cysteine | Glutamic acid | Glutamine | Glycine | Histidine | Isoleucine | Leucine | Lysine | Methionine | Phenylalanine | Proline | Serine | Threonine | Tryptophan | Tyrosine | Valine|
|Essential amino acid | Protein | Peptide | Genetic code|
|This page uses Creative Commons Licensed content from Wikipedia (view authors).|