PMID- 10810185 OWN - NLM STAT- MEDLINE DCOM- 20001010 LR - 20131121 IS - 0006-2979 (Print) IS - 0006-2979 (Linking) VI - 65 IP - 4 DP - 2000 Apr TI - Participation of glyceraldehyde-3-phosphate dehydrogenase in the regulation of 2,3-diphosphoglycerate level in erythrocytes. PG - 463-8 AB - 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. FAU - Fokina, K V AU - Fokina KV AD - Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow, 119899, Russia. FAU - Yazykova, M Y AU - Yazykova MY FAU - Danshina, P V AU - Danshina PV FAU - Schmalhausen, E V AU - Schmalhausen EV FAU - Muronetz, V I AU - Muronetz VI LA - eng PT - Journal Article PT - Research Support, Non-U.S. Gov't PL - United States TA - Biochemistry (Mosc) JT - Biochemistry. Biokhimiia JID - 0376536 RN - 138-81-8 (2,3-Diphosphoglycerate) RN - 9012-36-6 (Sepharose) RN - BBX060AN9V (Hydrogen Peroxide) RN - EC 1.2.1.- (Glyceraldehyde-3-Phosphate Dehydrogenases) RN - EC 2.7.2.3 (Phosphoglycerate Kinase) RN - EC 5.4.2.4 (Bisphosphoglycerate Mutase) RN - S88TT14065 (Oxygen) SB - IM MH - 2,3-Diphosphoglycerate/*blood MH - Animals MH - Bisphosphoglycerate Mutase/metabolism MH - Erythrocytes/*enzymology MH - Glyceraldehyde-3-Phosphate Dehydrogenases/*metabolism MH - Glycolysis MH - Humans MH - Hydrogen Peroxide/pharmacology MH - Hydrogen-Ion Concentration MH - Mice MH - Oxygen/metabolism MH - Phosphoglycerate Kinase/metabolism MH - Rabbits MH - Sepharose/metabolism MH - Substrate Specificity MH - Time Factors EDAT- 2000/05/16 09:00 MHDA- 2000/10/14 11:01 CRDT- 2000/05/16 09:00 PHST- 2000/05/16 09:00 [pubmed] PHST- 2000/10/14 11:01 [medline] PHST- 2000/05/16 09:00 [entrez] AID - BCM65040547 [pii] PST - ppublish SO - Biochemistry (Mosc). 2000 Apr;65(4):463-8.