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Group V sPLA2: classical and novel functions.

Barbara Balestrieri·Jonathan P Arm
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Abstract

Group V sPLA(2) is unique among the family of secretory sPLA(2) enzymes in being able to bind to cell membranes through both interfacial-binding and through binding to proteoglycan. The function of group V sPLA(2) as an enzyme and its cross-talk with cPLA(2)alpha in initiating eicosanoid generation is well documented. Evidence, though, is emerging on the ability of this molecule to act as a regulator of several intracellular and extracellular pathways independently of its ability to provide arachidonic acid for eicosanoid generation, acting within the cell or as a secreted enzyme. In this article we will provide an overview of the properties of the enzyme and how they relate to our current understanding of its function.

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AnimalsArachidonic AcidEicosanoidsGroup IV Phospholipases A2Group V Phospholipases A2HumansPhospholipases AProtein BindingProteoglycansSignal TransductionJournal ArticleReview

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Barbara Balestrieri, Jonathan P Arm. 2006-07-28. Group V sPLA2: classical and novel functions.. https://doi.org/10.1016/j.bbalip.2006.07.008

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