Linked Life Data

3021940

Source:http://linkedlifedata.com/resource/pubmed/id/3021940

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1986-12-16
pubmed:abstractText
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. In these cells angiotensins I and II and angiotensin converting enzyme were found to coexist with renin by immunohistochemical studies and by the direct determination with cultured cells. Studies with these cells indicated 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 while more than 95% renin remained within the cells. Secretion of angiotensin II from the angiotensin producing cells was demonstrated with perfused mesenteric artery. The secretion was stimulated by the adrenergic beta-agonist isoproterenol in a dose-dependent manner and specifically inhibited by a beta 2-antagonist. Angiotensin II secreted from the vascular bed by the beta 2-adrenoceptor stimulation acts locally to facilitate norepinephrine release. These studies demonstrate local production and secretion of angiotensin II and define its physiological role.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0952-1178
pubmed:author
pubmed:issnType
Print
pubmed:volume
4
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
S11-6
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
Intracellular action of renin, angiotensin production and release.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Review