High molecular weight kininogen as substrate for cathepsin B

Autor(es)

Barros, NMT ^[1] ; Tersariol, ILS ^[2] ; Oliva, MLV ^[3] ; Araújo, MS ^[4] ; Sampaio, CAM ^[5] ; Juliano, L ^[6] ; da Motta, G ^[7]

Afiliação do(s) autor(es)

^[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

• Tipo de documento: Artigo Científico
• Fonte: Biological Chemistry; v. 385, n. 6, p. 551-555, 2004.

Resumo

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)

• Processo FAPESP: 02/09808-6 - Estudo do processamento enzimático de proteínas plasmáticas envolvidas nos mecanismos hemostáticos
• Beneficiário: Guacyara da Motta
• Modalidade de apoio: Auxílio à Pesquisa - Regular