| pubmed-article:2162536 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2162536 | lifeskim:mentions | umls-concept:C0027819 | lld:lifeskim |
| pubmed-article:2162536 | lifeskim:mentions | umls-concept:C0017638 | lld:lifeskim |
| pubmed-article:2162536 | lifeskim:mentions | umls-concept:C0003018 | lld:lifeskim |
| pubmed-article:2162536 | lifeskim:mentions | umls-concept:C0682527 | lld:lifeskim |
| pubmed-article:2162536 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:2162536 | lifeskim:mentions | umls-concept:C1709694 | lld:lifeskim |
| pubmed-article:2162536 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:2162536 | pubmed:dateCreated | 1990-7-26 | lld:pubmed |
| pubmed-article:2162536 | pubmed:abstractText | The metabolism of angiotensin (Ang) peptides was studied in NG108-15 neuroblastoma x glioma hybrid cells which express Ang II receptors, renin, dipeptidyl carboxypeptidase A (converting enzyme), as well as Ang I and Ang II. In these experiments, 0.2 nM of either 125I-Ang I or 125I-Ang II was incubated with intact cell monolayers and the medium was analyzed for 125I-products by high performance liquid chromatography. The major product generated from the metabolism of labeled Ang I or Ang II was identified as the amino-terminal heptapeptide Ang-(1-7). N-benzyloxycarbonyl-prolyl-prolinal (ZPP), a specific inhibitor of prolyl endopeptidase, inhibited the formation of Ang-(1-7) from Ang I by 35%. Complete inhibition of Ang-(1-7) generation was attained with p-chloromercuriphenyl-sulfonate, which suggests that a sulfhydryl-containing peptidase other than prolyl endopeptidase is also involved in Ang-(1-7) formation. Ang II was observed to be a minor product resulting from Ang I metabolism. Although the converting enzyme inhibitor enalaprilat (MK-422) significantly reduced Ang II formation, it had no effect on the levels of Ang-(1-7). These findings demonstrate a preferential processing of Ang I into Ang-(1-7) which is not dependent on the prior formation of Ang II. | lld:pubmed |
| pubmed-article:2162536 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2162536 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2162536 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2162536 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2162536 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2162536 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2162536 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2162536 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2162536 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2162536 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2162536 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2162536 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2162536 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2162536 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2162536 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2162536 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2162536 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2162536 | pubmed:issn | 0196-9781 | lld:pubmed |
| pubmed-article:2162536 | pubmed:author | pubmed-author:FerrarioC MCM | lld:pubmed |
| pubmed-article:2162536 | pubmed:author | pubmed-author:TallantE AEA | lld:pubmed |
| pubmed-article:2162536 | pubmed:author | pubmed-author:BrosnihanK... | lld:pubmed |
| pubmed-article:2162536 | pubmed:author | pubmed-author:ChappellM CMC | lld:pubmed |
| pubmed-article:2162536 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2162536 | pubmed:volume | 11 | lld:pubmed |
| pubmed-article:2162536 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2162536 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2162536 | pubmed:pagination | 375-80 | lld:pubmed |
| pubmed-article:2162536 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:2162536 | pubmed:meshHeading | pubmed-meshheading:2162536-... | lld:pubmed |
| pubmed-article:2162536 | pubmed:meshHeading | pubmed-meshheading:2162536-... | lld:pubmed |
| pubmed-article:2162536 | pubmed:meshHeading | pubmed-meshheading:2162536-... | lld:pubmed |
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| pubmed-article:2162536 | pubmed:meshHeading | pubmed-meshheading:2162536-... | lld:pubmed |
| pubmed-article:2162536 | pubmed:meshHeading | pubmed-meshheading:2162536-... | lld:pubmed |
| pubmed-article:2162536 | pubmed:meshHeading | pubmed-meshheading:2162536-... | lld:pubmed |
| pubmed-article:2162536 | pubmed:meshHeading | pubmed-meshheading:2162536-... | lld:pubmed |
| pubmed-article:2162536 | pubmed:meshHeading | pubmed-meshheading:2162536-... | lld:pubmed |
| pubmed-article:2162536 | pubmed:meshHeading | pubmed-meshheading:2162536-... | lld:pubmed |
| pubmed-article:2162536 | pubmed:meshHeading | pubmed-meshheading:2162536-... | lld:pubmed |
| pubmed-article:2162536 | pubmed:meshHeading | pubmed-meshheading:2162536-... | lld:pubmed |
| pubmed-article:2162536 | pubmed:meshHeading | pubmed-meshheading:2162536-... | lld:pubmed |
| pubmed-article:2162536 | pubmed:articleTitle | Processing of angiotensin peptides by NG108-15 neuroblastoma x glioma hybrid cell line. | lld:pubmed |
| pubmed-article:2162536 | pubmed:affiliation | Department of Brain, Cleveland Clinic Foundation, OH 44195-5070. | lld:pubmed |
| pubmed-article:2162536 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2162536 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2162536 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
