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High molecular weight kininogen as substrate for cathepsin B

Date
2004-06-01
Author
Barros, NMT
Tersariol, ILS
Oliva, MLV
Araujo, M. S.
Sampaio, CAM
Juliano, L.
Motta, G. da
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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.
URI
http://repositorio.unifesp.br/handle/11600/27791
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  • EPM - Artigos [13559]

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