| pubmed-article:14686920 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:14686920 | lifeskim:mentions | umls-concept:C0225336 | lld:lifeskim |
| pubmed-article:14686920 | lifeskim:mentions | umls-concept:C0007603 | lld:lifeskim |
| pubmed-article:14686920 | lifeskim:mentions | umls-concept:C1383501 | lld:lifeskim |
| pubmed-article:14686920 | lifeskim:mentions | umls-concept:C1744635 | lld:lifeskim |
| pubmed-article:14686920 | lifeskim:mentions | umls-concept:C0271510 | lld:lifeskim |
| pubmed-article:14686920 | lifeskim:mentions | umls-concept:C0004083 | lld:lifeskim |
| pubmed-article:14686920 | lifeskim:mentions | umls-concept:C0181586 | lld:lifeskim |
| pubmed-article:14686920 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:14686920 | pubmed:dateCreated | 2003-12-22 | lld:pubmed |
| pubmed-article:14686920 | pubmed:abstractText | Cytosolic phospholipase A2-alpha (cPLA2-alpha) is a calcium-activated enzyme involved in agonist-induced arachidonic acid release. In endothelial cells, free arachidonic acid is predominantly converted into prostacyclin, a potent vasodilator and inhibitor of platelet activation. As the rate-limiting step in prostacyclin production is the generation of free arachidonic acid by cPLA2-alpha, this enzyme has become an attractive pharmacological target and the focus of many studies. Following stimulation with calcium-mobilizing agonists, cPLA2-alpha translocates to intracellular phospholipid membranes via its C2 domain. In this study, the calcium-induced association of cPLA2-alpha with EA.hy.926 endothelial cell membranes was investigated. Subcellular fractionation and immunofluorescence studies showed that following stimulation with histamine, thrombin or the calcium ionophore A23187, cPLA2-alpha relocated to intracellular membranes. Treatment of A23187-stimulated cells with EGTA or BAPTA-AM demonstrated that a substantial pool of cPLA2-alpha remained associated with membrane fractions in a calcium-independent manner. Furthermore, immunofluorescence microscopy studies revealed that cells stimulated for periods of greater than 10 min showed a high proportion of calcium-independent membrane-associated cPLA2-alpha. Calcium-independent membrane association of cPLA2-alpha was not due to hydrophobic or cytoskeletal interactions. Finally, the recombinant C2 domain of cPLA2-alpha exhibited calcium-independent membrane binding to membranes isolated from A23187-stimulated cells but not those isolated from nonstimulated cells. These findings suggest that novel mechanisms involving accessory proteins at the target membrane play a role in the regulation of cPLA2-alpha. Such regulatory associations could enable the cell to discriminate between the varying levels of cytosolic calcium induced by different stimuli. | lld:pubmed |
| pubmed-article:14686920 | pubmed:language | eng | lld:pubmed |
| pubmed-article:14686920 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14686920 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:14686920 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14686920 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14686920 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14686920 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14686920 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14686920 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14686920 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14686920 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:14686920 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:14686920 | pubmed:issn | 0014-2956 | lld:pubmed |
| pubmed-article:14686920 | pubmed:author | pubmed-author:SmithJennifer... | lld:pubmed |
| pubmed-article:14686920 | pubmed:author | pubmed-author:WalkerJohnJ | lld:pubmed |
| pubmed-article:14686920 | pubmed:author | pubmed-author:PonnambalamSr... | lld:pubmed |
| pubmed-article:14686920 | pubmed:author | pubmed-author:GrewalSeemaS | lld:pubmed |
| pubmed-article:14686920 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:14686920 | pubmed:volume | 271 | lld:pubmed |
| pubmed-article:14686920 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:14686920 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:14686920 | pubmed:pagination | 69-77 | lld:pubmed |
| pubmed-article:14686920 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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| pubmed-article:14686920 | pubmed:meshHeading | pubmed-meshheading:14686920... | lld:pubmed |
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| pubmed-article:14686920 | pubmed:meshHeading | pubmed-meshheading:14686920... | lld:pubmed |
| pubmed-article:14686920 | pubmed:meshHeading | pubmed-meshheading:14686920... | lld:pubmed |
| pubmed-article:14686920 | pubmed:meshHeading | pubmed-meshheading:14686920... | lld:pubmed |
| pubmed-article:14686920 | pubmed:meshHeading | pubmed-meshheading:14686920... | lld:pubmed |
| pubmed-article:14686920 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:14686920 | pubmed:articleTitle | Stimulation-dependent recruitment of cytosolic phospholipase A2-alpha to EA.hy.926 endothelial cell membranes leads to calcium-independent association. | lld:pubmed |
| pubmed-article:14686920 | pubmed:affiliation | School of Biochemistry and Molecular Biology, University of Leeds, UK. | lld:pubmed |
| pubmed-article:14686920 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:14686920 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:5321 | entrezgene:pubmed | pubmed-article:14686920 | lld:entrezgene |
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