Proline is a nonessential amino acid. It contains a secondary α-imino group and is sometimes called an α-imino acid. Proline, and its metabolite hydroxyproline, constitute a third of the total amino acids found in collagen. Lysine, proline, hydroxyproline, and vitamin C are all important in the synthesis of collagen for skin, bones, tendons, and cartilage. Proline is abundant in meat, bone meal, poultry, salmon, wheat, barley, and corn. In addition to dietary sources, proline can be synthesized from glutamate/glutamine, arginine, and ornithine. It can also be synthesized within enterocytes from degradation of small peptides.
In addition to collagen formation, proline has many other physiologic functions including regulation of gene expression, mTOR activation (integrating nutrient and growth factor signaling in cells), cellular redox reactions, protein synthesis, hydroxyproline generation, arginine synthesis, and it is a scavenging antioxidant.
References:
- Jurgens P, Schwartau M, Doehn M. [Disorders of amino acid metabolism in a patient with identified thiamine deficiency]. Infusionstherapie klinische Ernahrung. 1982;9(6):312-316.
- Gropper S SJ, Groff J. Adv Nutr Human Metab. 5th ed. Belmont, CA: Wadsworth, Cengage Learning; 2009.
- Wu G, Bazer FW, Burghardt RC, et al. Proline and hydroxyproline metabolism: implications for animal and human nutrition. Amino Acids. 2011;40(4):1053-1063.
- Reeds PJ. Dispensable and indispensable amino acids for humans. J Nutr. 2000;130(7):1835s-1840s.
Low levels may be reflective of poor dietary intake, GI malabsorption, maldigestion, or low levels of its precursors.
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High dietary intake of proline-rich foods can elevate levels. There are vitamin and mineral cofactors needed for downstream metabolism of proline in its many physiologic processes. Functional deficiency of nutrient cofactors, such as vitamin B1, can result in elevated levels. Furthermore, administration of vitamin B1 has been shown to lower proline levels, as well as other amino acids in severe thiamine deficiency.
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