Cardiovascular actions of angiotensin-(1-7)

Ferreira, Anderson J.; Santos, Robson Augusto Souza

doi:10.1590/s0100-879x2005000400003

Cited by 147 publications

(124 citation statements)

References 56 publications

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“…It has been shown, in rats and humans that ACE inhibitors can decrease body weight (34 -36). Furthermore, many studies have shown that Ang-(1-7) can counter-regulate Ang II actions and participate in the ACE inhibitor effects (37,38). Our data showing an increased fat mass in Mas-KO mice suggest that the Ang-(1-7)/Mas axis is crucial in the control of fat accumulation and lipolysis.…”

Section: Discussionsupporting

confidence: 49%

Mas Deficiency in FVB/N Mice Produces Marked Changes in Lipid and Glycemic Metabolism

Santos

Fernandes²,

Mario³

et al. 2008

Diabetes

224

184

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OBJECTIVE-Metabolic syndrome is characterized by the variable coexistence of obesity, hyperinsulinemia, insulin resistance, dyslipidemia, and hypertension. It is well known that angiotensin (Ang) II is importantly involved in the metabolic syndrome. However, the role of the vasodilator Ang-(1-7)/Mas axis is not known. The aim of this study was to evaluate the effect of genetic deletion of the G protein-coupled receptor, Mas, in the lipidic and glycemic metabolism in FVB/N mice. RESULTS-Despite normal body weight, Mas-knockout (Mas-KO) mice presented dyslipidemia, increased levels of insulin and leptin, and an ϳ50% increase in abdominal fat mass. In addition, Mas gene-deleted mice presented glucose intolerance and reduced insulin sensitivity as well as a decrease in insulin-stimulated glucose uptake by adipocytes and decreased GLUT4 in adipose tissue. Mas Ϫ/Ϫ presented increased muscle triglycerides, while liver triglyceride levels were normal. Expression of TGF-␤ and AGT genes was higher in Mas-KO animals in comparison with controls. RESEARCH DESIGN AND METHODS-Plasma CONCLUSIONS-These results show that

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Section: Discussionsupporting

confidence: 49%

Mas Deficiency in FVB/N Mice Produces Marked Changes in Lipid and Glycemic Metabolism

Santos

Fernandes²,

Mario³

et al. 2008

Diabetes

224

184

View full text Add to dashboard Cite

show abstract

“…Ang(1-7) has been shown to cause vasorelaxation in multiple vascular beds [7][8][9][10][11] through the release of vasodilator prostaglandins, nitric oxide and endothelial-derived relaxing factor. 7,12 With regard to the heart, Ang(1-7) can decrease hypertrophy and fibrosis induced by Ang II. 13 Additionally, ACE2 overexpression in the heart has been shown to protect against cardiac damage induced by Ang II or seen in spontaneously hypertensive rats (SHR).…”

Section: Introductionmentioning

confidence: 99%

Simultaneous administration of Ang(1-7) or A-779 does not affect the chronic hypertensive effects of angiotensin II in normal rats

Collister

Nahey

2010

J Renin Angiotensin Aldosterone Syst

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“…ACE2 has a high affinity for Ang II to form Ang (1-7), which is also formed by the action of ACE on Ang (1-9). 47,48 Possibly the degradation of Ang I can also result from the action of ACE, due to high levels of activity and protein expression found in this study. As described in the literature, ACE 3,4 and/or tonin 13,21,22 pathways may contribute to the low levels of Ang I.…”

Section: Discussionmentioning

confidence: 70%

Characterization of the renal renin-angiotensin system in transgenic mice that express rat tonin

Ribeiro

Palomino

Lima

et al. 2015

J Renin Angiotensin Aldosterone Syst

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Introduction: Tonin is an enzyme that is able to generate angiotensin II (Ang II) from angiotensin I (Ang I) or directly from angiotensinogen. Our goal was to characterize the renal renin-angiotensin system in transgenic mice that express rat tonin (TGM`(rTon)). Materials and methods: Mice were euthanized and the kidneys removed for analysis. Tonin activity was evaluated by radioimmunoassay and angiotensin I-converting enzyme (ACE) activity by HPLC. Tonin, ACE and angiotensin II-converting enzyme (ACE2) expression was analyzed by Western blotting. Results: Tonin activity was significantly increased in TGM`(rTon) compared to their respective wild-type (WT) littermates (1.7 ± 0.21 vs 0.11 ± 0.02 nmol of Ang II/min/mg of protein). Tonin activity had a strong positive correlation with tonin expression in both TGM`(rTon) and their respective wild-type littermates. The ACE activity and expression levels of 65-kDa N-domain angiotensin I-converting enzyme isoform were significantly increased in the TGM`(rTon) when compared with WT. ACE2 expression levels were statistically significantly higher in the TGM`(rTon) when compared with WT. Angiotensin 1–7 (Ang(1–7)) and Ang I levels were significantly lower in the TGM`(rTon). Conclusions: We suggest that the environment of tonin abundance may increase N-domain ACE activity liberated by a secretase able to cleave somatic ACE.

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Cardiovascular actions of angiotensin-(1-7)

Abstract: Angiotensin-

Cited by 147 publications

References 56 publications

Mas Deficiency in FVB/N Mice Produces Marked Changes in Lipid and Glycemic Metabolism

Mas Deficiency in FVB/N Mice Produces Marked Changes in Lipid and Glycemic Metabolism

Simultaneous administration of Ang(1-7) or A-779 does not affect the chronic hypertensive effects of angiotensin II in normal rats

Characterization of the renal renin-angiotensin system in transgenic mice that express rat tonin

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