Plasma prekallikrein/kallikrein processing by lysosomal cysteine proteases

Barros, NMT; Puzer, L; Tersariol, ILS; Oliva, MLV; Sampaio, CAM; Carmona, AK; 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.)

Plasma prekallikrein/kallikrein processing by lysosomal cysteine proteases

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Author(s):	Barros, NMT ; Puzer, L ; Tersariol, ILS ; Oliva, MLV ; Sampaio, CAM ; Carmona, AK ; da Motta, G ^[7] Total Authors: 7
Document type:	Journal article
Source:	Biological Chemistry; v. 385, n. 11, p. 1087-1091, 2004.
Abstract
Plasma kallikrein plays a role in coagulation, fibrinolysis and inflammation. Cathepsins B and L participate in (patho)physiological processes such as peptide antigen processing, tissue remodeling events, protein turnover in cells, hormone processing and tumor invasion. The present work analyzes the processing of prekallikrein/kallikrein by lysosomal cathepsins. Prekallikrein is not hydrolyzed by catB, and catL generates an inactive fragment of prekallikrein. Both kallikrein chains are hydrolyzed by catL and the light chain is mainly hydrolyzed by catB; kallikrein activity is lower after incubation with catL compared to catB. Our data suggest that the plasma kallikrein/ kinin system can be controlled by cathepsins. (AU)

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