Echistatin from

General description
Echistatin is a small peptide disintegrin that has no multiple epitopes.[1] It is a single chain polypeptide with a molecular mass of 5400. Echistatin has eight cysteines and the sequence arginine glycine aspartic acid (RGD).[2] Application
Echistatin from Echis carinatus has been used in diabetic rabbits grouping and treatment[3] and murine iPSC (induced pluripotent stem cell) culture.[4] Biochem/physiol Actions
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.
Echistatin has the ability to prevent IRS-1 (insulin receptor substrate-1) phosphorylation induced by IGF-1 (insulin like growth factor-1).[1] Echistatin α1, purified from the venom of the saw scaled viper, Echis carinatus has the capability to block platelet aggregation.[2]