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Thromb Haemost 1991; 65(04): 421-424
DOI: 10.1055/s-0038-1648164
Original Article
Schattauer GmbH Stuttgart

Superoxide Dismutase Cooperates with Prostacyclin to Inhibit Platelet Aggregation: a Comparative Study in Washed Platelets and Platelet Rich Plasma

Daniela Salvemini
The William Harvey Research Institute, St. Bartholomew’s Hospital Medical College, London, United Kingdom
,
Gilberto de Nucci
The William Harvey Research Institute, St. Bartholomew’s Hospital Medical College, London, United Kingdom
,
John R Vane
The William Harvey Research Institute, St. Bartholomew’s Hospital Medical College, London, United Kingdom
› Author Affiliations
Further Information

Publication History

Received: 23 April 1990

Accepted after revision 27 November 1990

Publication Date:
02 July 2018 (online)

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Summary

The role of superoxide anions (O2 −) in human platelet aggregation in Krebs’ buffer or plasma was investigated. In indome thacin (10 μM)-treated washed platelets superoxide dismutase (SOD; 60 U/ml) or ferricytochrome c (FCC; 70 μM) inhibited platelet aggregation by thrombin but not that by collagen or ADP. In addition, in indomethacin (10 μM)-treated washed platelets, SOD significantly potentiated the anti-aggregatory activity of prostacyclin (PGI2) or iloprost when thrombin but not collagen was used as the aggregating agent. In platelet rich plasma, SOD (60 U/ml) did not inhibit platelet aggregation nor did it potentiate the anti-aggregatory activity of iloprost when ADP, collagen or thrombin were used as aggregating agents. Thus, O2 − participate in the aggregatory activity of thrombin but not collagen or ADP and PGI2 or iloprost, by reducing the sensitivity of platelets to thrombin, co-operate with SOD to inhibit thrombin-induced platelet aggregation

The interpretation of the use of SOD in experiments involving endothelium-derived relaxing factor (NO) is discussed

 

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