Journal
BLOOD CELLS MOLECULES AND DISEASES
Volume 37, Issue 3, Pages 180-187Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bcmd.2006.09.003
Keywords
erythrocytes; cytoskeletal proteins; diamide; osmotic fragility; protein-glutathione mixed disulfides
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In this work, protein-glutathione mixed disulfide formation in human red blood cells (RBCs) was evaluated in vitro by using the thiol-specific reagent diamide. We investigated what mechanism could lead to S-glutathionylation of membrane skeletal proteins, what are the main target proteins, and the correlation between protein S-glutathionylation and RBC hemolysis. Diamide caused a decrease in the reduced form of glutathione (GSH), which was accompanied by an increase in the basal level of glutathione disuffide (GSSG) and in S-glutathionylation of protein 4.2 and spectrin. The increase in membrane skeletal protein S-glutathionylation was correlated with a lower susceptibility of RBCs to osmotic hemolysis, suggesting that S-glutathionylation of protein 4.2 and spectrin could contribute to regulate RBC membrane stability. (c) 2006 Elsevier Inc. All rights reserved.
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