Thimet oligopeptidase EC is a major liver kininase

Thimet oligopeptidase EC is a major liver kininase

Autor Molina, H. M. Google Scholar
Carmona, A. K. Google Scholar
Kouyoumdjian, M. Google Scholar
Borges, D. R. Google Scholar
Instituição Universidade Federal de São Paulo (UNIFESP)
Resumo Bradykinin (BK) is a potent hepato-portal hypertensive agent although it is efficiently inactivated by the liver. the organ converts angiotensin I to All, but at a much slower rate than it inactivates BK, We had previously identified EC as an hepatic bradykinin inactivating endopeptidase that hydrolyzes BE; at the F-5-S-6 bond. the aim of this study was to determine the relative importance of BIE, as compared to other kininases, in normal, cirrhotic or inflamed rat livers, as well as in samples of human liver. Using specific substrates and inhibitors we showed that: 1) purified BIE preparation hydrolyzed BE( and a BK analogue (BK-Q) with similar efficacy; BK-Q was functionally active since it caused an increase in hepato-portal pressure, as did BK itself. 2) BK degradation in rat serum was performed by ACE since BIE and prolylendopeptidase (PEP) activities were negligible. 3) normal rat liver homogenate contained a large amount of BIE activity which was eliminated by a specific EC inhibitor; ACE and PEP activities were negligible. 4) Then was no difference (p>0.05) in BIE activity in the liver homogenates from rats with normal, inflamed or cirrhotic livers. 5) BIE activity was efficiently removed from livers (normal, inflamed or cirrhotic) that were perfused with TritonX-100. 6) Human liver had an similar enzymatic pattern although ACE activity was detected. We concluded that in normal, inflamed or cirrhotic rat livers, as well as in the human liver, the bradykinin inactivating endopeptidase CEC, and not ACE, is the major hepatic kininase. (C) 2000 Elsevier Science inc. All rights reserved.
Assunto bradykinin
liver inactivation
liver enzymes EC
major ever kininase
thimet oligopeptidase
bradykinin-inactivating enzyme
Idioma Inglês
Data 2000-06-23
Publicado em Life Sciences. Oxford: Pergamon-Elsevier B.V., v. 67, n. 5, p. 509-520, 2000.
ISSN 0024-3205 (Sherpa/Romeo, fator de impacto)
Editor Elsevier B.V.
Extensão 509-520
Direito de acesso Acesso restrito
Tipo Artigo
Web of Science WOS:000087861000003

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