|Related Categories||Application Index, Biochemicals and Reagents, Cell Biology, Cell Signaling Enzymes, Cell Signaling and Neuroscience,|
Disintegrins represent a novel family of integrin β1 and β3 inhibitor proteins isolated from viper venoms. They are low molecular-weight, cysteine-rich peptides containing the Arg-Gly-Asp (RGD) sequence. They are the most potent known inhibitors of integrin function. Disintegrins interfere with cell adhesion to the extracellular matrix, including adhesion of melanoma cells and fibroblasts to fibronectin, and are potent inhibitors of platelet aggregation.
Chemical synthesis of echistatina potent inhibitor of platelet aggregation from Echis carinatus: synthesis and biological activity of selected analogs. Garsky, V.M., et al. Proc. Natl. Acad. Sci. U. S. A. 86, 4022-4026, (1989)
Platelet glycoprotein IIb-IIIa protein antagonists from snake venoms: evidence for a family of platelet-aggregation inhibitors. Dennis, M.S., et al. Proc. Natl. Acad. Sci. U. S. A. 87, 2471-75, (1990)
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