Thromb Haemost 1995; 74(03): 954-957
DOI: 10.1055/s-0038-1649854
Original Article
Platelets
Schattauer GmbH Stuttgart

Interaction of Echicetin with a High Affinity Thrombin Binding Site on Platelet Glycoprotein GPIb

Manling Peng
1  The Sol Sherry Thrombosis Research Center, Philadelphia, PA, USA
2  The Department of Biochemistry, Philadelphia, PA, USA
,
Frances A Emig
2  The Department of Biochemistry, Philadelphia, PA, USA
,
Ahua Mao
3  The Department of Pharmacology, Philadelphia, PA, USA
,
Weiqi Lu
1  The Sol Sherry Thrombosis Research Center, Philadelphia, PA, USA
4  The Department of Physiology, Temple University School of Medicine, Philadelphia, PA, USA
,
Edward P Kirby
1  The Sol Sherry Thrombosis Research Center, Philadelphia, PA, USA
2  The Department of Biochemistry, Philadelphia, PA, USA
,
Stefan Niewiarowski
1  The Sol Sherry Thrombosis Research Center, Philadelphia, PA, USA
4  The Department of Physiology, Temple University School of Medicine, Philadelphia, PA, USA
,
M Anna Kowalska
1  The Sol Sherry Thrombosis Research Center, Philadelphia, PA, USA
4  The Department of Physiology, Temple University School of Medicine, Philadelphia, PA, USA
› Author Affiliations
Further Information

Publication History

Received 30 December 1994

Accepted after revision 18 May 1995

Publication Date:
09 July 2018 (online)

Summary

Echicetin, a protein isolated from Echis carinatus snake venom, inhibited platelet aggregation and secretion induced by low concentrations of thrombin (<0.2 U/ml), by binding to platelet glycoprotein lb (GPIb). The inhibition was not observed when the platelets were stimulated with higher concentrations of thrombin (>0.2 U/ml). Echicetin competed with thrombin for binding to the high affinity site on GPIb. Thrombin also inhibited 50% of the binding of 125I-echicetin to the platelets.