High molecular weight kininogen as substrate for cathepsin B

High molecular weight kininogen as substrate for cathepsin B

Author 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
Institution Universidade Federal de São Paulo (UNIFESP)
Abstract 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.
Keywords cystatins
cysteine peptidase
Language English
Date 2004-06-01
Published in Biological Chemistry. Berlin: Walter de Gruyter & Co, v. 385, n. 6, p. 551-555, 2004.
ISSN 1431-6730 (Sherpa/Romeo, impact factor)
Publisher Walter de Gruyter & Co
Extent 551-555
Origin http://dx.doi.org/10.1515/BC.2004.066
Access rights Closed access
Type Article
Web of Science ID WOS:000222500200015
URI http://repositorio.unifesp.br/handle/11600/27791

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