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. 2005 Jun 1;38(11):1501-10.
doi: 10.1016/j.freeradbiomed.2005.02.019.

S-glutathionylation in human platelets by a thiol-disulfide exchange-independent mechanism

Isabella Dalle-Donne  1 , Daniela Giustarini, Roberto Colombo, Aldo Milzani, Ranieri Rossi
Affiliations

S-glutathionylation in human platelets by a thiol-disulfide exchange-independent mechanism

Isabella Dalle-Donne et al. Free Radic Biol Med. .

Abstract

Protein-glutathione mixed disulfide formation was investigated in vitro by exposure of human platelets to the thiol-specific oxidant azodicarboxylic acid-bis-dimethylamide (diamide). We found that diamide causes a decrease in the reduced form of glutathione (GSH), paralleled by an increase in protein-GSH mixed disulfides (S-glutathionylated proteins), which was not accompanied by any significant increase in the basal level of glutathione disulfide (GSSG). The increase in the appearance of S-glutathionylated proteins was inversely correlated with ADP-induced platelet aggregation. Platelet cytoskeleton was analyzed by SDS-PAGE followed by Western immunoblotting with anti-GSH antibody. The main S-glutathionylated cytoskeletal protein proved to be actin, which accounts for 35% of the platelet total protein content. Our results suggest that neither GSSG formation nor a consequent thiol-disulfide exchange mechanism is involved in actin S-glutathionylation of human platelets exposed to diamide. Instead, a mechanism involving the initial oxidative activation of actin thiol groups, which then react with GSH to the protein-GSH mixed disulfides, makes it likely that platelet actin is S-glutathionylated without any significant increase in the GSSG content.

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