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Journal of Lipid Research, Vol. 41, 1680-1688, October 2000
Copyright © 2000 by Lipid Research, Inc.

Original Article

Sphingolipids and cholesterol modulate membrane susceptibility to cytosolic phospholipase A₂

Correspondence to: Kamen S. Koumanov

Modulation of cytosolic phospholipase A₂ (cPLA₂) activity by sphingomyelin (SPH), ceramide (Cer), and cholesterol (Chol) was investigated in CHO-2B cells activated by the calcium ionophore A23187 and epinephrine. Chol depletion of CHO-2B cells by treatment with methyl-ß-cyclodextrin (5 mM) resulted in the inhibition of the release of arachidonic acid whereas the restoration of the level by Chol-loaded cyclodextrin relieved inhibition. Conversion of CHO-2B cellular SPH to Cer by Staphylococcus aureus sphingomyelinase enhanced endogenous cPLA₂ activation as well as uptake by cells of C2- and C6-ceramide analogs. These results were confirmed in vitro with purified human recombinant cPLA₂ acting on a model phospholipid substrate. The enzyme activity was inhibited by SPH but reactivated by Cer as well as by Chol added to glycerophospholipid liposomal substrates containing SPH.

The results of this study, which combine in situ and in vitro experimental approaches, indicate that membrane microdomains enriched in SPH and Chol play a role in the modulation of the activity of cPLA₂ and in arachidonic acid-derived mediator production. — Klapisz, E., J. Masliah, G. Béréziat, C. Wolf, and K. S. Koumanov. Sphingolipids and cholesterol modulate membrane susceptibility to cytosolic phospholipase A₂. J. Lipid Res. 2000. 41: 1680;–1688.

Supplementary key words: arachidonic acid, ceramide, CHO cells, cholesterol, phospholipase A₂, sphingomyelin

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