title: Prevention of dicarbonyl-mediated advanced glycation by glyoxalases: implication in skin aging.
abstract: Skin aging is the result of intrinsic chronological aging and photoaging, due to UV exposure, that both share important histological modifications and molecular features, including alterations of proteins. One of the main damage is glycation that occurs when reducing sugars react non-enzymatically with proteins. This reaction also happens when the dicarbonyl compounds GO (glyoxal) and MG (methylglyoxal), which are glucose derivatives, react with proteins. These compounds can be detoxified by the glyoxalase system composed of two enzymes, Glo1 (glyoxalase I) and Glo2 (glyoxalase II). The aims of the present mini-review are to briefly summarize our current knowledge of the biological roles of these enzymes in aging and then discuss the relevance of studying the role of glycation and of detoxifying systems in human skin aging.
authors.forename: Sabrina
authors.initials: S
authors.lastname: Radjei
authors.forename: Bertrand
authors.initials: B
authors.lastname: Friguet
authors.affiliation: ∥LVMH Recherche, 185 avenue de Verdun, 45800 Saint-Jean-de-Braye, France.
authors.forename: Carine
authors.initials: C
authors.lastname: Nizard
authors.forename: Isabelle
authors.initials: I
authors.lastname: Petropoulos
mesh_terms: D000818:Animals; D006031:Glycosylation; D006801:Humans; D007791:Lactoylglutathione Lyase / Q000378:metabolism*; D011765:Pyruvaldehyde / Q000378:metabolism; D015595:Skin Aging / Q000502:physiology*
chemical_list: D011765:Pyruvaldehyde; D007791:Lactoylglutathione Lyase