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- Title
Identification of prolylcarboxypeptidase as the cell matrix-associated prekallikrein activator
- Authors
Moreira, Claudia R.; Schmaier, Alvin H.; Mahdi, Fakhri; da Motta, Guacyara; Nader, Helena B.; Shariat-Madar, Zia
- Abstract
Investigations determined that the cell matrix-associated prekallikrein (PK) activator is prolylcarboxypeptidase. PK activation on human umbilical vein endothelial cell (HUVEC) matrix is inhibited by antipain (IC50=50 μM) but not anti-factor 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 μM) blocks matrix-associated PK activation. Angiotensin II (IC50=100 μM) 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 μM angiotensin II, 1 μM corn trypsin inhibitor, and 50 μM antipain, but not angiotensin 1–7. 1 mM angiotensin II or 300 μM 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 prolylcarboxypeptidase is the matrix PK activator.
- Subjects
PEPTIDES; PLASMINOGEN activators; ENDOTHELIUM; IMMUNOGLOBULINS
- Publication
FEBS Letters, 2002, Vol 523, Issue 1-3, p167
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/S0014-5793(02)02980-0