ACTIVATION, FUNCTIONING, REGULATION AND LOCALIZATION OF PHOSPHOLIPASE D AT THE INTERFACE

Abstract

The review elucidates works on isolation of phospholipase D from various sources, a detailed study of its activation at the interface during hydrolysis of lecithin and lysolecithin in the presence of metal ions, organic solvents, detergents, adsorbents and products of hydrolysis, as well as in composition of mitochondrial membranes and microsomes under various reaction conditions. Based on the research findings, a hypothesis is being put forward about activation, functioning, regulation and localization of phospholipase D at the interface of lipid-water, lipid-lipid and lipid-protein phases in the course of forming of a cluster, raft or microdomain with products of hydrolysis or their natural and synthetic analogues in the presence of bivalent metal ions. Phospholipase D is considered as a pri-membrane vector enzyme, a lateral pump, or as a 2D printer that converts a substrate into a product while depositing it with Ca2+ ions into a growing new phosphatidate microdomain.
Possible applications of the proposed mechanism of lipolysis regulation in solving various issues of membranology, biotechnology, nutrition and medical practice are being discussed.