Assembly of high molecular weight kininogen and activation of prekallikrein on cell matrix

Assembly of high molecular weight kininogen and activation of prekallikrein on cell matrix

Author Motta, G. Google Scholar
Shariat-Madar, Z. Google Scholar
Mahdi, F. Google Scholar
Sampaio, Claudio AM Autor UNIFESP Google Scholar
Schmaier, A. H. Google Scholar
Institution Universidade Federal de São Paulo (UNIFESP)
Univ Michigan
Abstract Investigations determined if extracellular matrix of endothelial cells (EC) is a platform for HK assembly and PK activation. In buffers containing bovine serum albumin, biotin-RK binding to ECV304 cells or their matrix requires greater than or equal to 50 muM added Zn2+. Ortho-phenanthroline or a HK domain 5 peptide blocks HK binding, Binding to umbilical vein EC or matrix, but not ECV304 cells or matrix, is mediated by cytokeratin 1. Biotin-HK binds to ECV304 cells or matrix with a K-d of 15.8 or 9.0 nM and a B-max of 2.6 X 10(7) or 21.4 X 10(7) sites/cell, respectively. PK activation un ECV304 cells or matrix is blocked by antipain or SBTI and corn trypsin inhibitor partially inhibits kallikrein formation. PK activation occurs on ECV304 cells or matrix prepared without serum or in human factor XII deficient serum. indicating that the PK activator is not factor XIIa. EC matrix promotes plasminogen activation after the assembly of HK, PK and pro-urokinase. These studies indicate that matrix of various EC has the ability to assemble HK allowing for PK activation and subsequent activities.
Keywords HMW kininogen
prekallikrein
endothelial cells
extracellular matrix
pro-urokinase
plasminogen
Language English
Date 2001-09-01
Published in Thrombosis And Haemostasis. Stuttgart: F K Schattauer Verlag Gmbh, v. 86, n. 3, p. 840-847, 2001.
ISSN 0340-6245 (Sherpa/Romeo, impact factor)
Publisher F K Schattauer Verlag Gmbh
Extent 840-847
Access rights Closed access
Type Article
Web of Science ID WOS:000170992600019
URI http://repositorio.unifesp.br/11600/45660

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