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Abstract
The phospholipid-hydrolyzing enzyme phospholipase A 2 (PLA 2) (EC 3.1.1.4) exists in several forms which can be located in the cytosol or on cellular membranes. We review briefly cellular regulatory mechanisms involving covalent modification by protein kinase C and the action of Ca 2+, cytokines, G proteins and other cellular proteins. The major focus is the role of phospholipid structure on PLA 2 actvity, including (1) the mechanism of PLA 2 action on synthetic phospholipid bilayers, (2) perturbation of synthetic and cellular membranes with lipophilic agents and membrane-interactive peptides and (3) the ability of these agents to activate endogenous PLA 2 activity, with emphasis on the venom and plant toxins melittin, cardiotoxin and Pyrularia thionin.
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