Interaction of echicetin with a high affinity thrombin binding site on platelet glycoprotein GPIb

Thromb Haemost. 1995 Sep;74(3):954-7.

Abstract

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 Ib (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.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Blood Platelets / drug effects
  • Blood Platelets / metabolism
  • Carrier Proteins
  • Epitopes
  • Humans
  • Molecular Sequence Data
  • Peptides / blood
  • Platelet Aggregation Inhibitors / pharmacology*
  • Platelet Glycoprotein GPIb-IX Complex / metabolism*
  • Platelet Membrane Glycoproteins / metabolism
  • Proteins / immunology
  • Proteins / metabolism
  • Proteins / pharmacology*
  • Receptors, Cell Surface / metabolism
  • Receptors, Thrombin / metabolism*
  • Secretory Rate / drug effects
  • Thrombin / pharmacology
  • Viper Venoms / blood
  • Viper Venoms / pharmacology*

Substances

  • Carrier Proteins
  • Epitopes
  • Peptides
  • Platelet Aggregation Inhibitors
  • Platelet Glycoprotein GPIb-IX Complex
  • Platelet Membrane Glycoproteins
  • Proteins
  • Receptors, Cell Surface
  • Receptors, Thrombin
  • Viper Venoms
  • von Willebrand factor receptor
  • echicetin
  • Thrombin