High molecular weight kininogen as substrate for cathepsin B

High molecular weight kininogen as substrate for cathepsin B

Autor Barros, NMT Google Scholar
Tersariol, ILS Google Scholar
Oliva, MLV Google Scholar
Araujo, M. S. Google Scholar
Sampaio, CAM Google Scholar
Juliano, L. Google Scholar
Motta, G. da Google Scholar
Instituição Universidade Federal de São Paulo (UNIFESP)
UMC
Resumo We investigated the influence of pH and divalent cations (Zn2+, Mg2+ and Ca2+) on high molecular weight kininogen processing by cathepsin B. At pH 6.3, high molecular weight kininogen is hydrolyzed by cathepsin B at three sites generating fragments of 80, 60 and 40 kDa. Cathepsin B has kininogenase activity at this pH which is improved in the absence of divalent cations. At pH 7.35, high molecular weight kininogen is slightly cleaved by cathepsin B into fragments of 60 kDa, and cathepsin B kininogenase activity is impaired. Our results suggest that high molecular weight kininogen is a substrate for cathepsin B under pathophysiological conditions.
Palavra-chave cystatins
cysteine peptidase
kinin
zinc
Idioma Inglês
Data de publicação 2004-06-01
Publicado em Biological Chemistry. Berlin: Walter de Gruyter & Co, v. 385, n. 6, p. 551-555, 2004.
ISSN 1431-6730 (Sherpa/Romeo, fator de impacto)
Publicador Walter de Gruyter & Co
Extensão 551-555
Fonte http://dx.doi.org/10.1515/BC.2004.066
Direito de acesso Acesso restrito
Tipo Artigo
Web of Science WOS:000222500200015
Endereço permanente http://repositorio.unifesp.br/handle/11600/27791

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