Arachidonate supports hydrolysis of phosphatidylinositol by neutrophil cytosolic phospholipase C: Relation to NADPH oxidase

A. Faber, I. Aviram

Research output: Contribution to journalArticlepeer-review

Abstract

NADPH oxidase is a superoxide-generating, membrane-bound complex activated in stimulated phagocytes or in a reconstituted system consisting of membranes, cytosolic components and arachidonate or SDS. To delineate mechanism of oxidase activation in the cell-free system, hydrolysis of phosphoinositides in the combined membrane-cytosol oxidase mixture was investigated. Arachidonate promoted hydrolysis of membrane-[3H]-phosphatidylinositol by cytosolic phospholipase C. PI hydrolysis was similarly supported by other unsaturated fatty acids and by SDS. Unlike activation of the NADPH oxidase, PI hydrolysis required the presence of calcium ions. Implications of these findings to the mechanism of NADPH oxidase activation are discussed.

Original languageEnglish
Pages (from-to)751-758
Number of pages8
JournalBiochemistry International
Volume23
Issue number4
StatePublished - 1991

Fingerprint

Dive into the research topics of 'Arachidonate supports hydrolysis of phosphatidylinositol by neutrophil cytosolic phospholipase C: Relation to NADPH oxidase'. Together they form a unique fingerprint.

Cite this