Membrane skeletal protein S-glutathionylation and hemolysis in human red blood cells.
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 disulfide (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.
Rossi
Ranieri
R
Department of Neuroscience, University of Siena, I-53100 Siena, Italy.
Giustarini
Daniela
D
Milzani
Aldo
A
Dalle-Donne
Isabella
I
D003958:Diamide / Q000737:chemistry*; D004910:Erythrocyte Membrane / Q000737:chemistry*; D005978:Glutathione / Q000737:chemistry*; D006461:Hemolysis; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry*; D013049:Spectrin / Q000737:chemistry*
D008565:Membrane Proteins; D003958:Diamide; D013049:Spectrin; D005978:Glutathione