Cellular regulation and proposed biological functions of group VIA calcium-independent phospholipase A2 in activated cells
- PMID: 15993747
- DOI: 10.1016/j.cellsig.2005.03.002
Cellular regulation and proposed biological functions of group VIA calcium-independent phospholipase A2 in activated cells
Abstract
Mammalian cells contain several calcium-independent phospholipase A2 (PLA2) enzymes. The best studied of them is the so-called Group VIA PLA2 (iPLA2-VIA), which is an 85-88 kDa enzyme with unique structural features among the PLA2 superfamily of enzymes, and has been found to play a key role in homeostatic membrane phospholipid metabolism in various cell types. Growing evidence suggests that, in addition to its homeostatic function, iPLA2-VIA may also play distinct roles in cellular signaling. This review focuses on the biochemical mechanisms that regulate the activity of iPLA2-VIA in activated cells, and the biological functions proposed for this enzyme during stimulus-response coupling.
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