title: Native protein glycoxidation and aging.
abstract: Structural and functional alterations of proteins are observed during aging. Glycation of long half-life proteins, involving reducing carbohydrates, leads to the formation of intra and intermolecular cross-links and the production of free radicals. These processes depend on the amount of glucose available and on molecular oxygen which contributes to the production of free radicals. These processes are observed without dysfunction of carbohydrate metabolism and progress with age. However, whether this process is a primary cause or a consequence of aging remains a question of debate. Prevention of excessive glycoxidation could be a goal of recommendations designed to control the tissular alterations occurring in aging.
authors.affiliation: Laboratoire de Biochimie, Hôpital Nord, CHU-Hôpitaux de Saint-Etienne, 42055 Saint-Etienne Cedex, France.
authors.forename: M
authors.initials: M
authors.lastname: Meli
authors.forename: J
authors.initials: J
authors.lastname: Frey
authors.forename: C
authors.initials: C
authors.lastname: Perier
mesh_terms: D000375:Aging / Q000378:metabolism*; D001120:Arginine / Q000378:metabolism; D050260:Carbohydrate Metabolism; D005609:Free Radicals / Q000378:metabolism; D005947:Glucose / Q000378:metabolism*; D017127:Glycation End Products, Advanced / Q000378:metabolism; D006031:Glycosylation; D006207:Half-Life; D006801:Humans; D008239:Lysine / Q000378:metabolism; D015416:Maillard Reaction; D010084:Oxidation-Reduction; D011506:Proteins / Q000378:metabolism*
chemical_list: D005609:Free Radicals; D017127:Glycation End Products, Advanced; D011506:Proteins; D001120:Arginine; D005947:Glucose; D008239:Lysine