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

Manling Peng; Frances A Emig; Ahua Mao; Weiqi Lu; Edward P Kirby; Stefan Niewiarowski; M Anna Kowalska

doi:10.1055/s-0038-1649854

Thrombosis and Haemostasis, Inhaltsverzeichnis

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

¹The Sol Sherry Thrombosis Research Center, Philadelphia, PA, USA

²The Department of Biochemistry, Philadelphia, PA, USA

,

Frances A Emig

²The Department of Biochemistry, Philadelphia, PA, USA

,

Ahua Mao

³The Department of Pharmacology, Philadelphia, PA, USA

,

Weiqi Lu

¹The Sol Sherry Thrombosis Research Center, Philadelphia, PA, USA

⁴The Department of Physiology, Temple University School of Medicine, Philadelphia, PA, USA

,

Edward P Kirby

¹The Sol Sherry Thrombosis Research Center, Philadelphia, PA, USA

²The Department of Biochemistry, Philadelphia, PA, USA

,

Stefan Niewiarowski

¹The Sol Sherry Thrombosis Research Center, Philadelphia, PA, USA

⁴The Department of Physiology, Temple University School of Medicine, Philadelphia, PA, USA

,

M Anna Kowalska

¹The Sol Sherry Thrombosis Research Center, Philadelphia, PA, USA

⁴The Department of Physiology, Temple University School of Medicine, Philadelphia, PA, USA

› Institutsangaben

Abstract

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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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Referenzen

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