title: Participation of glyceraldehyde-3-phosphate dehydrogenase in the regulation of 2,3-diphosphoglycerate level in erythrocytes.
abstract: Data are presented concerning the possible participation of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) in regulation of the glycolytic pathway and the level of 2,3-diphosphoglycerate in erythrocytes. Experimental support has been obtained for the hypothesis according to which a mild oxidation of GAPDH must result in acceleration of glycolysis and in decrease in the level of 2, 3-diphosphoglycerate due to the acyl phosphatase activity of the mildly oxidized enzyme. Incubation of erythrocytes in the presence of 1 mM hydrogen peroxide decreases 2,3-diphosphoglycerate concentration and causes accumulation of 3-phosphoglycerate. It is assumed that the acceleration of glycolysis in the presence of oxidative agents described previously by a number of authors could be attributed to the acyl phosphatase activity of GAPDH. A pH-dependent complexing of GAPDH and 3-phosphoglycerate kinase or 2, 3-diphosphoglycerate mutase is found to determine the fate of 1,3-diphosphoglycerate that serves as a substrate for the synthesis of 2,3-diphosphoglycerate as well as for the 3-phosphoglycerate kinase reaction in glycolysis. A withdrawal of the two-enzyme complexes from the erythrocyte lysates using Sepharose-bound anti-GAPDH antibodies prevents the pH-dependent accumulation of the metabolites. The role of GAPDH in the regulation of glycolysis and the level of 2,3-diphosphoglycerate in erythrocytes is discussed.
authors.affiliation: Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow, 119899, Russia.
authors.forename: K V
authors.initials: KV
authors.lastname: Fokina
authors.forename: M Y
authors.initials: MY
authors.lastname: Yazykova
authors.forename: P V
authors.initials: PV
authors.lastname: Danshina
authors.forename: E V
authors.initials: EV
authors.lastname: Schmalhausen
authors.forename: V I
authors.initials: VI
authors.lastname: Muronetz
mesh_terms: D019794:2,3-Diphosphoglycerate / Q000097:blood*; D000818:Animals; D001731:Bisphosphoglycerate Mutase / Q000378:metabolism; D004912:Erythrocytes / Q000201:enzymology*; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000378:metabolism*; D006019:Glycolysis; D006801:Humans; D006861:Hydrogen Peroxide / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D051379:Mice; D010100:Oxygen / Q000378:metabolism; D010735:Phosphoglycerate Kinase / Q000378:metabolism; D011817:Rabbits; D012685:Sepharose / Q000378:metabolism; D013379:Substrate Specificity; D013997:Time Factors
chemical_list: D019794:2,3-Diphosphoglycerate; D012685:Sepharose; D006861:Hydrogen Peroxide; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D010735:Phosphoglycerate Kinase; D001731:Bisphosphoglycerate Mutase; D010100:Oxygen