| pubmed-article:10516168 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10516168 | lifeskim:mentions | umls-concept:C0080103 | lld:lifeskim |
| pubmed-article:10516168 | lifeskim:mentions | umls-concept:C0001473 | lld:lifeskim |
| pubmed-article:10516168 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:10516168 | lifeskim:mentions | umls-concept:C0598428 | lld:lifeskim |
| pubmed-article:10516168 | lifeskim:mentions | umls-concept:C0332120 | lld:lifeskim |
| pubmed-article:10516168 | lifeskim:mentions | umls-concept:C0050734 | lld:lifeskim |
| pubmed-article:10516168 | pubmed:issue | 4 Pt 2 | lld:pubmed |
| pubmed-article:10516168 | pubmed:dateCreated | 1999-11-17 | lld:pubmed |
| pubmed-article:10516168 | pubmed:abstractText | Adducin point mutations are associated with genetic hypertension in Milan hypertensive strain (MHS) rats and in humans. In transfected cells, adducin affects actin cytoskeleton organization and increases the Na(+)-K(+)-pump rate. The present study has investigated whether rat and human adducin polymorphisms differently modulate rat renal Na(+)-K(+)-ATPase in vitro. We report the following. 1) Both rat and human adducins stimulate Na(+)-K(+)-ATPase activity, with apparent affinity in tens of nanomolar concentrations. 2) MHS and Milan normotensive strain (MNS) adducins raise the apparent ATP affinity for Na(+)-K(+)-ATPase. 3) The mechanism of action of adducin appears to involve a selective acceleration of the rate of the conformational change E(2) (K) --> E(1) (Na) or E(2)(K). ATP --> E(1)Na. ATP. 4) Apparent affinities for mutant rat and human adducins are significantly higher than those for wild types. 5) Recombinant human alpha- and beta-adducins stimulate Na(+)-K(+)-ATPase activity, as do the COOH-terminal tails, and the mutant proteins display higher affinities than the wild types. 6) The cytoskeletal protein ankyrin, which is known to bind to Na(+)-K(+)-ATPase, also stimulates enzyme activity, whereas BSA is without effect; the effects of adducin and ankyrin when acting together are not additive. 7) Pig kidney medulla microsomes appear to contain endogenous adducin; in contrast with purified pig kidney Na(+)-K(+)-ATPase, which does not contain adducin, added adducin stimulates the Na(+)-K(+)-ATPase activity of microsomes only about one-half as much as that of purified Na(+)-K(+)-ATPase. Our findings strongly imply the existence of a direct and specific interaction between adducin and Na(+)-K(+)-ATPase in vitro and also suggest the possibility of such an interaction in intact renal membranes. | lld:pubmed |
| pubmed-article:10516168 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10516168 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10516168 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10516168 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10516168 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10516168 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:10516168 | pubmed:issn | 0002-9513 | lld:pubmed |
| pubmed-article:10516168 | pubmed:author | pubmed-author:SalardiSS | lld:pubmed |
| pubmed-article:10516168 | pubmed:author | pubmed-author:FerrariPP | lld:pubmed |
| pubmed-article:10516168 | pubmed:author | pubmed-author:RiveraRR | lld:pubmed |
| pubmed-article:10516168 | pubmed:author | pubmed-author:BianchiGG | lld:pubmed |
| pubmed-article:10516168 | pubmed:author | pubmed-author:KarlishS JSJ | lld:pubmed |
| pubmed-article:10516168 | pubmed:author | pubmed-author:TripodiGG | lld:pubmed |
| pubmed-article:10516168 | pubmed:author | pubmed-author:GoldshlegerRR | lld:pubmed |
| pubmed-article:10516168 | pubmed:author | pubmed-author:FerrandiMM | lld:pubmed |
| pubmed-article:10516168 | pubmed:author | pubmed-author:ManuntaPP | lld:pubmed |
| pubmed-article:10516168 | pubmed:author | pubmed-author:BarassiPP | lld:pubmed |
| pubmed-article:10516168 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10516168 | pubmed:volume | 277 | lld:pubmed |
| pubmed-article:10516168 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10516168 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10516168 | pubmed:pagination | H1338-49 | lld:pubmed |
| pubmed-article:10516168 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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| pubmed-article:10516168 | pubmed:meshHeading | pubmed-meshheading:10516168... | lld:pubmed |
| pubmed-article:10516168 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10516168 | pubmed:articleTitle | Evidence for an interaction between adducin and Na(+)-K(+)-ATPase: relation to genetic hypertension. | lld:pubmed |
| pubmed-article:10516168 | pubmed:affiliation | Prassis Research Institute Sigma-Tau, 20019 Settimo Milanese, Italy. | lld:pubmed |
| pubmed-article:10516168 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10516168 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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