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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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Submitted March 23, 2004
Accepted April 27, 2004

Platelet Surface Glutathione Reductase-Like Activity

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

Department of Medicine, The University of Texas Health Science Center, San Antonio, TX, USA
Department of Biochemistry, State University of New York Downstate Medical Center, Brooklyn, NY, USA

* Corresponding author; email: essex{at}uthscsa.edu.

We previously found that reduced glutathione (GSH) or a mixture of GSH/GSSG potentiated platelet aggregation. We here report that glutathione disulfide, 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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