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)

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