Role of PGI(2) and effects of ACE inhibition on the bradykinin potentiation by angiotensin-(1-7) in resistance vessels of SHR

Role of PGI(2) and effects of ACE inhibition on the bradykinin potentiation by angiotensin-(1-7) in resistance vessels of SHR

Autor Fernandes, L. Google Scholar
Fortes, Z. B. Google Scholar
Casarini, D. E. Google Scholar
Nigro, D. Google Scholar
Tostes, RCA Google Scholar
Santos, RAS Google Scholar
Carvalho, MHC de Google Scholar
Instituição Universidade de São Paulo (USP)
Universidade Federal de São Paulo (UNIFESP)
Universidade Federal de Minas Gerais (UFMG)
Resumo The present study determined the participation of PGI(2) in the angiotensin-(1-7) [Ang-(1-7)libradykinin (BK) interaction, in the presence and absence of Angiotensin Converting Enzyme (ACE) inhibition, trying to correlate it with tissue levels of both peptides. the isolated mesenteric arteriolar bed of Spontaneously Hypertensive Rats (SHR) was perfused with Krebs or Krebs plus enalaprilat (10 DM), and drugs were injected alone or in association. BK (10 nM)-induced relaxation was potentiated by Ang-(1-7) (2.2 mug) in the presence or absence of enalaprilat. Ang-(1-7) receptor blockade [A-779 (4.8 mug)] did not interfere with the BK effect in preparations perfused with normal Krebs, but reversed the increased BK relaxation observed after ACE inhibition. PGI(2) release by mesenteric vessels was not altered by BK or Ang-(1-7) alone, but was increased when both peptides were injected in association, in the absence or in the presence of enalaprilat. ACE inhibition caused a 2-fold increase in the BK tissue levels, and a significant decrease in the Ang-(1-7) values. We conclude that endogenous Ang-(1-7) has an important contribution to the effect of ACE inhibitors participating in the enhancement of BK response. the mechanism of Ang-(1-7) potentiating effect probably involves an increased production of PGI(2). Our results suggest that a different enzymatic pathway (non-related to ACE) is involved in the local Ang-(1-7) metabolism. (C) 2004 Elsevier B.V. All rights reserved.
Palavra-chave angiotensin
angiotensin-converting enzyme
renin-angiotensin system
Idioma Inglês
Data de publicação 2005-04-15
Publicado em Regulatory Peptides. Amsterdam: Elsevier B.V., v. 127, n. 1-3, p. 183-189, 2005.
ISSN 0167-0115 (Sherpa/Romeo, fator de impacto)
Publicador Elsevier B.V.
Extensão 183-189
Direito de acesso Acesso restrito
Tipo Artigo
Web of Science WOS:000227023900022
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