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  • 1
    Electronic Resource
    Electronic Resource
    VARIATION IN ANGIOTENSIN-CONVERTING ENZYME (ACE) INHIBITOR AFFINITY AT TWO BINDING SITES ON RAT PULMONARY ACE: INFLUENCE ON BRADYKININ HYDROLYSIS (1992)
    Oxford, UK : Blackwell Publishing Ltd
    Clinical and experimental pharmacology and physiology 19 (1992), S. 0 
    Details
    ISSN: 1440-1681
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: 1. ACE from rat lung and testis was characterized by radioligand binding studies using [125I]-Ro 31-8472, the radioiodinated hydroxy derivative of the potent ACE inhibitor cilazaprilat.2. Analysis of the displacement of [125I]-Ro 31-8472 from ACE by ACE inhibitors of different structure by the ligand program was best fitted by a two binding site model for lung ACE and a one binding site model for testis ACE.3. There was marked variation in ACE inhibitor binding affinity at the two binding sites of lung ACE across the panel of ACE inhibitors studied (equilibrium dissociation constant; Kd; pmol/ L) for site one vs site two: cilazaprilat 40 ± 3 vs 430 ± 92*; lisinopril 25±1 vs 848 ± 107**; and quinaprilat 4 ± 1 vs 1869 ± 720; **P 〈 0.05; **P 〈 0.005, t-test, n= 3). Reduction in binding affinity at site two of lung ACE was related to an increase in ACE inhibitor side chain length or complexity of carboxyl terminal moiety. ACE inhibitor binding affinity at the testis ACE binding site resembled site one of lung ACE.4. Inhibition of bradykinin hydrolysis by lung ACE in the presence of increasing concentrations of cilazaprilat or quinaprilat was similar (F= 0.64; P〉0.05), suggesting that bradykinin cleavage predominates at ACE active site one.5. The differences in ACE inhibitor affinity at the two ACE active sites has implications in physiological substrate selectivity, and may influence the pharmacodynamic effects of different ACE inhibitors.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1440-1681.1992.tb00470.x
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  • 2
    Electronic Resource
    Electronic Resource
    ACUTE AND CHRONIC EFFECTS OF ANGIOTENSIN-CONVERTING ENZYME INHIBITORS ON TISSUE ANGIOTENSIN-CONVERTING ENZYME (1992)
    Oxford, UK : Blackwell Publishing Ltd
    Clinical and experimental pharmacology and physiology 19 (1992), S. 0 
    Details
    ISSN: 1440-1681
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: 1. The effects of angiotensin-converting enzyme (ACE) inhibitors on the tissue ACE were assessed by quantitative in vitro autoradiography after acute and chronic administrations of the drugs.2. Following acute administration of lisinopril, perindopril or benazepril, ACE was markedly inhibited in the lung, kidney and blood vessels but not in the testis. In the brain, ACE was inhibited mainly in structures with a deficient blood brain barrier.3. High doses of perindopril progressively inhibited ACE in other brain structures. Tissue ACE inhibition persisted after serum levels of the enzyme had returned to control levels. In the case of perindopril, the time course of tissue ACE inhibition correlated with the inhibition of the pressor responses to exogenous angiotensin I.4. After chronic administration of lisinopril or perindopril for 14 days, a similar pattern of ACE inhibition was observed in the kidney, lung and blood vessels. In the lung, however, lisinopril was found to increase total ACE by 30%, while plasma ACE was increased two-threefold by both lisinopril and perindopril. Testicular ACE remained unaltered by chronic lisinopril treatment.5. Overall, the changes in tissue ACE after the administration of inhibitors more closely parallel the drugs' biological effects than changes in plasma ACE or drug levels. ACE in the testis and brain is protected by permeability barriers that limit access of the drugs.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1440-1681.1992.tb02803.x
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  • 3
    Electronic Resource
    Electronic Resource
    GENOTYPIC INFLUENCE ON PLASMA DIPEPTIDYL CARBOXYPEPTIDASE-1 ACTIVITY IN HYPERTENSIVES (1994)
    Oxford, UK : Blackwell Publishing Ltd
    Clinical and experimental pharmacology and physiology 21 (1994), S. 0 
    Details
    ISSN: 1440-1681
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: 1. Plasma dipeptidyl carboxypeptidase-1 (DCP1; angiotensin I-converting enzyme, kininase II; EC 3.4.15.1) tracks with the deletion allele in genotypes of a 287 bp insertion/deletion (I/D) polymorphism of its gene, DCP1, in healthy Caucasian populations. The aim of the present study was to see whether genotype has a similar influence on plasma DCP1 in hypertensives.2. The study involved 35 Caucasian patients with severe, familial essential hypertension, who were not being treated with DCP1 inhibitors, and 94 normotensives. Genotyping for the I/D polymorphism was performed by polymerase chain reaction and plasma DCP1 activity was measured by rate of hydrolysis of both [3H]-Hip-Gly-Gly and Hip-His-Leu.3. Plasma DCP1 activity (nmol Gly-Gly/min per mL; mean ± s.e.m.) was 67 ± 2, 82 ± 4 and 91 ± 6 in II, ID and DD hypertensives, respectively, which was similar to values of 68 ± 4, 82 ± 3 and 94 ± 3 in normotensives (P= 0.0001 by one-way analysis of variance). Results for the His-Leu assay indicated similar tracking with genotype.4. The Michaelis constant (μmol Hip-Gly-Gly/mL; mean ± s.e.m., n= 10) for DD subjects was the same as for II subjects (10.6 ± 1.6 vs 11.1 ± 2.3; P = 0.86).5. In conclusion, in severely hypertensive Caucasian subjects, plasma DCP1 activity is subject to a similar genotypic influence in hypertensives as has been reported previously in normotensives. Furthermore, the plasma DCP1 enzyme itself appears to be functionally similar for each genotype.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1440-1681.1994.tb02525.x
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  • 4
    Electronic Resource
    Electronic Resource
    ANGIOTENSIN-CONVERTING ENZYME IN MACRO-AND MICROVESSELS OF THE RAT (1991)
    Oxford, UK : Blackwell Publishing Ltd
    Clinical and experimental pharmacology and physiology 18 (1991), S. 0 
    Details
    ISSN: 1440-1681
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: 1. Angiotensin-converting enzyme (ACE) was measured in the aorta, cerebral and mesenteric microvessels of Wistar-Kyoto rats using a specific radioligand assay.2. Ligand binding studies revealed a four-fold increase in concentration of ACE in mesenteric microvessels, compared with aorta or brain microvessels. The dissociation constant (Kd) was similar in all tissues.3. The effects of oral administration of the ACE inhibitor S9650 on vascular ACE in vivo were measured.4. S9650 produced a dose-dependent inhibition of vascular ACE from brain and mesenteric microvessels.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1440-1681.1991.tb01462.x
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  • 5
    Electronic Resource
    Electronic Resource
    MESENTERIC RESISTANCE AND BRAIN MICROVASCULAR ANGIOTENSIN-CONVERTING ENZYME IN THE SPONTANEOUSLY HYPERTENSIVE RAT (1992)
    Oxford, UK : Blackwell Publishing Ltd
    Clinical and experimental pharmacology and physiology 19 (1992), S. 0 
    Details
    ISSN: 1440-1681
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: 1. Angiotensin-converting enzyme (ACE) concentration was measured in mesenteric and brain microvessels from spontaneously hypertensive rats (SHR) and compared with normotensive controls using a specific radioligand binding assay.2. Plasma angiotensin-converting enzyme activity was similar in SHR (n= 15) and normotensive controls (n= 21; 58 ± 1 nmol HL/mL per min, vs 64 ± 6 nmol HL/mL per min).3. There was no significant difference between the mesenteric vascular angiotensin-converting enzyme radioligand binding site density (Bmax, fmol/ mg protein) of SHR and normotensive controls (954 ±77 vs 890 ±56, P= 0.5, unpaired Student's t-test), despite significant differences in systolic blood pressure (220 ± 8 mmHg vs 120 ± 6 mmHg respectively, P 〈 0.01) and increased mesenteric wet weight to body weight ratio in the hypertensive rats (0.28 ± 0.02 mg/g, n= 5 vs 0.16 ± 0.02 mg/g, n= 7, P 〈 0.01).4. Brain vascular angiotensin-converting enzyme radioligand binding site density (Bmax, fmol/ mg protein) was also similar in SHR and normotensive controls (467 ±62, n= 5 vs 497 ± 64, n= 5, P= 0.7, unpaired Student's t-test).5. These results demonstrate that vascular angiotensin-converting enzyme concentration is not altered in the SHR and that vascular ACE is not increased in this form of vascular hypertrophy or regulated by the blood pressure level.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1440-1681.1992.tb00469.x
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