High molecular weight kininogen as substrate for cathepsin B

Barros, NMT; Tersariol, ILS; Oliva, MLV; Araújo, MS; Sampaio, CAM; Juliano, L; da Motta, G

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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

High molecular weight kininogen as substrate for cathepsin B

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Author(s):	Barros, NMT ^[1] ; Tersariol, ILS ^[2] ; Oliva, MLV ^[3] ; Araújo, MS ^[4] ; Sampaio, CAM ^[5] ; Juliano, L ^[6] ; da Motta, G ^[7] Total Authors: 7
Affiliation:	^[1] UNIFESP/EPM - Brasil ^[2] Centro Interdisciplinar de Investigações Bioquímicas, UMC - Brasil ^[3] UNIFESP/EPM - Brasil ^[4] UNIFESP/EPM - Brasil ^[5] UNIFESP/EPM - Brasil ^[6] UNIFESP/EPM - Brasil ^[7] UNIFESP/EPM - Brasil Total Affiliations: 7
Document type:	Journal article
Source:	Biological Chemistry; v. 385, n. 6, p. 551-555, 2004.
Abstract
We investigated the influence of pH and divalent cations (Zn[2+], Mg[2+] and Ca[2+]) 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. (AU)

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