| pubmed-article:8622972 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8622972 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:8622972 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:8622972 | lifeskim:mentions | umls-concept:C1996904 | lld:lifeskim |
| pubmed-article:8622972 | lifeskim:mentions | umls-concept:C0032615 | lld:lifeskim |
| pubmed-article:8622972 | lifeskim:mentions | umls-concept:C1880497 | lld:lifeskim |
| pubmed-article:8622972 | lifeskim:mentions | umls-concept:C0597484 | lld:lifeskim |
| pubmed-article:8622972 | lifeskim:mentions | umls-concept:C0439799 | lld:lifeskim |
| pubmed-article:8622972 | lifeskim:mentions | umls-concept:C0332120 | lld:lifeskim |
| pubmed-article:8622972 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:8622972 | pubmed:dateCreated | 1996-6-18 | lld:pubmed |
| pubmed-article:8622972 | pubmed:abstractText | The effects of free polyunsaturated fatty acids (PUFA) on the binding of ligands to receptors on voltage-sensitive Na+ channels of neonatal rat cardiac myocytes were assessed. The radioligand was [benzoyl-2,5-(3)H] batrachotoxinin A 20alpha-benzoate ([(3)H]BTXB), a toxin that binds to the Na+ channel. The PUFA that have been shown to be antiarrhythmic, including eicosapentaenoic acid (EPA; C20:5n-3), docosahexaenoic acid (DHA; C22:6n-3), eicosatetraynoic acid (ETYA), linolenic acid (C18:3n-3), and linoleic acid (C18:2n-6), inhibited [(3)H]BTXB binding in a dose-dependent fashion with IC50 values of 28-35 microM, whereas those fatty acids that have no antiarrhythmic effects including saturated fatty acid (stearic acid, C18:0), monounsaturated fatty acid (oleic acid; C18:1n-9), and EPA methyl ester did not have a significant effect on [(3)H]BTXB binding. Enrichment of the myocyte membrane with cholesterol neither affected [(3)H]BTXB binding when compared with control cells nor altered the inhibitory effects of PUFA on [(3)H]BTXB binding. Scatchard analysis of [(3)H]BTXB binding showed that EPA reduced the maximal binding without altering the Kd for [(3)H]BTXB binding, indicating allosteric inhibition. The inhibition by EPA of [(3)H]BTXB binding was reversible (within 30 min) when delipidated bovine serum albumin was added. The binding of the PUFA to this site on the Na+ channel is reversible and structure-specific and occurs at concentrations close to those required for apparent antiarrhythmic effects and a blocking effect on the Na+ current, suggesting that binding of the PUFA at this site relates to their antiarrhythmic action. | lld:pubmed |
| pubmed-article:8622972 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8622972 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8622972 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8622972 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8622972 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8622972 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8622972 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8622972 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8622972 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8622972 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8622972 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8622972 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8622972 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8622972 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8622972 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8622972 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8622972 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8622972 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8622972 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8622972 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8622972 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8622972 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8622972 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8622972 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8622972 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8622972 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8622972 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8622972 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8622972 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8622972 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8622972 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8622972 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8622972 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8622972 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8622972 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8622972 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8622972 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8622972 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8622972 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8622972 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8622972 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8622972 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:8622972 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:8622972 | pubmed:author | pubmed-author:LeafAA | lld:pubmed |
| pubmed-article:8622972 | pubmed:author | pubmed-author:KangJ XJX | lld:pubmed |
| pubmed-article:8622972 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8622972 | pubmed:day | 16 | lld:pubmed |
| pubmed-article:8622972 | pubmed:volume | 93 | lld:pubmed |
| pubmed-article:8622972 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8622972 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8622972 | pubmed:pagination | 3542-6 | lld:pubmed |
| pubmed-article:8622972 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:8622972 | pubmed:meshHeading | pubmed-meshheading:8622972-... | lld:pubmed |
| pubmed-article:8622972 | pubmed:meshHeading | pubmed-meshheading:8622972-... | lld:pubmed |
| pubmed-article:8622972 | pubmed:meshHeading | pubmed-meshheading:8622972-... | lld:pubmed |
| pubmed-article:8622972 | pubmed:meshHeading | pubmed-meshheading:8622972-... | lld:pubmed |
| pubmed-article:8622972 | pubmed:meshHeading | pubmed-meshheading:8622972-... | lld:pubmed |
| pubmed-article:8622972 | pubmed:meshHeading | pubmed-meshheading:8622972-... | lld:pubmed |
| pubmed-article:8622972 | pubmed:meshHeading | pubmed-meshheading:8622972-... | lld:pubmed |
| pubmed-article:8622972 | pubmed:meshHeading | pubmed-meshheading:8622972-... | lld:pubmed |
| pubmed-article:8622972 | pubmed:meshHeading | pubmed-meshheading:8622972-... | lld:pubmed |
| pubmed-article:8622972 | pubmed:meshHeading | pubmed-meshheading:8622972-... | lld:pubmed |
| pubmed-article:8622972 | pubmed:meshHeading | pubmed-meshheading:8622972-... | lld:pubmed |
| pubmed-article:8622972 | pubmed:meshHeading | pubmed-meshheading:8622972-... | lld:pubmed |
| pubmed-article:8622972 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8622972 | pubmed:articleTitle | Evidence that free polyunsaturated fatty acids modify Na+ channels by directly binding to the channel proteins. | lld:pubmed |
| pubmed-article:8622972 | pubmed:affiliation | Department of Medicine, Harvard Medical School, Boston, MA 02114, USA. | lld:pubmed |
| pubmed-article:8622972 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8622972 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8622972 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8622972 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8622972 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8622972 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8622972 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8622972 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8622972 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8622972 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8622972 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8622972 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8622972 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8622972 | lld:pubmed |
