Thromb Haemost 1981; 45(03): 290-293
DOI: 10.1055/s-0038-1650190
Original Article
Schattauer GmbH Stuttgart

Superoxide, Xanthine Oxidase and Platelet Reactions: Further Studies on Mechanisms by which Oxidants Influence Platelets

Peter H Levine
The Blood Research Laboratory and Medical Division, The Memorial Hospital and the Department of Medicine, the University of Massachusetts Medical School, Worcester, MA, U.S.A.
,
Danielle G Sladdin
The Blood Research Laboratory and Medical Division, The Memorial Hospital and the Department of Medicine, the University of Massachusetts Medical School, Worcester, MA, U.S.A.
,
Norman I Krinsky
The Blood Research Laboratory and Medical Division, The Memorial Hospital and the Department of Medicine, the University of Massachusetts Medical School, Worcester, MA, U.S.A.
*   The Department of Biochemistry and Pharmacology, Tufts University School of Medicine, Boston, MA, U.S.A.
› Author Affiliations
Further Information

Publication History

Received 08 April 1980

Accepted 24 April 1981

Publication Date:
06 July 2018 (online)

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Summary

In the course of studying the effects on platelets of the oxidant species superoxide (O- 2), Of was generated by the interaction of xanthine oxidase plus xanthine. Surprisingly, gel-filtered platelets, when exposed to xanthine oxidase in the absence of xanthine substrate, were found to generate superoxide (O- 2), as determined by the reduction of added cytochrome c and by the inhibition of this reduction in the presence of superoxide dismutase.

In addition to generating Of, the xanthine oxidase-treated platelets display both aggregation and evidence of the release reaction. This xanthine oxidase induced aggreagtion is not inhibited by the addition of either superoxide dismutase or cytochrome c, suggesting that it is due to either a further metabolite of O- 2, or that O- 2 itself exerts no important direct effect on platelet function under these experimental conditions. The ability of Of to modulate platelet reactions in vivo or in vitro remains in doubt, and xanthine oxidase is an unsuitable source of O- 2 in platelet studies because of its own effects on platelets.