Inhibition Of Renin Activity Research Articles

Dog Kidney Phospholipids and the Question of Renin Inhibition

We have investigated renin inhibitory activity in relation to the chemical composition of several phospholipids, especially those isolated from an organic fraction of dog kidneys reported to contain a phosphatidyl amino acid renin 'preinhibitor'. In our hands, this fraction, eluted from a silicic acid column with chloroform–methanol (4:1), contained large amounts of phosphatidylthanolamine (PE) as established by infrared spectroscopy, silica gel, paper, and gas–liquid chromatography, elemental analysis, and specific stains. No other ninhydrin-positive phospholipid migrating as 'preinhibitor' on thin-layer chromatographs was detected, with the possible exception of a very minor, unidentified, ethanolamine-positive component. Also eluted with the PE was lyso PE, in a quantity (0.16 mg/g kidney) within the range originally reported for 'preinhibitor'. But coidentity of 'preinhibitor' and lyso PE is unlikely since the latter is deacylated, contains ethanolamine and a much higher percentage (66 mol %) of arachidonate in its esterified fatty acids, and does not inhibit renin in vitro. Dog and rat kidney PE, and, most potently, ox brain phosphatidylserine, all inhibited renin in vitro, but not in vivo. These data argue against the existence and proposed structure of the renal renin 'preinhibitor', and also against the concept of a unique inhibitory role of a specific base moiety and fatty acid composition. Lack of in vivo renin inhibition using the infusion technique by which such inhibition was originally demonstrated questions the relevance of the tested phospholipids as physiological regulators of the rennin–angiotensin system.

A procedure for the determination of a renin inhibitor in human plasma

An improved method for the determination of a phospholipid, which inhibits renin and is present in human plasma, is described. The phospholipid is extracted from plasma, added to a reconstituted renin-angiotensinogen system free from endogenous phospholipase(s) and then activated by the addition of an excess of exogenous phospholipase A. Angiotensin I produced in an assay medium containing renin-angiotensinogen and phospholipase A is compared with angiotensin I developed in an assay medium containing renin-angiotensinogen-phospholipid and phospholipase A. The inhibition of renin activity is expressed as percentage reduction in the production rate of angiotensin I, evaluated by radioimmunoassay of angiotensin I.

Isolation and renin-inhibitory activity of phosphoglyceride from shark kidney.

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTIsolation and Renin-Inhibitory Activity of Phosphoglyceride from Shark KidneyJoseph Turcotte and Robert BoydCite this: J. Med. Chem. 1973, 16, 2, 166–168Publication Date (Print):February 1, 1973Publication History Published online8 September 2004Published inissue 1 February 1973https://doi.org/10.1021/jm00260a600RIGHTS & PERMISSIONSArticle Views31Altmetric-Citations9LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InReddit PDF (436 KB) Get e-Alerts Get e-Alerts