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Journal of Parenteral and Enteral Nutrition
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Review: Glycine

John C. Hall, FRACS

University Department of Surgery, Royal Perth Hospital, Western Australia, Australia

Glycine consists of a single carbon molecule attached to an amino and a carboxyl group. Its small size helps it to function as a flexible link in proteins and allows for the formation of helices, an extracellular signaling molecule, recognition sites on cell membranes and enzymes, a modifier of molecular activity via conjugation and glycine extension of hormone precursors, and an osmoprotectant. There is substantial experimental evidence that free glycine may have a role in protecting tissues against insults such as ischemia, hypoxia, and reperfusion. This impressive catalogue of functions makes an interesting contrast with glycine's perceived metabolic role as a nonessential amino acid. Glycine interconverts with serine to provide a mechanism for the transfer of activated one-carbon groups. Glycine has just been viewed as a convenient source of nitrogen to add to solutions of nutrients. Although this may have unexpected benefits when such solutions are used in clinical practice, it does raise the specter of a possible confounding effect in experiments when glycine is added to control solutions to make them isonitrogenous. (Journal of Parenteral and Enteral Nutrition 22:393-398, 1998)

Journal of Parenteral and Enteral Nutrition, Vol. 22, No. 6, 393-398 (1998)
DOI: 10.1177/0148607198022006393
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