Please use this identifier to cite or link to this item: https://repositorio.unifesp.br/handle/11600/29086
Title: Heparin modulation of human plasma kallikrein on different substrates and inhibitors
Authors: Gozzo, Andrezza Justino [UNIFESP]
Nunes, Viviane A. [UNIFESP]
Cruz-Silva, Ilana [UNIFESP]
Carmona, Adriana K. [UNIFESP]
Nader, Helena Bonciani [UNIFESP]
Faljoni-Alario, Adelaide
Sampaio, Misako U. [UNIFESP]
Araujo, Mariana S. [UNIFESP]
Universidade Federal de São Paulo (UNIFESP)
Universidade de São Paulo (USP)
Keywords: antithrombin
C1-inhibitor
factor XII
glycosaminoglycans
plasminogen
synthetic substrates
Issue Date: 1-Aug-2006
Publisher: Walter de Gruyter & Co
Citation: Biological Chemistry. Berlin: Walter de Gruyter & Co, v. 387, n. 8, p. 1129-1138, 2006.
Abstract: The interplay of different proteases and glycosaminoglycans is able to modulate the activity of the enzymes and to affect their structures. Human plasma kallikrein ( huPK) is a proteolytic enzyme involved in intrinsic blood clotting, the kallikrein-kinin system and fibrinolysis. We investigated the effect of heparin on the action, inhibition and secondary structure of huPK. the catalytic efficiency for the hydrolysis of substrates by huPK was determined by Michaelis-Menten kinetic plots: 5.12 x 10(4) M-1 S-1 for acetyl-Phe-Arg-p-nitroanilide, 1.40 x 10(5) M-1 S-1 for H-D-ProPhe-Arg-p-nitroanilide, 2.25 x 10(4) M-1 S-1 for Abz-Gly-Phe-Ser-Pro-Phe-Arg-Ser-Ser-Arg-Gln-EDDnp, 4.24 x 10(2) M-1 S-1 for factor XII and 5.58 x 10(2) M-1 S-1 for plasminogen. Heparin reduced the hydrolysis of synthetic substrates ( by 2.0-fold), but enhanced factor XII and plasminogen hydrolysis ( 7.7- and 1.4-fold, respectively). the second-order rate constants for inhibition of huPK by antithrombin and C1-inhibitor were 2.40 x 10(2) M-1 S-1 and 1.70 x 10(4) M-1 S-1, respectively. Heparin improved the inhibition of huPK by these inhibitors ( 3.4- and 1.4-fold). Despite the fact that huPK was able to bind to a heparin-Sepharose matrix, its secondary structure was not modified by heparin, as monitored by circular dichroism. These actions may have a function in the control or maintenance of some pathophysiological processes in which huPK participates.
URI: http://repositorio.unifesp.br/handle/11600/29086
ISSN: 1431-6730
Other Identifiers: http://dx.doi.org/10.1515/BC.2006.139
Appears in Collections:Artigo

Files in This Item:
There are no files associated with this item.


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.