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Titolo:
The disintegrin-like domain of the snake venom metalloprotease alternagin inhibits alpha 2 beta 1 integrin-mediated cell adhesion
Autore:
Souza, DHF; Iemma, MRC; Ferreira, LL; Faria, JP; Oliva, MLV; Zingali, RB; Niewiarowski, S; Selistre-de-Araujo, HS;
Indirizzi:
Univ Fed Sao Carlos, Dept Ciencias Fisiol, BR-13560 Sao Carlos, SP, BrazilUniv Fed Sao Carlos Sao Carlos SP Brazil BR-13560 Sao Carlos, SP, Brazil Univ Fed Sao Paulo, Dept Bioquim, Sao Paulo, Brazil Univ Fed Sao Paulo Sao Paulo Brazil lo, Dept Bioquim, Sao Paulo, Brazil Fed Univ Rio De Janeiro, Dept Bioquim Med, BR-21941 Rio De Janeiro, BrazilFed Univ Rio De Janeiro Rio De Janeiro Brazil BR-21941 e Janeiro, Brazil Temple Univ, Dept Physiol, Philadelphia, PA 19122 USA Temple Univ Philadelphia PA USA 19122 Physiol, Philadelphia, PA 19122 USA
Titolo Testata:
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
fascicolo: 2, volume: 384, anno: 2000,
pagine: 341 - 350
SICI:
0003-9861(200012)384:2<341:TDDOTS>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
PLATELET-AGGREGATION INHIBITOR; BOTHROPS-JARARACA VENOM; CROTALUS-ATROX VENOM; HEMORRHAGIC METALLOPROTEINASES; TRIMERESURUS-FLAVOVIRIDIS; BIOLOGICAL-ACTIVITY; CONTAINING PEPTIDE; MOLECULAR-CLONING; COLLAGEN RECEPTOR; SEQUENCE-ANALYSIS;
Keywords:
metalloprotease; disintegrin; snake venom; cell adhesion; collagen; alpha(2)beta(1); in tegrin;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
53
Recensione:
Indirizzi per estratti:
Indirizzo: Selistre-de-Araujo, HS Univ Fed Sao Carlos, Dept Ciencias Fisiol, BR-13560Sao Carlos, SP, Brazil Univ Fed Sao Carlos Sao Carlos SP Brazil BR-13560
Citazione:
D.H.F. Souza et al., "The disintegrin-like domain of the snake venom metalloprotease alternagin inhibits alpha 2 beta 1 integrin-mediated cell adhesion", ARCH BIOCH, 384(2), 2000, pp. 341-350

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 ofcells 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.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/07/20 alle ore 22:34:17