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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
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Publikationsverlauf

Received 30. Dezember 1994

Accepted after revision 18. Mai 1995

Publikationsdatum:
09. Juli 2018 (online)

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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.

 

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