| Literature DB >> 15993747 |
Jesús Balsinde1, María A Balboa.
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.Entities:
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Year: 2005 PMID： 15993747 DOI： 10.1016/j.cellsig.2005.03.002
Source DB: PubMed Journal: Cell Signal ISSN： 0898-6568 Impact factor: 4.315