Platelet surface glutathione reductase-like activity.
We previously found that reduced glutathione (GSH) or a mixture of GSH/glutathione disulfide (GSSG) potentiated platelet aggregation. We here report that GSSG, when added to platelets alone, also potentiates platelet aggregation. Most of the GSSG was converted to GSH by a flavoprotein-dependent platelet surface mechanism. This provided an appropriate redox potential for platelet activation. The addition of GSSG to platelets generated sulfhydryls in the beta subunit of the alpha(IIb)beta(3) fibrinogen receptor, suggesting a mechanism for facilitation of agonist-induced platelet activation.
Essex
David W
DW
University of Texas Health Science Center at San Antonio, Mail Code 7880, 7703 Floyd Curl Drive, San Antonio, TX 78229, USA. essex@uthscsa.edu
Li
Mengru
M
Feinman
Richard D
RD
Miller
Anna
A
D001792:Blood Platelets / Q000201:enzymology*; D004220:Disulfides / Q000378:metabolism; D005978:Glutathione / Q000378:metabolism; D019803:Glutathione Disulfide / Q000494:pharmacology*; D005980:Glutathione Reductase / Q000378:metabolism*; D006801:Humans; D010084:Oxidation-Reduction; D010974:Platelet Aggregation / Q000187:drug effects* / Q000502:physiology; D019039:Platelet Glycoprotein GPIIb-IIIa Complex / Q000378:metabolism
D004220:Disulfides; D019039:Platelet Glycoprotein GPIIb-IIIa Complex; D005980:Glutathione Reductase; D005978:Glutathione; D019803:Glutathione Disulfide