Cellular regulation and proposed biological functions of group VIA calcium-independent phospholipase A2 in activated cells |
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Authors: | Balsinde Jesús Balboa María A |
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Affiliation: | Eicosanoid Research Division, Institute of Molecular Biology and Genetics, University of Valladolid School of Medicine, Avenida Ramón y Cajal 7, 47005 Valladolid, Spain. jbalsinde@ibgm.uva.es |
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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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