| http://purl.uniprot.org/citations/14686920 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/14686920 | http://www.w3.org/2000/01/rdf-schema#comment | "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."xsd:string |
| http://purl.uniprot.org/citations/14686920 | http://purl.org/dc/terms/identifier | "doi:10.1046/j.1432-1033.2003.03903.x"xsd:string |
| http://purl.uniprot.org/citations/14686920 | http://purl.uniprot.org/core/author | "Smith J."xsd:string |
| http://purl.uniprot.org/citations/14686920 | http://purl.uniprot.org/core/author | "Walker J."xsd:string |
| http://purl.uniprot.org/citations/14686920 | http://purl.uniprot.org/core/author | "Ponnambalam S."xsd:string |
| http://purl.uniprot.org/citations/14686920 | http://purl.uniprot.org/core/author | "Grewal S."xsd:string |
| http://purl.uniprot.org/citations/14686920 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/14686920 | http://purl.uniprot.org/core/name | "Eur J Biochem"xsd:string |
| http://purl.uniprot.org/citations/14686920 | http://purl.uniprot.org/core/pages | "69-77"xsd:string |
| http://purl.uniprot.org/citations/14686920 | http://purl.uniprot.org/core/title | "Stimulation-dependent recruitment of cytosolic phospholipase A2-alpha to EA.hy.926 endothelial cell membranes leads to calcium-independent association."xsd:string |
| http://purl.uniprot.org/citations/14686920 | http://purl.uniprot.org/core/volume | "271"xsd:string |
| http://purl.uniprot.org/citations/14686920 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/14686920 |
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