| pubmed-article:1612017 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1612017 | lifeskim:mentions | umls-concept:C0007603 | lld:lifeskim |
| pubmed-article:1612017 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
| pubmed-article:1612017 | lifeskim:mentions | umls-concept:C1882726 | lld:lifeskim |
| pubmed-article:1612017 | lifeskim:mentions | umls-concept:C0521447 | lld:lifeskim |
| pubmed-article:1612017 | lifeskim:mentions | umls-concept:C0230664 | lld:lifeskim |
| pubmed-article:1612017 | lifeskim:mentions | umls-concept:C1707455 | lld:lifeskim |
| pubmed-article:1612017 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:1612017 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:1612017 | pubmed:dateCreated | 1992-7-27 | lld:pubmed |
| pubmed-article:1612017 | pubmed:abstractText | Although the action of angiotensin-II (Ang-II) is believed to be mediated by a transmembrane signal transduction mechanism, accumulating evidence suggests that Ang-II may also have a direct nuclear action. We have characterized the nuclear Ang-II-binding site in purified nuclei preparation from rat liver and compared it to plasma membrane Ang-II receptors. [125I]Ang-II binding to isolated nuclei reached equilibration in 30 min at 25 C, slower than binding to plasma membrane, which reached equilibration within 10 min. Scatchard analysis of [125I]Ang-II binding to isolated nuclei revealed a single class of binding sites (Kd = 1.4 nM; binding capacity = 10 fmol/mg protein or 460 sites/nucleus). In the nuclear preparation, Ang-II and its fragments competed for binding a potency order of Ang-III = Ang-II greater than Ang-II-(1-7) greater than Ang-II-(1-6) greater than Ang-II-(1-5). Losartan potassium (DuP 753), a selective blocker of the Ang-II receptor subtype I, fully inhibits nuclear Ang-II binding with affinity similar to that in plasma membrane. The pH optimum for [125I]Ang-II binding to nuclei was 7.0, while binding to plasma membrane was optimal at pH 8.0. Low concentrations (0.05-0.1 mM) of dithiothreitol increased [125I]Ang-II binding to nuclei, but not to plasma membrane. In the absence of detergent, Ang-II-binding sites appear to consist of soluble protein releasable from nuclei by freezing and thawing, hence distinct in physicochemical properties from the membrane-bound receptor. Size-exclusion HPLC estimated the mol wt of the soluble Ang-II-binding sites to be 66 kilodaltons. These nuclear Ang-II-binding sites have some similarities to but also show notable physicochemical differences from plasma membrane Ang-II receptors, and they may play a role in mediating the intracellular action of Ang-II. | lld:pubmed |
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| pubmed-article:1612017 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1612017 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1612017 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1612017 | pubmed:citationSubset | AIM | lld:pubmed |
| pubmed-article:1612017 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:1612017 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1612017 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:1612017 | pubmed:issn | 0013-7227 | lld:pubmed |
| pubmed-article:1612017 | pubmed:author | pubmed-author:TangS SSS | lld:pubmed |
| pubmed-article:1612017 | pubmed:author | pubmed-author:DzauV JVJ | lld:pubmed |
| pubmed-article:1612017 | pubmed:author | pubmed-author:RoggHH | lld:pubmed |
| pubmed-article:1612017 | pubmed:author | pubmed-author:SchumacherRR | lld:pubmed |
| pubmed-article:1612017 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1612017 | pubmed:volume | 131 | lld:pubmed |
| pubmed-article:1612017 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1612017 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1612017 | pubmed:pagination | 374-80 | lld:pubmed |
| pubmed-article:1612017 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:1612017 | pubmed:meshHeading | pubmed-meshheading:1612017-... | lld:pubmed |
| pubmed-article:1612017 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1612017 | pubmed:articleTitle | Characterization of nuclear angiotensin-II-binding sites in rat liver and comparison with plasma membrane receptors. | lld:pubmed |
| pubmed-article:1612017 | pubmed:affiliation | Molecular and Cellular Vascular Research Laboratory, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts 02115. | lld:pubmed |
| pubmed-article:1612017 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1612017 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:1612017 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:1612017 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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