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Biochim Biophys Acta. 2006 Nov;1761(11):1280-8. Epub 2006 Jul 28.

Group V sPLA2: classical and novel functions.

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Department of Medicine, Harvard Medical School, Brigham and Women's Hospital, Boston, MA 02115, USA.


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.

[Indexed for MEDLINE]

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