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Echistatin is a small disintegrin peptide originally isolated
from Echis carinatus (saw-scaled viper) venom. It contains an
RGD (Arg-Gly-Asp) integrin-binding motif and acts as a potent antagonist of
RGD-binding integrins, particularly αvβ3, αIIbβ3, αvβ5 and α5β1.
By disrupting integrin-mediated adhesion and signalling, echistatin can inhibit
tumour-cell attachment, migration, invasion, proliferation and angiogenesis.
Preclinical cancer studies have shown inhibition of tumour growth and pulmonary
metastasis, particularly in αvβ3-overexpressing osteosarcoma models, and
echistatin has also inhibited migration of melanoma, glioblastoma and pancreatic
cancer cells. Its anticancer activity is therefore primarily associated with
integrin antagonism, especially αvβ3 inhibition. Echistatin
is classified as an experimental peptide/disintegrin rather than as a
natural supplement, and current anticancer evidence is predominantly
preclinical.
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