Free radicals induce reversible membrane-cytoplasm translocation of glyceraldehyde-3-phosphate dehydrogenase in human erythrocytes

Archives of Biochemistry and Biophysics
C MallozziM Minetti

Abstract

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

Citations

Jul 14, 1998·American Journal of Hematology·H T TerraS T Saad
Nov 22, 1997·FEBS Letters·P S BrookesS J Heales
Nov 18, 2010·The Journals of Gerontology. Series A, Biological Sciences and Medical Sciences·David de Gonzalo-CalvoAna Coto-Montes
Dec 25, 2019·Biochimica Et Biophysica Acta. Biomembranes·Susana RochaAlice Santos-Silva
Dec 23, 2006·The International Journal of Biochemistry & Cell Biology·M Elisabetta ClementiFrancesco Misiti
Sep 9, 2008·Food and Chemical Toxicology : an International Journal Published for the British Industrial Biological Research Association·Maria Cristina AlbertiniMarina Dachà

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