Membrane structure, toxins and phospholipase A2 activity.

L P Vernon; J D Bell

doi:10.1016/0163-7258(92)90003-i

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Membrane structure, toxins and phospholipase A2 activity.

L P Vernon·J D Bell

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Abstract

The phospholipid-hydrolyzing enzyme phospholipase A2 (PLA2) (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 Ca2+, cytokines, G proteins and other cellular proteins. The major focus is the role of phospholipid structure on PLA2 activity, including (1) the mechanism of PLA2 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 PLA2 activity, with emphasis on the venom and plant toxins melittin, cardiotoxin and Pyrularia thionein.

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Animals Calcium Cell Membrane Cytokines Enzyme Activation GTP-Binding Proteins Humans Models, Biological Phospholipases A Phospholipases A2 Toxins, Biological Journal Article Review

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L P Vernon, J D Bell. 1992. Membrane structure, toxins and phospholipase A2 activity.. https://doi.org/10.1016/0163-7258(92)90003-i

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