Cellular regulation and proposed biological functions of group VIA calcium-independent phospholipase A2 in activated cells.
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.
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
Jesús
J
Balsinde
María A
MA
Balboa
D000595:Amino Acid Sequence; D000818:Animals; D017209:Apoptosis; D048708:Cell Growth Processes; D002633:Chemotaxis; D015777:Eicosanoids / Q000378:metabolism; D004791:Enzyme Inhibitors / Q000494:pharmacology; D054522:Group VI Phospholipases A2; D006801:Humans; D008969:Molecular Sequence Data; D010741:Phospholipases A / Q000737:chemistry / Q000378:metabolism / Q000502:physiology*; D054467:Phospholipases A2; D015398:Signal Transduction
D015777:Eicosanoids; D004791:Enzyme Inhibitors; D010741:Phospholipases A; D054522:Group VI Phospholipases A2; C516475:PLA2G6 protein, human; D054467:Phospholipases A2