Drugs online research references
Endocrinology. 1989 Jul;125(1):486-91.
Production of renin, angiotensin II, and aldosterone by adrenal explant cultures: response to potassium and converting enzyme inhibition.
Shier DN, Kusano E, Stoner GD, Franco-Saenz R, Mulrow PJ.
Department of Medicine, Medical College of Ohio, Toledo 43699.
The existence of renin in a number of extrarenal tissues has been well documented, but the physiological role of extrarenal renin remains unknown. To study the physiological role of adrenal renin, we developed a serum-free culture system for adrenal capsular/zona glomrulosa explants. Explants showed good viability in culture (greater than 80%), and demonstrated net production of aldosterone, angiotensin II, and prorenin. Aldosterone production was consistently stimulated by an increase in potassium (6 mM) in the culture medium. Both aldosterone and angiotensin II production could be attenuated by adding the angiotensin converting enzyme inhibitor lisinopril to the culture medium (0.1 mM). These data suggest that rat adrenal explants are capable of producing all of the components of a functional renin-angiotensin-aldosterone system and that these components can interact in response to physiological stimuli. These findings support the hypothesis that a local adrenal renin system may play a physiological role in the control of adrenal aldosterone production.
online pharmacy ref source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=2544410&dopt=Abstract
Free Radic Res Commun. 1993;19(3):173-81.
Angiotensin converting enzyme inhibitors as oxygen free radical scavengers.
Mira ML, Silva MM, Queiroz MJ, Manso CF.
Instituto de Quimica Fisiologica, Faculdade de Medicina, Lisboa-Portugal.
The authors have compared the ability of two non-SH-containing angiotensin converting enzyme (ACE) inhibitors (enalaprilat and lisinopril) with an -SH containing ACE inhibitor (captopril) to scavenge the hydroxyl radical (.OH). All three compounds were able to scavenge .OH radicals generated in free solution at approximately diffusion-controlled rates (10(10) M-1 s-1) as established by the deoxyribose assay in the presence of EDTA. The compounds also inhibited deoxyribose degradation in reaction mixtures which did not contain EDTA but not so effectively. This later findings also suggests that they have some degree of metal-binding capability. Chemiluminescence assays of oxidation of hypoxanthine by xanthine oxidase in the presence of luminol, confirm that the three ACE inhibitors are oxygen free radical scavengers. Our results indicate that the presence of a sulphydryl group in the chemical structure of ACE inhibitors is not relevant for their oxygen free radical scavenging ability.
online pharmacy ref source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=8244086&dopt=Abstract
Rev Port Cardiol. 1992 May;11(5):425-30.
[Angiotensin-converting enzyme inhibitors as neutralizers of hydroxyl radical]
[Article in Portuguese]
Mira ML, Silva MM, Queiros MJ, Manso C.
Instituto de Quimica Fisiologica. Faculdade de Medicina de Lisboa.
Angiotensin converting enzyme inhibitors are utilized in the treatment of essential hypertension and of chronic cardiac failure. They are also employed in the treatment of the myocardial lesion of ischemia-reperfusion, which involves oxygen free radicals. In the present study we investigated the possibility of three angiotensin converting enzyme inhibitors (captopril, enalapril, lisinopril) to act as hydroxyl radical scavengers. The rate constants for reactions of those compounds with .OH were determined using the deoxyribose method. All there compounds proved to be good scavengers of .OH with rate constants of about 10(10)M-1s-1 and are iron chelators specially enalapril. The fact that captopril possesses a thiol group does not confer an higher antioxidative capacity. These results suggest that scavenging of oxygen free radicals may be a possible mechanism contributing to the therapeutic effect of angiotensin converting enzyme inhibitors.
online pharmacy ref source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=1325814&dopt=Abstract
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