Pressor activity of angiotensin II-(2-7)-hexapeptide in man.

Kono, Tsuyoshi; Taniguchi, Ataru; Imura, Hiroo; Oseko, Fumimaro; Khosla, M. C.

doi:10.1507/endocrj1954.32.767

Cited by 6 publications

(6 citation statements)

References 6 publications

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“…A previous study 47 reported that Ang2-10 is vasodilatory and antiproliferative whereas another study 55 reported that Ang2-10 was vasoconstrictive, but likely only after conversion to AT3 (2)(3)(4)(5)(6)(7)(8). As for the remaining APs, in humans, Ang(2-7) induces mild vasoconstriction, 56 Ang(3-7) is thought to be a centrally acting vasoconstrictor, 57 and Ang1-5 binds MasR and causes vasodilatation and increased natriuretic peptide release. 58 A third important finding of our study is the ability to shift the balance of APs within the RAAS using rhACE2.…”

Section: Discussionmentioning

confidence: 99%

“…A previous study reported that Ang2‐10 is vasodilatory and antiproliferative whereas another study reported that Ang2‐10 was vasoconstrictive, but likely only after conversion to AT3(2‐8). As for the remaining APs, in humans, Ang(2‐7) induces mild vasoconstriction, Ang(3‐7) is thought to be a centrally acting vasoconstrictor, and Ang1‐5 binds MasR and causes vasodilatation and increased natriuretic peptide release . Thus, results of RAAS AP equilibrium analysis in dogs with CHF receiving ACEI indicated an increase in beneficial APs including Ang1‐9, Ang1‐7, and Ang2‐10; no change in beneficial APs including AT4(3‐8) and Ang1‐5; an increase in maladaptive APs, including Ang2‐7 and Ang3‐7; and no change in maladaptive APs including AT2(1‐8) and AT3(2‐8).…”

Section: Discussionmentioning

confidence: 99%

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Plasma and tissue angiotensin‐converting enzyme 2 activity and plasma equilibrium concentrations of angiotensin peptides in dogs with heart disease

Larouche‐Lebel

Loughran

Oyama

et al. 2019

Veterinary Internal Medicne

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Background Angiotensin‐converting enzyme 2 (ACE2) is a homologue of angiotensin‐converting enzyme (ACE) and produces angiotensin peptides (APs), such as angiotensin 1‐9 and 1‐7 that are vasodilatory and natriuretic, and act to counterbalance angiotensin II. Hypothesis Evidence of ACE2 can be found in tissues and plasma of dogs. Equilibrium concentrations of renin angiotensin aldosterone system (RAAS) APs differ in dogs with heart disease compared to healthy dogs and recombinant human ACE2 (rhACE2) alters relative concentrations of APs. Animals Forty‐nine dogs with and 34 dogs without heart disease. Methods Immunohistochemistry and assays for tissue and plasma ACE2 activity and equilibrium concentrations of plasma RAAS APs were performed. Results Immunolabeling for ACE2 was present in kidney and myocardial tissue. Median plasma ACE2 activity was significantly increased in dogs with congestive heart failure (CHF; 6.9 mU/mg; interquartile range [IQR], 5.1‐12.1) as compared to control (2.2 mU/mg; IQR, 1.8‐3.0; P = .0003). Plasma equilibrium analysis of RAAS APs identified significant increases in the median concentrations of beneficial APs, such as angiotensin 1‐7, in dogs with CHF (486.7 pg/mL; IQR, 214.2‐1168) as compared to those with preclinical disease (41.0 pg/mL; IQR, 27.4‐45.1; P < .0001) or control (11.4 pg/mL; IQR, 7.1‐25.3; P = .01). Incubation of plasma samples from dogs with CHF with rhACE2 increased beneficial APs, such as angiotensin 1‐9 (preincubation, 10.3 pg/mL; IQR, 4.4‐37.2; postincubation, 2431 pg/mL; IQR, 1355‐3037; P = .02), while simultaneously decreasing maladaptive APs, such as angiotensin II (preincubation, 53.4 pg/mL; IQR, 28.6‐226.4; postincubation, 2.4 pg/mL; IQR, 0.50‐5.8; P = .02). Conclusions and Clinical Importance Recognition of the ACE2 system expands the conventional view of the RAAS in the dog and represents an important potential therapeutic target.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Plasma and tissue angiotensin‐converting enzyme 2 activity and plasma equilibrium concentrations of angiotensin peptides in dogs with heart disease

Larouche‐Lebel

Loughran

Oyama

et al. 2019

Veterinary Internal Medicne

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“…Actions of Ang (1–7) are associated with vasodilation and cardioprotection, as well as decreased hypertrophy, fibrosis, and thrombosis [32]. Further aminopeptidase activity on Ang (1–7) produces Ang (2–7) and Ang (3–7), which may also have biological activity [33]–[35].…”

Section: Introductionmentioning

confidence: 99%

Distribution of Non-AT1, Non-AT2 Binding of 125I-Sarcosine1, Isoleucine8 Angiotensin II in Neurolysin Knockout Mouse Brains

et al. 2014

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The recent identification of a novel binding site for angiotensin (Ang) II as the peptidase neurolysin (E.C. 3.4.24.16) has implications for the renin-angiotensin system (RAS). This report describes the distribution of specific binding of 125I-Sarcosine1, Isoleucine8 Ang II (125I-SI Ang II) in neurolysin knockout mouse brains compared to wild-type mouse brains using quantitative receptor autoradiography. In the presence of p-chloromercuribenzoic acid (PCMB), which unmasks the novel binding site, widespread distribution of specific (3 µM Ang II displaceable) 125I-SI Ang II binding in 32 mouse brain regions was observed. Highest levels of binding >700 fmol/g initial wet weight were seen in hypothalamic, thalamic and septal regions, while the lowest level of binding <300 fmol/g initial wet weight was in the mediolateral medulla. 125I-SI Ang II binding was substantially higher by an average of 85% in wild-type mouse brains compared to neurolysin knockout brains, suggesting the presence of an additional non-AT1, non-AT2, non-neurolysin Ang II binding site in the mouse brain. Binding of 125I-SI Ang II to neurolysin in the presence of PCMB was highest in hypothalamic and ventral cortical brain regions, but broadly distributed across all regions surveyed. Non-AT1, non-AT2, non-neurolysin binding was also highest in the hypothalamus but had a different distribution than neurolysin. There was a significant reduction in AT2 receptor binding in the neurolysin knockout brain and a trend towards decreased AT1 receptor binding. In the neurolysin knockout brains, the size of the lateral ventricles was increased by 56% and the size of the mid forebrain (−2.72 to +1.48 relative to Bregma) was increased by 12%. These results confirm the identity of neurolysin as a novel Ang II binding site, suggesting that neurolysin may play a significant role in opposing the pathophysiological actions of the brain RAS and influencing brain morphology.

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“…Ang (2-7) exhibits a slight pressor effect in healthy humans (25), although its endogenous production and physiologic role are yet to be determined. Ang (3)(4)(5)(6)(7) is an Ang fragment that has been identified in rat brain tissue (26).…”

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confidence: 99%

Endothelial Metabolism of Angiotensin II to Angiotensin III, not Angiotensin (1–7), Augments the Vasorelaxation Response in Adrenal Cortical Arteries

Kopf

Campbell

2013

Endocrinology

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Hyperaldosteronism is linked to the development and progression of several different cardiovascular diseases. Angiotensin (Ang) II increases aldosterone secretion and adrenal blood flow. Ang II peptide fragments are produced by various peptidases, and these Angs have diverse and vital physiologic roles. Due to the uncharacteristic vasorelaxation of adrenal arteries by Ang II, we tested the hypothesis that Ang II metabolism contributes to its relaxant activity in adrenal arteries. Metabolism of Angs by bovine adrenal cortical arteries and isolated bovine adrenal vascular cells was measured by liquid chromatography-mass spectrometry. The primary Ang metabolites of adrenal arteries are Ang III and Ang (1-7), with Ang IV produced to a lesser extent. Bovine microvascular endothelial cells produced a similar metabolic profile to adrenal arteries, whereas bovine adrenal artery smooth muscle cells exhibited less metabolism. In preconstricted adrenal arteries, Ang II caused relaxation in picomolar concentrations and constrictions at 10nM. Ang-converting enzyme 2 inhibition augmented this relaxation response, whereas aminopeptidase inhibition did not. Ang III was equipotent to Ang II in relaxing adrenal arteries. Ang IV did not cause relaxation. Nitric oxide synthase inhibition enhanced Ang II-induced constriction of adrenal arteries. Aminopeptidase inhibition increased the concentration range for Ang II-induced constriction of adrenal arteries. Ang III and Ang IV did not change the basal tone but caused constriction of adrenal arteries with nitric oxide synthase inhibition. These data indicate that Ang II metabolism modulates the vascular effects of Ang II in the adrenal vasculature.

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Pressor activity of angiotensin II-(2-7)-hexapeptide in man.

Cited by 6 publications

References 6 publications

Plasma and tissue angiotensin‐converting enzyme 2 activity and plasma equilibrium concentrations of angiotensin peptides in dogs with heart disease

Plasma and tissue angiotensin‐converting enzyme 2 activity and plasma equilibrium concentrations of angiotensin peptides in dogs with heart disease

Distribution of Non-AT1, Non-AT2 Binding of 125I-Sarcosine1, Isoleucine8 Angiotensin II in Neurolysin Knockout Mouse Brains

Endothelial Metabolism of Angiotensin II to Angiotensin III, not Angiotensin (1–7), Augments the Vasorelaxation Response in Adrenal Cortical Arteries

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