Abstract
Disintegrins, a family of low molecular weight, RGD-containing peptides found in snake venoms prevent the binding of adhesive ligands to a number of integrin receptors. Albolabrin, bitistatin, echistatin, and eristostatin bind to the platelet fibrinogen receptor (GPIIb/IIIa) acting thus as potent inhibitors of platelet aggregation. Here, we have determined the cross-linking of these disintegrins on isolated GPIIb/IIIa. The cross-linking site of all of them was within GPIIIa 217-302, a domain that has been implicated in a number of receptor functions including heterodimer association, activation-dependent conformational changes, and fibrinogen binding.
Publication types
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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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Binding Sites
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Cross-Linking Reagents
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Crotalid Venoms / metabolism
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Humans
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Intercellular Signaling Peptides and Proteins
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Oligopeptides
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Peptides / metabolism*
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Peptides / pharmacology
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Platelet Aggregation Inhibitors / metabolism
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Platelet Membrane Glycoproteins / drug effects
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Platelet Membrane Glycoproteins / metabolism*
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Snake Venoms
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Viper Venoms / metabolism*
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Viper Venoms / pharmacology
Substances
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Cross-Linking Reagents
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Crotalid Venoms
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Intercellular Signaling Peptides and Proteins
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Oligopeptides
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Peptides
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Platelet Aggregation Inhibitors
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Platelet Membrane Glycoproteins
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Snake Venoms
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Viper Venoms
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echistatin
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bitistatin
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albolabrin
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eristostatin
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arginyl-glycyl-aspartic acid