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High molecular weight kininogen as substrate for cathepsin B
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N.M.T. Barros
Published/Copyright:
June 1, 2005
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.
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Published Online: 2005-06-01
Published in Print: 2004-06-07
Copyright © 2004 by Walter de Gruyter GmbH & Co. KG
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