Regulation of inositol lipid-specific phospholipase Cδ by changes in Ca2+ ion concentrations

Author:

ALLEN Victoria1,SWIGART Philip2,CHEUNG Robert1,COCKCROFT Shamshad2,KATAN Matilda1

Affiliation:

1. CRC Centre for Cell and Molecular Biology, Chester Beatty Laboratories, Fulham Road, London SW3 6JB, U.K.

2. Department of Physiology, Rockefeller Building, University College London, University Street, London W1P 8BT, U.K.

Abstract

Studies of inositol lipid-specific phospholipase C (PLC) have elucidated the main regulatory pathways for PLCβ and PLCγ but the regulation of PLCΔ isoenzymes still remains obscure. Here we demonstrate that an increase in Ca2+ ion concentration within the physiological range (0.1-10 μM) is sufficient to stimulate PLCΔ1, but not PLCγ1 and PLCβ1, to hydrolyse cellular inositol lipids present in permeabilized cells. The activity of PLCΔ1 is further enhanced in the presence of phosphatidylinositol transfer protein (PI-TP). Both full activation by Ca2+ ions and stimulation in the presence of PI-TP require an intact PH domain involved in the membrane attachment of PLCδ1. The physiological implication of this study is that PLCΔ1 could correspond to a previously uncharacterized PLC responsible for Ca2+ ion-stimulated inositol lipid hydrolysis observed in many cellular systems.

Publisher

Portland Press Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry

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