Studies on the angiotensin converting enzyme with different substrates

Piquilloud, Yvonne; Reinharz, A.; Roth, Marc

doi:10.1016/0005-2744(70)90090-2

Cited by 217 publications

(108 citation statements)

References 12 publications

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“…The method used was based on spectrofluorimetric determination of histidyl-L-leucine (HL) using Z-phenyl-histidyl-leucine (Bachem Bioscience Inc, USA) as an ACE substrate. [16][17][18] All determinations were made simultaneously in duplicate. Intraassay and interassay variation coefficients were both 1%.…”

Section: Measurement Of Plasma Ace Activitymentioning

confidence: 99%

Neutral endopeptidase and angiotensin I converting enzyme insertion/deletion gene polymorphism in humans

Oliveri

et al. 2004

J Hum Hypertens

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Neutral endopeptidase (NEP) hydrolyses angiotensins (Ang) I and II and generates angiotensin-(1-7) ]. In humans, the insertion/deletion (I/D) angiotensin-I converting enzyme (ACE) gene polymorphism determined plasma ACE levels by 40%. In rats, a similar polymorphism determines ACE levels which are inversely associated to NEP activity. The objective of this study is to evaluate the relationship between ACE expression and plasma NEP activity in normotensive subjects and in hypertensive patients. In total, 58 consecutive patients with hypertension, evaluated in our Hypertension Clinic, were compared according to their ACE I/D genotypes with 54 control subjects in terms of both plasma ACE activity and NEP activities. Plasma ACE activity was elevated 51 and 70% in both DD ACE groups (normotensives and hypertensives) compared with their respective ID and II ACE groups (Po0.001). A significant effect of the ACE polymorphism and of the hypertensive status on ACE activity was observed (Po0.001). In normotensive DD ACE subjects, NEP activity was 0.30 7 0.02 U/ml, whereas in the normotensive II ACE and in the normotensive ID ACE subjects NEP activity was increased 65 and 48%, respectively (Po0.001). In the hypertensive DD ACE patients, NEP activity was 0.47 7 0.03 U/mg. An effect of the I/D ACE genotypes on NEP activity (Po0.04) and an interaction effect between the I/D ACE genotype and the hypertensive status were also observed (Po0.001). These results are consistent with a normal and inverse relationship between the ACE polymorphism and NEP activity in normotensive humans (as is also observed in rats). This normal relationship is not observed in hypertensive patients.

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Section: Measurement Of Plasma Ace Activitymentioning

confidence: 99%

Neutral endopeptidase and angiotensin I converting enzyme insertion/deletion gene polymorphism in humans

Oliveri

et al. 2004

J Hum Hypertens

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“…Plasma renin activity was likewise determined but without the addition of angiotensinogen. Angiotensin converting enzyme was assayed by the fluorimetric method of Piquilloud et al 6 with Z-Phe-His-Leu as substrate. Ang I-degrading enzyme activities were quantified as described recently.…”

Section: Methodsmentioning

confidence: 99%

Reninlike enzymes in human vasculature.

Thurnreiter

Plaschke

et al. 1990

Hypertension

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“…Most tissues were homogenized in 9 volumes of buffer (1:10 Cushman & Cheung (1971), and a modification (Cheung et al, 1980) of the fluorometric method for quantitating the product His-Leu (Piquilloud et al, 1969). The final concentrations of components in the 0.25-ml assay incubation mixture were: potassium phosphate buffer, pH 7.8, 100 mM, NaCl, 300 mm, tissue homogenate at the final dilution shown in Table 1, and substrate Leenen & de Jong (1971 for 25 min by reducing the normal rate of perfusion (25 ± 1.7 ml min-') to zero, and the hearts were reperfused for 30 min with solution containing either drug or vehicle.…”

Section: Preparation Of Uncentrifuged Homogenates Of Tissuesmentioning

confidence: 99%

Comparisons in vitro, ex vivo, and in vivo of the actions of seven structurally diverse inhibitors of angiotensin converting enzyme (ACE).

Dw¹,

Wang²,

Fung³

et al. 1989

Brit J Clinical Pharma

108

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1. Seven drugs (captopril, zofenopril, enalapril, ramipril, lisinopril, fosinopril, and SQ 29,852) were compared in vitro in homogenates of aorta, brain, heart, lung, and kidney and in sera of spontaneously hypertensive rats (SHR) both with respect to potencies of their active moieties as inhibitors of angiotensin‐converting enzyme (ACE), and, where applicable, rates of hydrolysis of their prodrug ester functions. 2. In ex vivo dose‐response and time‐course studies, the inhibitory effects of the seven drugs on tissue ACEs and their relative distributions to SHR tissues were compared following oral administration. 3. The relative potencies of the inhibitory moieties of the drugs (in parentheses) and the normalized ‘equiactive’ oral doses employed for time‐course studies were: SQ 29,852 (1.0), 100 mg kg‐1; captopril (3.5), 30 mg kg‐1; enalapril (12), 20 mg kg‐1; fosinopril (13), 25 mg kg‐1; zofenopril (20), 10 mg kg‐1; lisinopril (24), 10 mg kg‐1; and ramipril (51), 5 mg kg‐1. 4. Following oral administration of the drugs to SHR, the degree and duration of ACE inhibition in aorta and lung correlated with the antihypertensive actions, with ramipril, lisinopril, and zofenopril producing effects of the greatest magnitude and duration. 5. Ramipril and enalapril did not inhibit brain ACE ex vivo; captopril and zofenopril had modest but short‐lasting effects; and fosinopril, lisinopril, and SQ 29,852 had long‐lasting inhibitory actions, which, with the latter two, were delayed in onset. 6. All of the drugs produced significant inhibition of kidney ACE, with ramipril and fosinopril having somewhat weaker effects, perhaps due to biliary routes of excretion. 7. Captopril, fosinopril, and particularly zofenopril inhibited cardiac ACE ex vivo with degrees and durations that were marked compared with those of the other drugs; preliminary studies with isolated hearts suggest a possible relationship between inhibition of cardiac ACE and preservation of cardiac function subsequent to ischaemia.

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Studies on the angiotensin converting enzyme with different substrates

Cited by 217 publications

References 12 publications

Neutral endopeptidase and angiotensin I converting enzyme insertion/deletion gene polymorphism in humans

Neutral endopeptidase and angiotensin I converting enzyme insertion/deletion gene polymorphism in humans

Reninlike enzymes in human vasculature.

Comparisons in vitro, ex vivo, and in vivo of the actions of seven structurally diverse inhibitors of angiotensin converting enzyme (ACE).

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