Identification of prolylcarboxypeptidase as the cell matrix-associated prekallikrein activator

Identification of prolylcarboxypeptidase as the cell matrix-associated prekallikrein activator

Author Moreira, Claudia Regina Autor UNIFESP Google Scholar
Schmaier, A. H. Google Scholar
Mahdi, F. Google Scholar
Motta, Guacyara da Autor UNIFESP Google Scholar
Nader, Helena Bonciani Autor UNIFESP Google Scholar
Shariat-Madar, Z. Google Scholar
Institution Univ Michigan
Universidade Federal de São Paulo (UNIFESP)
Abstract Investigations determined that the cell matrix-associated prekallikrein (PK) activator is prolylearboxypeptidase. PK activation on human umbilical vein endothelial cell (HUVEC) matrix is inhibited by antipain (IC50 = 50 muM) but not antifactor XIIa antibody, 3 mM benzamidine, 5 mM iodoacetic acid or iodoacetamide, or 3 mM N-ethylmaleimide. Corn trypsin inhibitor (IC50 = 100 nM) or Fmoc-aminoacylpyrrolidine-2-nitrile (IC50 = 100 muM) blocks matrix-associated PK activation. Angiotensin II (IC50 = 100 muM) or bradykinin (IC50 = 3 mM), but not angiotensin 1-7 or bradykinin 1-5, inhibits matrix-associated PK activation. ECV304 cell matrix PK activator also is blocked by 100 muM angiotensin II, 1 muM corn trypsin inhibitor, and 50 muM antipain, but not angiotensin 1-7. 1 mM angiotensin 11 or 300 muM Fmoc-aminoacylpyrrolidine-2-nitrile indirectly blocks plasminogen activation by inhibiting kallikrein formation for single chain urokinase activation. On immunoblot, prolylcarboxypeptidase antigen is associated with HUVEC matrix. These studies indicate that prolylearboxypeptidase is the matrix PK activator. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
Keywords prolylcarboxypeptidase
lysosomal carboxypeptidase
angiotensinase C
prekallikrein
single chain urokinase
angiotensin II
bradykinin
Language English
Date 2002-07-17
Published in Febs Letters. Amsterdam: Elsevier B.V., v. 523, n. 1-3, p. 167-170, 2002.
ISSN 0014-5793 (Sherpa/Romeo, impact factor)
Publisher Elsevier B.V.
Extent 167-170
Origin http://dx.doi.org/10.1016/S0014-5793(02)02980-0
Access rights Open access Open Access
Type Article
Web of Science ID WOS:000177219300034
URI http://repositorio.unifesp.br/handle/11600/26931

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