| First Author | Kramer RM | Year | 1997 |
| Journal | FEBS Lett | Volume | 410 |
| Issue | 1 | Pages | 49-53 |
| PubMed ID | 9247121 | Mgi Jnum | J:41484 |
| Mgi Id | MGI:893962 | Doi | 10.1016/s0014-5793(97)00322-0 |
| Citation | Kramer RM, et al. (1997) Structure, function and regulation of Ca2+-sensitive cytosolic phospholipase A2 (cPLA2). FEBS Lett 410(1):49-53 |
| abstractText | The 85-kDa cytosolic PLA2 (cPLA2) is present in many cells and tissues and its unusual functional properties and catalytic mechanism are being elucidated. Notably, cPLA2 becomes catalytically active in the presence of free Ca2+ concentrations as present in stimulated cells and preferentially cleaves arachidonic acid-containing phospholipids. A variety of agonists, growth factors and cytokines, as well as stressful stimuli activate cPLA2 to hydrolyze cellular phospholipids thereby liberating fatty acids and lysophospholipids and providing the precursor substrates for the biosynthesis of eicosanoids and platelet-activating factor. These products of cPLA2 contribute to inflammatory and degenerative disease states and cPLA2 is therefore an attractive target for the development of novel therapies. |
