Angiotensin-(1-7) is an endogenous ligand for the G protein-coupled receptor Mas.

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Date
2003
Authors
Santos, Robson Augusto Souza dos
Silva, Ana Cristina Simões e
Maric, Christine
Rabelo, Denise Maria Rover da Silva
Machado, Raquel do Pilar
Buhr, Insa de
Walther, Silvia Heringer
Pinheiro, Sérgio Veloso Brant
Lopes, Miriam Teresa Paz
Bader, Michael
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Abstract
The renin–angiotensin system plays a critical role in blood pressure control and body fluid and electrolyte homeostasis. Besides angiotensin (Ang) II, other Ang peptides, such as Ang III [Ang-(2–8)], Ang IV [Ang-(3–8)], and Ang-(1–7) may also have important biological activities. Ang-(1–7) has become an angiotensin of interest in the past few years, because its cardiovascular and baroreflex actions counteract those of Ang II. Unique angiotensin-binding sites specific for this heptapeptide and studies with a selective Ang-(1–7) antagonist indicated the existence of a distinct Ang-(1–7) receptor. We demonstrate that genetic deletion of the G proteincoupled receptor encoded by the Mas protooncogene abolishes the binding of Ang-(1–7) to mouse kidneys. Accordingly, Mas-deficient mice completely lack the antidiuretic action of Ang-(1–7) after an acute water load. Ang-(1–7) binds to Mas-transfected cells and elicits arachidonic acid release. Furthermore, Mas-deficient aortas lose their Ang-(1–7)-induced relaxation response. Collectively, these findings identify Mas as a functional receptor for Ang-(1–7) and provide a clear molecular basis for the physiological actions of this biologically active peptide.
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Keywords
Binding, Mas protooncogene, Renin angiotensin system
Citation
SANTOS, R. A. S. et al. Angiotensin-(1-7) is an endogenous ligand for the G protein-coupled receptor Mas. Proceedings National Academy Science, v. 100, n.14, p. 8258-8263, 2003. Disponível em: <http://www.pnas.org/content/100/14/8258.long>. Acesso em: 23 fev. 2017.
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