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
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Comparative Study
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Blood Platelets / drug effects
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Blood Platelets / metabolism
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Carrier Proteins
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Epitopes
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Humans
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Molecular Sequence Data
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Peptides / blood
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Platelet Aggregation Inhibitors / pharmacology*
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Platelet Glycoprotein GPIb-IX Complex / metabolism*
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Platelet Membrane Glycoproteins / metabolism
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Proteins / immunology
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Proteins / metabolism
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Proteins / pharmacology*
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Receptors, Cell Surface / metabolism
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Receptors, Thrombin / metabolism*
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Secretory Rate / drug effects
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Thrombin / pharmacology
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Viper Venoms / blood
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Viper Venoms / pharmacology*
Substances
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Carrier Proteins
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Epitopes
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Peptides
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Platelet Aggregation Inhibitors
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Platelet Glycoprotein GPIb-IX Complex
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Platelet Membrane Glycoproteins
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Proteins
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Receptors, Cell Surface
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Receptors, Thrombin
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Viper Venoms
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von Willebrand factor receptor
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echicetin
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Thrombin