Free Radicals Induce Reversible Membrane-Cytoplasm Translocation of Glyceraldehyde-3-Phosphate Dehydrogenase in Human Erythrocytes

摘要: We investigated the role of oxygen free radicals in modulation glyceraldehyde-3-phosphate dehydrogenase binding to erythrocyte membrane. Previous studies have demonstrated that vitro tyrosine phosphorylation Band 3 prevents various glycolytic enzymes its cytoplasmic domain. Since these are inhibited their bound state, functional consequence red blood cells should be increase glycolysis. To generate radicals, we used an azo-compound, hydrophilic 2,2'-azobis(2-amidinopropane) hydrochloride, which, at 37 degrees C and presence oxygen, decomposes produces peroxyl a constant rate. The reaction with intact induced time-dependent loss membrane-bound enzyme, dehydrogenase, associated concomitant decrease enzyme activity. At same time, was phosphorylated tyrosine. These results were completely reversible plasma after removal oxidative stress. also enhanced production lactate cells. Our data reveal powerful mechanism metabolic regulation can boost or reduce energy times special need such as during radical attack.