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Molecules in focus: cytosolic phospholipase A2-alpha.

Authors: Niknami, M  Patel, M  Witting, PK  Dong, Q 
Citation: Niknami M, etal., Int J Biochem Cell Biol. 2009 May;41(5):994-7. doi: 10.1016/j.biocel.2008.07.017. Epub 2008 Aug 8.
Pubmed: (View Article at PubMed) PMID:18761105
DOI: Full-text: DOI:10.1016/j.biocel.2008.07.017

Cytosolic phospholipase A(2)-alpha (cPLA(2)-alpha) cleaves its preferred substrate, arachidonic acid, at the sn-2 position of membrane glycerophospholipids. Stimulation of cells with agents that mobilize intracellular calcium and/or promote the phosphorylation of cPLA(2)-alpha leads to (i) translocation of the enzyme from cytosol to endoplasmic reticulum, Golgi apparatus and perinuclear membranes-where it associates with the arachidonic acid in close proximity to downstream eicosanoid-producing enzymes; and (ii) the change in configuration induced by phosphorylation increases the phospholipid binding affinity and arachidonic acid release. As a mediator of growth factors, cytokines, chemokines, and hormones that modulate survival and growth in various cell types, cPLA(2)-alpha has attracted considerable attention as a potential therapeutic target in control of inflammation and cancer. The importance of the enzyme may have been underestimated by the relatively normal phenotype in the enzyme knockout animals. A clear phenotype has emerged when these knockout animals are used as models of various diseases.


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RGD Object Information
RGD ID: 8552898
Created: 2014-04-30
Species: All species
Last Modified: 2014-04-30
Status: ACTIVE


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