Angiotensin converting enzyme variability in hypertensive and normotensive rats.

Michel, Bruno; Welsch, C; Coquard, Catherine; Grima, Michèle; Barthelmebs, Mariette; Jl, Imbs

doi:10.1161/01.hyp.21.4.442

Cited by 11 publications

(2 citation statements)

References 23 publications

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“…Based on these results, we carried out the present work to evaluate the relevance of vascular ACE for the development of hypertension in these rats. A recent report shows that the ACE activity differs considerably between various colonies of SHR and WKY rats but not within a strain from a single stock, 20 so the animals used for this study were obtained from the same colony investigated in the previous linkage studies. 8 "…”

Section: Discussionmentioning

confidence: 99%

Differential regulation of vascular angiotensin I-converting enzyme in hypertension.

et al. 1994

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The angiotensin I-converting enzyme (ACE) gene is found on the locus that has been linked to high blood pressure after sodium loading in rats, so in the present study we investigated the role of vascular ACE for the pathophysi-ology of hypertension in the corresponding parental strains, Wistar-Kyoto (WKY) rats and stroke-prone spontaneously hypertensive rats (SHRSP), in basal conditions at different ages and after sodium loading. Blood pressure was already significantly enhanced in SHRSP from 4 weeks of age, and sodium loading induced an additional increase only in the hypertensive strain. In the aorta, basal ACE gene expression, analyzed by quantitative polymerase chain reaction, and ACE activity were similar in both strains, whereas mRNA levels were elevated in SHRSP after salt compared with WKY rats and correlated with an increase in enzymatic activity. In Jk ngiotensin I-converting enzyme (ACE) is a zinc / \ metallopeptidase that is expressed throughout A. A. the body as a membrane-bound enzyme in particular high concentrations in vascular endothelial cells and intestinal and renal brush borders. In addition, a soluble form of ACE, most likely released from the endothelium through the action of a processing enzyme , 1-2 is found in plasma. 3 ACE catalyzes the conversion of the inactive deca-peptide angiotensin I (Ang I) to the active octapeptide Ang II, which plays a major role in regulating blood pressure as well as in fluid and electrolyte homeostasis. At the vascular level, Ang II induces potent vasocon-striction, either through a direct action on the Ang II receptors of the smooth muscle 4 or indirectly by prejunctional 5 modulation of norepinephrine release. Moreover, Ang II has also been suggested to induce vascular hypertrophy. 6 In addition to its role in Ang II formation, the vasodilator peptide bradykinin is inac-tivated by ACE through a sequential cleavage of two carboxy-terminal dipeptides. 7 Therefore, the functional role of ACE is the release of a potent vasopres-sor and trophic factor as well as the degradation of a vasodilator. An increase in the activity of the renin-angiotensin system has been implicated in the pathogenesis of arterial hypertension for a long time, although the mesenteric arteries, ACE mRNA levels were significantly enhanced in SHRSP at all ages, although ACE activity was not different between the strains. These results were not modified after sodium loading. These data demonstrate that the level of ACE activity in plasma and vascular tissue can be controlled in a different manner within a rat strain and that in contrast to the soluble form, the membrane-bound ACE may be the one responsible for determining the vasoactive effects of angioten-sin II. In addition, ACE undergoes a different regulation in vascular tissues of SHRSP compared with WKY rats, which might be involved in the regulation of blood pressure in these animals. (Hypertension. 1994-^4:280-286.) Key Words • angiotensin I-converting enzyme • blood vessels • hypertension, genetic • rats, inbred SHR, stroke-prone ...

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Section: Discussionmentioning

confidence: 99%

Differential regulation of vascular angiotensin I-converting enzyme in hypertension.

et al. 1994

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“…In the control low-flow experiments (n ϭ 6, Sprague-Dawley rats, 8 -9 mo old), hearts were perfused in the CF mode throughout the experiment. The use of the Sprague-Dawley strain as the control for SHR myocardial studies (in some cases, preferred over the WKY strain) has been previously reported (14,47). Before the perfusion experiment, heart weight was estimated from rat body weight.…”

Section: Methodsmentioning

confidence: 99%

Myocardial Po₂does not limit aerobic metabolism in the postischemic heart

Chung

2016

American Journal of Physiology-Heart and Circulatory Physiology

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Reperfused hypertrophic hearts are prone to develop reflow abnormalities, which are likely to impair O2 return to the myocardium. Yet, reflow deficit may not be the only factor determining postischemic oxygenation in the hypertrophic heart. Altered O2 demand may also contribute to hypoxia. In addition, the extent to which myocardial Po2 dictates energy and functional recovery in the reperfused heart remains uncertain. In the present study, moderately hypertrophied hearts from spontaneously hypertensive rats were subjected to ischemia-reperfusion, and the recovery time courses of pH and high-energy phosphates were followed by (31)P NMR. (1)H NMR measurement of intracellular myoglobin assessed tissue O2 levels. The present study found that the exacerbation of hypoxia in the postischemic spontaneously hypertensive rat heart arises mostly from impaired microvascular supply of O2. However, postischemic myocardial Po2, at least when it exceeds ∼18% of the preischemic level, does not limit mitochondrial respiration and high-energy phosphate resynthesis. It only passively reflects changes in the O2 supply-demand balance.

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Preventive and treatment effects of a hemp seed (Cannabis sativa L.) meal protein hydrolysate against high blood pressure in spontaneously hypertensive rats

Girgih

Alashi

et al. 2013

Eur J Nutr

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Angiotensin converting enzyme variability in hypertensive and normotensive rats.

Cited by 11 publications

References 23 publications

Differential regulation of vascular angiotensin I-converting enzyme in hypertension.

Differential regulation of vascular angiotensin I-converting enzyme in hypertension.

Myocardial Po₂does not limit aerobic metabolism in the postischemic heart

Preventive and treatment effects of a hemp seed (Cannabis sativa L.) meal protein hydrolysate against high blood pressure in spontaneously hypertensive rats

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Angiotensin converting enzyme variability in hypertensive and normotensive rats.

Cited by 11 publications

References 23 publications

Differential regulation of vascular angiotensin I-converting enzyme in hypertension.

Differential regulation of vascular angiotensin I-converting enzyme in hypertension.

Myocardial Po2does not limit aerobic metabolism in the postischemic heart

Preventive and treatment effects of a hemp seed (Cannabis sativa L.) meal protein hydrolysate against high blood pressure in spontaneously hypertensive rats

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Product

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Myocardial Po₂does not limit aerobic metabolism in the postischemic heart