Cellular regulation and proposed biological functions of group VIA calcium-independent phospholipase A2 in activated cells

Mammalian cells contain several calcium-independent phospholipase A(2) (PLA(2)) enzymes. The best studied of them is the so-called Group VIA PLA(2) (iPLA(2)-VIA), which is an 85-88 kDa enzyme with unique structural features among the PLA(2) 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, iPLA(2)-VIA may also play distinct roles in cellular signaling. This review focuses on the biochemical mechanisms that regulate the activity of iPLA(2)-VIA in activated cells, and the biological functions proposed for this enzyme during stimulus-response coupling. (c) 2005 Elsevier Inc. All rights reserved.