| Literature DB >> 3154625 |
T Inagami1, K Mizuno, M Nakamaru, K N Pandey, M Naruse, K Naruse, K Misono, T Okamura, M Kawamura, K Higashimori.
Abstract
The enzyme renin has been purified and characterized by structural analysis. Pure renin protein was used to produce a specific antibody to renin, which was useful in demonstrating the presence of a specific renin in many tissues other than kidney. Further, in these cells angiotensins I and II and converting enzyme all were found to coexist with renin by immunohistochemical studies, indicating the local production of renin, angiotensinogen and angiotensins in these cells. Angiotensin II produced in the cultured cells was secreted to the outside of the cells. Secretion of angiotensin II from the angiotensin-producing cells was demonstrated with perfused mesenteric artery. The secretion of angiotensin II from the vascular beds was inhibited by converting enzyme inhibitors, and was stimulated by the adrenergic beta-agonist isoproterenol. These studies demonstrate local production and controlled secretion of angiotensin II and define its physiologic role.Entities:
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Year: 1988 PMID: 3154625 DOI: 10.1007/bf00051182
Source DB: PubMed Journal: Cardiovasc Drugs Ther ISSN: 0920-3206 Impact factor: 3.727