The disintegrin-like domain of the snake venom metalloprotease alternagin inhibits alpha 2 beta 1 integrin-mediated cell adhesion

The disintegrin-like domain of the snake venom metalloprotease alternagin inhibits alpha 2 beta 1 integrin-mediated cell adhesion

Author Souza, DHF Google Scholar
Iemma, MRC Google Scholar
Ferreira, L. L. Google Scholar
Faria, J. P. Google Scholar
Oliva, MLV Google Scholar
Zingali, R. B. Google Scholar
Niewiarowski, S. Google Scholar
Selistre-de-Araujo, H. S. Google Scholar
Institution Universidade Federal de São Carlos (UFSCar)
Universidade Federal de São Paulo (UNIFESP)
Fed Univ Rio de Janeiro
Temple Univ
Abstract The alpha (2)beta (1) integrin is a major collagen receptor that plays an essential role in the adhesion of normal and tumor cells to the extracellular matrix. Here we describe the isolation of a novel metalloproteinase/disintegrin, which is a potent inhibitor of the collagen binding to alpha (2)beta (1) integrin. This 55-kDa protein (alternagin) and its disintegrin domain (alternagin-C) were isolated from Bothrops alternatus snake venom. Amino acid sequencing of alternagin-C revealed the disintegrin structure. Alternagin and alternagin-C inhibit collagen I-mediated adhesion of K562-alpha (2)beta (1)-transfected cells, the IC50 was 134 and 100 nM for alternagin and alternagin-C, respectively. Neither protein interfered with the adhesion of cells expressing alpha (IIb)beta (3), alpha (1)beta (1), alpha (5)beta (1), alpha (4)beta (1) alpha (v)beta (3), and alpha (9)beta (1) integrins to other ligands such as fibrinogen, fibronectin, and collagen IV. Alternagin and alternagin-C also mediated the adhesion of the K562-alpha (2)beta (1)-transfected cells. Our results show that the disintegrin-like domain of alternagin is responsible for its ability to inhibit collagen binding to alpha (2)beta (1) integrin. (C) 2000 Academic Press.
Keywords metalloprotease
disintegrin
snake venom
cell adhesion
collagen
alpha(2)beta(1)
in tegrin
Language English
Date 2000-12-15
Published in Archives of Biochemistry and Biophysics. San Diego: Academic Press Inc, v. 384, n. 2, p. 341-350, 2000.
ISSN 0003-9861 (Sherpa/Romeo, impact factor)
Publisher Academic Press Inc
Extent 341-350
Origin http://dx.doi.org/10.1006/abbi.2000.2120
Access rights Closed access
Type Article
Web of Science ID WOS:000166154200016
URI http://repositorio.unifesp.br/handle/11600/26430

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