Please use this identifier to cite or link to this item: https://repositorio.unifesp.br/handle/11600/28019
Title: Plasma prekallikrein/kallikrein processing by lysosomal cysteine proteases
Authors: Barros, NMT
Puzer, L.
Tersariol, ILS
Oliva, MLV
Sampaio, CAM
Carmona, A. K.
Motta, G. da
Universidade Federal de São Paulo (UNIFESP)
UMC
Keywords: cathepsins
kallikrein
kinin system
proteolysis
Issue Date: 1-Nov-2004
Publisher: Walter de Gruyter & Co
Citation: Biological Chemistry. Berlin: Walter de Gruyter & Co, 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.
URI: http://repositorio.unifesp.br/handle/11600/28019
ISSN: 1431-6730
Other Identifiers: http://dx.doi.org/10.1515/BC.2004.141
Appears in Collections:Em verificação - Geral

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