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L-Proline/L-Hydroxyproline

Proline and hydroxyproline are nonessential amino acids. Nearly all proteins contain proline which is the third most abundant amino acid in the body (glutamine and alanine are first and second most abundant). Hydroxyproline is the breakdown or waste product of proline. Hydroxyproline is an indicator that there is collagen and bone breakdown. Proline synthesis begins with the breakdown of ornithine and glutamic acid.

Function- Proline is best known for being one of the main components of collagen. Supplementation would be indicated in cases of wound healing, hyper-mobile joints, anti-aging skin formulas, soft tissue injuries and excessive bruising. It seems to be more productive if this nutrient is combined with vitamin C.

Proline may have benefits in relation to cognitive learning. Substance P is a neurotransmitter in the brain in which proline is a component.

Deficiency- Supplementation would be indicated in cases of wound healing, hyper-mobile joints, anti-aging skin formulas, soft tissue injuries and excessive bruising. It seems to be more productive if this nutrient is combined with vitamin C. Any condition that relates to neurotransmitter deficiency may be related to an inadequate amount of proline. Long term deficiency related to structure will be related in cases of osteoporosis.

Sources- Some whole foods which contain proline are avocados, cheese, turkey, eggs, yogurt, wild game, wheat germ, granola, oatmeal, chicken and ricotta cheese.

Precautions- If there are metabolic errors of metabolism there may be side effects with injesting proline but not otherwise.

Requirements- There is no Recommended Dietary Allowances (RDA) listed. Individual needs may differ due to clinical conditions, biochemical individuality and absorption. All sources of nutrients should be consumed in their most natural state, in the form of a variety of foods or supplements when necessary. Free form amino acid supplements are immediately absorbed by the body and should be consumed with natural occurring cofactors for best results. Consulting with a physician that is properly trained in the natural healing sciences and amino acid therapy may be needed for optimum results.

Written by Jerome Rerucha D.C.

References-
1. Abraira, C., DeBartolo, M., Katzen, R., and Lawrence, A. M., Disappearance of glucagonoma rash after surgical resection, but not during dietary normalization of serum amino acids. Amer. j. Clin. Nutr., 39(3):351-355, 1984.
2. Hershenbich, D., Garcia-Tsao, G., Saldana, S. A., and Rojkind, M., Relationship between blood lactic acid and serum proline in alcoholic liver cirrhosis. Gastementerol., 80:1012-1015,1981.
3. Dingman, W., and Sporn, M. B., The penetration of proline and proline derivatives into brain. /. Neurochem., 4:148-153, 1959.
4. Bruntrock, P., jentzsch, K. D., Heder, G., Stimulation of wound healing, using brain extract with fibroblast growth factor (FGF) activity. I. Quantitative and biochemical studies into the formation of granulation tissue. Exp. Pathol., 21(1): 46-53, 1982.
5. Atkinson MR, Wray LV Jr, Fisher SH 1990 Regulation of histidine and proline degradation enzymes by amino acid availability in Bacillus subtilis. J. Bacteriol. 172: 4758-4765.
6. Campbell HD, Webb GC, Young IG 1997 A human homologue of the Drosophila melanogaster sluggish-A (proline oxidase) gene maps to 22q11.2, and is a candidate gene for type-I hyperprolinaemia. Hum. Genet. 101: 69-74.
7. Hagedorn CH, Phang JM 1983 Transfer of reducing equivalents into mitochondria by the interconversions of proline and delta 1-pyrroline-5-carboxylate. Arch. Biochem. Biophys. 225: 95-101.
8. Jaeken J, Goemans N, Fryns JP, Francois I, de Zegher F 1996 Association of hyperprolinaemia type I and heparin cofactor II deficiency with CATCH 22 syndrome: evidence for a contiguous gene syndrome locating the proline oxidase gene. J. Inherit. Metab. Dis. 19: 275-277.


 
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