(Hypertension. 2001;38:660.)
© 2001 American Heart Association, Inc.
Renin-Angiotensin System |
Laboratório de Hipertensão, Instituto de Ciências Biológicas (R.A.S.d.S., K.T.P.) and Departamento de Pediatria, Fac. Medicina (C.S.S.), Universidade Federal de Minas Gerais, Belo Horizonte, Brazil; Departamento de Biofísica, Universidade Federal de São Paulo (J.B.P.), 04023-062, São Paulo, São Paulo; and Max-Delbrück-Center for Molecular Medicine (M.B.), Berlin-Buch, Germany.
Correspondence to Robson A.S. Santos, Departamento de Fisiologia e Biofísica, Av. Antonio Carlos, 6627-ICB-UFMG, 31270-901-Belo Horizonte, MG, Brazil. E-mail marrob{at}dedalus.lcc.ufmg.br
Abstract
Abstract The heptapeptide angiotensin (Ang)-(1-7) is currently considered one of the biologically active end products of the renin-angiotensin system. The formation of Ang-(1-7) by pathways independent of Ang II generation, the selectivity of its actions, and its peculiar property of exhibiting effects that are partially opposite of those of the parent compound, Ang II, confer a unique biochemical and functional profile to this peptide. In this article, we will review novel aspects of the biological actions of Ang-(1-7), dealing with its interaction with Ang II and kinins, especially in the kidney and blood vessels.
Key Words: bradykinin renin-angiotensin system receptors, angiotensin
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