Converting enzyme activity and angiotensin metabolism in the dog brainstem.

Santos, Robson Augusto Souza; Brosnihan, K. Bridget; Chappell, Mark C.; Pesquero, Jorge L.; Chernicky, Cheryl L.; Greene, Lewis Joel; Ferrario, Carlos M.

doi:10.1161/01.hyp.11.2_pt_2.i153

Cited by 146 publications

(98 citation statements)

References 14 publications

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“…26 Although the present experiments did not evaluate whether local conversion of Ang II to Ang-(l-7) contributed to these responses, several observations suggest that it is unlikely. First, we have shown that in medial NTS neurons that were excited by both Ang II and Ang-(l-7), the latency to peak excitation was similar for both Ang peptides.…”

Section: Discussionmentioning

confidence: 68%

Functional interactions between angiotensin II and substance P in the dorsal medulla.

1991

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be located presynaptically on SP-containing vagal afferent fibers, whereas SP binding sites are likely to be associated with intrinsic medial NTS cells. Moreover, recent studies 9 -11 reveal that SP has cardiovascular actions within the NTS, because femtomole injections of SP into this brain region produce hypotension and bradycardia similar to that elicited by Ang II. The mechanisms of neurotransmission and receptor interactions accounting for the similar actions of Ang II and SP in the NTS are not understood. However, the findings described above suggest that Ang II might cause the release of SP from vagal afferent fibers. We have used two approaches to test this possibility. First, we compared the effects of Ang II and SP on the spontaneous activity of medial NTS neurons recorded in vitro from slices of the rat dorsal medulla. Second, we determined whether Ang II stimulated the release of SP from rat medulla slices. Methods In Vitro Recording StudiesSprague-Dawley rats (250-275 g; Harlan Sprague Dawley, Inc., Indianapolis, Ind.) were anesthetized with halothane and decapitated. The dorsal medulla

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Section: Discussionmentioning

confidence: 68%

Functional interactions between angiotensin II and substance P in the dorsal medulla.

1991

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“…We also confirmed that conversion of Ang I into Ang-(l-7) is not dependent on an intermediate production of Ang II. 5 In MK-422-treated animals, inhibition of Ang II production was associated with increased levels of Ang-(l-7).…”

Section: Discussionmentioning

confidence: 97%

In vivo metabolism of angiotensin I by neutral endopeptidase (EC 3.4.24.11) in spontaneously hypertensive rats.

et al. 1992

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We investigated the processing enzymes involved in the formation of circulating angiotensin-(l-7) after intravenous administration of angiotensin I to conscious spontaneously hypertensive and Wistar-Kyoto rats. Immunoreactive products, including angiotensin I, angiotensin II, and angiotensin-(l-7), were measured in arterial blood by three specific radioimmunoassays. Angiotensin I infusion (2 nmol) induced a rapid increase in immunoreactive angiotensin II and angiotensin-(l-7). Pretreatment with the angiotensin converting enzyme inhibitor enalaprilat (2 mg/kg) eliminated angiotensin II formation and augmented circulating levels of angiotensin I and angiotensin-(l-7) in spontaneously hypertensive and Wistar-Kyoto rats. The elevated levels of angiotensin-(l-7) in enalaprilat-treated rats were blocked by concurrent treatment with the neutral endopeptidase (EC 3.4.24.11) inhibitor SCH 39,370 (15 mg/kg) in both strains. Administration of SCH 39,370 alone decreased angiotensin-(l-7) levels in spontaneously hypertensive rats, whereas angiotensin II levels increased in both strains (p<0.01). Comparisons of the metabolism of angiotensin I in the two rat strains showed increased formation of angiotensin-(l-7) in spontaneously hypertensive rats not given any of the enzyme inhibitors. In addition, levels of angiotensin I were higher after administration of SCH 39,370 in hypertensive rats. These novel findings reveal that neutral endopeptidase EC 3.4.24.11 participates in the conversion of angiotensin I to angiotensin-(l-7) and in the metabolism of angiotensin II in the circulation of both spontaneously hypertensive and Wistar-Kyoto rats. Our results suggest that neutral endopeptidase EC 3.4.24.11 is a major enzymatic constituent of the circulating renin-angiotensin system. (Hypertension 1992;19:692-696) KEY WORDS • angiotensin I • angiotensin II • angiotensin converting enzyme • enalaprilat • enzyme inhibitors • peptide peptidohydrolases • spontaneously hypertensive rats A ngiotensin-(l-7) ] is the first member / \ of the angiotensin peptide family to cause cells -Z \ -to secrete hormones and release autacoids without eliciting accompanying changes in blood pressure, water intake, and aldosterone secretion. Incubation of hypothalamic explants with Ang-(l-7) stimulates a dose-dependent release of vasopressin.

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“…As documented above, in the past few years a large body of evidence has been accumulated suggesting a role for Ang- (1)(2)(3)(4)(5)(6)(7) in the control of hydroelectrolyte balance. However, due to several factors discussed below there is no consensus regarding the major action of Ang-(1-7) in the kidney.…”

Section: Introductionmentioning

confidence: 94%

“…Ang-(1-7) can be formed by an angiotensin converting enzyme (ACE)-independent pathway (4), and exerts important biological effects. In vitro this peptide is a potent vasopressin secretagogue (5) and possesses a potent prostaglandin-releasing activity in several cell lines (6,7).…”

Section: Introductionmentioning

confidence: 99%

Renal actions of angiotensin-(1-7)

Silva¹,

Baracho²,

Passaglio³

et al. 1997

Braz J Med Biol Res

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The heptapeptide angiotensin-(1-7) is considered to be a biologically active endproduct of the renin-angiotensin system. This angiotensin, which is devoid of the most known actions of angiotensin II such as induction of drinking behavior and vasoconstriction, has several selective effects in the brain and periphery. In the present article we briefly review recent evidence for a physiological role of angiotensin-(1-7) in the control of hydroelectrolyte balance.

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Converting enzyme activity and angiotensin metabolism in the dog brainstem.

Cited by 146 publications

References 14 publications

Functional interactions between angiotensin II and substance P in the dorsal medulla.

Functional interactions between angiotensin II and substance P in the dorsal medulla.

In vivo metabolism of angiotensin I by neutral endopeptidase (EC 3.4.24.11) in spontaneously hypertensive rats.

Renal actions of angiotensin-(1-7)

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