Group V sPLA2: classical and novel functions.
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.
Balestrieri
Barbara
B
Department of Medicine, Harvard Medical School, Brigham and Women's Hospital, Boston, MA 02115, USA.
Arm
Jonathan P
JP
D000818:Animals; D016718:Arachidonic Acid / Q000378:metabolism*; D015777:Eicosanoids / Q000096:biosynthesis*; D054513:Group IV Phospholipases A2; D054505:Group V Phospholipases A2; D006801:Humans; D010741:Phospholipases A / Q000235:genetics / Q000378:metabolism*; D011485:Protein Binding / Q000502:physiology; D011509:Proteoglycans / Q000378:metabolism; D015398:Signal Transduction / Q000502:physiology*
D015777:Eicosanoids; D011509:Proteoglycans; D016718:Arachidonic Acid; D010741:Phospholipases A; D054513:Group IV Phospholipases A2; D054505:Group V Phospholipases A2; C516299:PLA2G5 protein, human