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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.


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HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY
Brief report

Platelet surface glutathione reductase-like activity

David W. Essex, Mengru Li, Richard D. Feinman, and Anna Miller

From 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 {beta} subunit of the {alpha}IIb{beta}3 fibrinogen receptor, suggesting a mechanism for facilitation of agonist-induced platelet activation.


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