Characterization of a monomeric disintegrin, ocellatusin, present in the venom of the Nigerian carpet viper, Echis ocellatus

35Citations
Citations of this article
25Readers
Mendeley users who have this article in their library.

Abstract

Ocellatusin is a new RGD-containing short monomeric disintegrin. It is a better inhibitor of α5β1 integrin and a more potent inducer of the expression of a ligand-induced binding site epitope on β1 integrin subunit than echistatin. In further contrast to echistatin, ocellatusin has a direct chemotactic stimulus on human neutrophils in vitro. The distinct effects of these two close evolutionarily related disintegrins might be explained by the presence of methionine-22 and histidine-29 in the RGD loop of ocellatusin, which are arginine and aspartic acid, respectively, in echistatin. These mutations may modulate the conformation and/or recognition properties of the integrin-binding loop of ocellatusin. © 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

Cite

CITATION STYLE

APA

Smith, J. B., Theakston, R. D. G., Coelho, A. L. J., Barja-Fidalgo, C., Calvete, J. J., & Marcinkiewicz, C. (2002). Characterization of a monomeric disintegrin, ocellatusin, present in the venom of the Nigerian carpet viper, Echis ocellatus. FEBS Letters, 512(1–3), 111–115. https://doi.org/10.1016/S0014-5793(02)02233-0

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free