| pubmed-article:2622457 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2622457 | lifeskim:mentions | umls-concept:C1135183 | lld:lifeskim |
| pubmed-article:2622457 | lifeskim:mentions | umls-concept:C0018787 | lld:lifeskim |
| pubmed-article:2622457 | lifeskim:mentions | umls-concept:C0036208 | lld:lifeskim |
| pubmed-article:2622457 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:2622457 | lifeskim:mentions | umls-concept:C0023779 | lld:lifeskim |
| pubmed-article:2622457 | lifeskim:mentions | umls-concept:C0443286 | lld:lifeskim |
| pubmed-article:2622457 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:2622457 | lifeskim:mentions | umls-concept:C0205409 | lld:lifeskim |
| pubmed-article:2622457 | lifeskim:mentions | umls-concept:C0260009 | lld:lifeskim |
| pubmed-article:2622457 | lifeskim:mentions | umls-concept:C0439596 | lld:lifeskim |
| pubmed-article:2622457 | pubmed:issue | 1-2 | lld:pubmed |
| pubmed-article:2622457 | pubmed:dateCreated | 1990-3-23 | lld:pubmed |
| pubmed-article:2622457 | pubmed:abstractText | Premethylation of purified porcine cardiac sarcolemma (SL) in the presence of 0.15, 10 and 150 microM S-adenosyl-L-methionine (AdoMet) did not change the phosphorylation of SL proteins catalyzed either by intrinsic cyclic AMP-dependent protein kinase (cAK) or by added catalytic (C) subunit of this enzyme. On the other hand, membrane exhibited increased lipid methyltransferase activity after preincubation with MgATP and C subunit. Prephosphorylation of membranes stimulated the total [3H]-methyl incorporation into SL lipids assayed at 0.15 microM [3H]AdoMet due to an enhancement of Vmax and without changes in the Km value for AdoMet. Analysis of the methylated lipid products revealed an increased methyl group incorporation into a nonpolar lipid fraction whereas phosphatidylethanolamine-N-methylation was not affected by phosphorylation. The results suggest that the cyclic AMP-mediated signal transduction at the level of cardiac SL is not affected by methylation-induced modifications of the membrane lipid microdomains. On the other hand, an intrinsic SL lipid methyltransferase activity is apparently not related to the N-methylation of phospholipids, is modulated by cyclic AMP-dependent protein phosphorylation. | lld:pubmed |
| pubmed-article:2622457 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2622457 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2622457 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2622457 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2622457 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2622457 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2622457 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2622457 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2622457 | pubmed:issn | 0300-8177 | lld:pubmed |
| pubmed-article:2622457 | pubmed:author | pubmed-author:DhallaN SNS | lld:pubmed |
| pubmed-article:2622457 | pubmed:author | pubmed-author:DaoTT | lld:pubmed |
| pubmed-article:2622457 | pubmed:author | pubmed-author:VetterRR | lld:pubmed |
| pubmed-article:2622457 | pubmed:author | pubmed-author:PanagiaVV | lld:pubmed |
| pubmed-article:2622457 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2622457 | pubmed:volume | 91 | lld:pubmed |
| pubmed-article:2622457 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2622457 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2622457 | pubmed:pagination | 51-61 | lld:pubmed |
| pubmed-article:2622457 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:2622457 | pubmed:meshHeading | pubmed-meshheading:2622457-... | lld:pubmed |
| pubmed-article:2622457 | pubmed:meshHeading | pubmed-meshheading:2622457-... | lld:pubmed |
| pubmed-article:2622457 | pubmed:meshHeading | pubmed-meshheading:2622457-... | lld:pubmed |
| pubmed-article:2622457 | pubmed:meshHeading | pubmed-meshheading:2622457-... | lld:pubmed |
| pubmed-article:2622457 | pubmed:meshHeading | pubmed-meshheading:2622457-... | lld:pubmed |
| pubmed-article:2622457 | pubmed:meshHeading | pubmed-meshheading:2622457-... | lld:pubmed |
| pubmed-article:2622457 | pubmed:meshHeading | pubmed-meshheading:2622457-... | lld:pubmed |
| pubmed-article:2622457 | pubmed:meshHeading | pubmed-meshheading:2622457-... | lld:pubmed |
| pubmed-article:2622457 | pubmed:meshHeading | pubmed-meshheading:2622457-... | lld:pubmed |
| pubmed-article:2622457 | pubmed:meshHeading | pubmed-meshheading:2622457-... | lld:pubmed |
| pubmed-article:2622457 | pubmed:meshHeading | pubmed-meshheading:2622457-... | lld:pubmed |
| pubmed-article:2622457 | pubmed:meshHeading | pubmed-meshheading:2622457-... | lld:pubmed |
| pubmed-article:2622457 | pubmed:articleTitle | Interactions between cyclic AMP-dependent protein phosphorylation and lipid transmethylation reactions in isolated porcine cardiac sarcolemma. | lld:pubmed |
| pubmed-article:2622457 | pubmed:affiliation | Division of Cardiovascular Sciences, St. Boniface General Hospital Research Centre, Winnipeg, Canada. | lld:pubmed |
| pubmed-article:2622457 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2622457 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
