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Blood, 1 September 2004, Vol. 104, No. 5, pp. 1383-1385. Prepublished online as a Blood First Edition Paper on May 13, 2004; DOI 10.1182/blood-2004-03-1097.
HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY Platelet surface glutathione reductase-like activityFrom the Division of Hematology, Department of Medicine, University of Texas Health Science Center at San Antonio, TX; and Department of Biochemistry, State University of New York Downstate Medical Center at Brooklyn, NY.
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
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