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N.M.T. Barros, I.L.S. Tersariol, M.L.V. Oliva, M.S. Araújo, C.A.M. Sampaio, L. Juliano, G. da Motta

High molecular weight kininogen as substrate for cathepsin B

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.

Biological Chemistry, Walter de Gruyter

Print ISSN: 1431-6730
Volume: 385, 06/2004
Pages: 551 - 555

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