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- Publisher Website: 10.1016/0895-7061(95)00026-L
- Scopus: eid_2-s2.0-0029033469
- PMID: 7544135
- WOS: WOS:A1995RB67900001
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Article: Inhibition of the angiotensin converting enzyme by perindoprilat and release or nitric oxide
Title | Inhibition of the angiotensin converting enzyme by perindoprilat and release or nitric oxide |
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Authors | |
Keywords | B1 receptors B2 receptors carboxypeptidase HOE-140 Nitric oxide |
Issue Date | 1995 |
Publisher | Elsevier Inc. The Journal's web site is located at http://www.elsevier.com/locate/amjhyper |
Citation | American Journal Of Hypertension, 1995, v. 8 n. 5 II SUPPL., p. 1S-6S How to Cite? |
Abstract | Experiments were designed to investigate the mechanism underlying the endothelium-dependent relaxations to perindoprilat, a converting enzyme inhibitor, in canine coronary arteries previously exposed to bradykinin. Rings suspended in organ chambers were exposed to bradykinin for 3 min and washed extensively for 150 min. In rings previously exposed to the peptide, bradykinin induced relaxations which were augmented in the presence of perindoprilat; this response was not affected by indomethacin, but nitro-L-arginine induced a rightward shift of the relaxation to the peptide without affecting its maximal effect. In canine coronary arteries previously exposed to the peptide, perindoprilat caused endothelium-dependent relaxations (IC50 = 7.83), which had been observed previously at concentrations where the converting enzyme inhibitor did not augment the response to bradykinin. Carboxypeptidase B2 but not aprotinin, impaired the relaxation to perindoprilat, suggesting a contribution of bradykinin. The relaxation to perindoprilat was not affected by the B2 antagonist Leu8-des-Arg9-bradykinin. However, the bradykinin B2 antagonist HOE-140 displayed a noncompetitive antagonism against the response to perindoprilat. The response to the converting enzyme inhibitor was not affected by indomethacin but was impaired significantly by nitro-L-arginine. The present findings suggest that in canine coronary arteries previously exposed to bradykinin, the relaxation to perindoprilat is mediated mainly by endothelium-derived nitric oxide. In addition, the response to perindoprilat may be due to factors other than just protection of bound bradykinin from degradation. |
Persistent Identifier | http://hdl.handle.net/10722/171165 |
ISSN | 2023 Impact Factor: 3.2 2023 SCImago Journal Rankings: 0.925 |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Desta, B | en_US |
dc.contributor.author | Vanhoutte, PM | en_US |
dc.contributor.author | Boulanger, CM | en_US |
dc.date.accessioned | 2012-10-30T06:12:29Z | - |
dc.date.available | 2012-10-30T06:12:29Z | - |
dc.date.issued | 1995 | en_US |
dc.identifier.citation | American Journal Of Hypertension, 1995, v. 8 n. 5 II SUPPL., p. 1S-6S | en_US |
dc.identifier.issn | 0895-7061 | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/171165 | - |
dc.description.abstract | Experiments were designed to investigate the mechanism underlying the endothelium-dependent relaxations to perindoprilat, a converting enzyme inhibitor, in canine coronary arteries previously exposed to bradykinin. Rings suspended in organ chambers were exposed to bradykinin for 3 min and washed extensively for 150 min. In rings previously exposed to the peptide, bradykinin induced relaxations which were augmented in the presence of perindoprilat; this response was not affected by indomethacin, but nitro-L-arginine induced a rightward shift of the relaxation to the peptide without affecting its maximal effect. In canine coronary arteries previously exposed to the peptide, perindoprilat caused endothelium-dependent relaxations (IC50 = 7.83), which had been observed previously at concentrations where the converting enzyme inhibitor did not augment the response to bradykinin. Carboxypeptidase B2 but not aprotinin, impaired the relaxation to perindoprilat, suggesting a contribution of bradykinin. The relaxation to perindoprilat was not affected by the B2 antagonist Leu8-des-Arg9-bradykinin. However, the bradykinin B2 antagonist HOE-140 displayed a noncompetitive antagonism against the response to perindoprilat. The response to the converting enzyme inhibitor was not affected by indomethacin but was impaired significantly by nitro-L-arginine. The present findings suggest that in canine coronary arteries previously exposed to bradykinin, the relaxation to perindoprilat is mediated mainly by endothelium-derived nitric oxide. In addition, the response to perindoprilat may be due to factors other than just protection of bound bradykinin from degradation. | en_US |
dc.language | eng | en_US |
dc.publisher | Elsevier Inc. The Journal's web site is located at http://www.elsevier.com/locate/amjhyper | en_US |
dc.relation.ispartof | American Journal of Hypertension | en_US |
dc.subject | B1 receptors | - |
dc.subject | B2 receptors | - |
dc.subject | carboxypeptidase | - |
dc.subject | HOE-140 | - |
dc.subject | Nitric oxide | - |
dc.subject.mesh | Angiotensin-Converting Enzyme Inhibitors - Pharmacology | en_US |
dc.subject.mesh | Animals | en_US |
dc.subject.mesh | Aprotinin - Pharmacology | en_US |
dc.subject.mesh | Bradykinin - Antagonists & Inhibitors - Pharmacology | en_US |
dc.subject.mesh | Carboxypeptidase B | en_US |
dc.subject.mesh | Carboxypeptidases - Pharmacology | en_US |
dc.subject.mesh | Coronary Vessels - Drug Effects - Metabolism | en_US |
dc.subject.mesh | Dogs | en_US |
dc.subject.mesh | Endothelium, Vascular - Drug Effects - Metabolism | en_US |
dc.subject.mesh | Female | en_US |
dc.subject.mesh | Indoles - Pharmacology | en_US |
dc.subject.mesh | Male | en_US |
dc.subject.mesh | Nitric Oxide - Metabolism | en_US |
dc.subject.mesh | Vasodilation - Drug Effects - Physiology | en_US |
dc.title | Inhibition of the angiotensin converting enzyme by perindoprilat and release or nitric oxide | en_US |
dc.type | Article | en_US |
dc.identifier.email | Vanhoutte, PM:vanhoutt@hku.hk | en_US |
dc.identifier.authority | Vanhoutte, PM=rp00238 | en_US |
dc.description.nature | link_to_subscribed_fulltext | en_US |
dc.identifier.doi | 10.1016/0895-7061(95)00026-L | - |
dc.identifier.pmid | 7544135 | - |
dc.identifier.scopus | eid_2-s2.0-0029033469 | en_US |
dc.identifier.volume | 8 | en_US |
dc.identifier.issue | 5 II SUPPL. | en_US |
dc.identifier.spage | 1S | en_US |
dc.identifier.epage | 6S | en_US |
dc.identifier.isi | WOS:A1995RB67900001 | - |
dc.publisher.place | United States | en_US |
dc.identifier.scopusauthorid | Desta, B=6603788474 | en_US |
dc.identifier.scopusauthorid | Vanhoutte, PM=7202304247 | en_US |
dc.identifier.scopusauthorid | Boulanger, CM=7006599024 | en_US |
dc.identifier.issnl | 0895-7061 | - |