In:
Proceedings of the National Academy of Sciences, Proceedings of the National Academy of Sciences, Vol. 100, No. 14 ( 2003-07-08), p. 8258-8263
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 protein-coupled 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.
Type of Medium:
Online Resource
ISSN:
0027-8424
,
1091-6490
DOI:
10.1073/pnas.1432869100
Language:
English
Publisher:
Proceedings of the National Academy of Sciences
Publication Date:
2003
detail.hit.zdb_id:
209104-5
detail.hit.zdb_id:
1461794-8
SSG:
11
SSG:
12
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