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J Biol Chem, Vol. 274, Issue 30, 20763-20771, July 23, 1999

Sphingolipid Depletion Increases Formation of the Scrapie Prion Protein in Neuroblastoma Cells Infected with Prions

Naava NaslavskyDagger , Hilary Shmeeda, Gilgi FriedlanderDagger , Anat YanaiDagger , Anthony H. Futermanparallel , Yechezkel Barenholz, and Albert TaraboulosDagger

From the Departments of Dagger  Molecular Biology and  Biochemistry, The Hebrew University-Hadassah Medical School, P. O. Box 12272, Jerusalem 91120 and the parallel  Department of Biological Chemistry, The Weizmann Institute of Sciences, Rehovot 76100, Israel

Sphingolipid-rich rafts play an essential role in the posttranslational (Borchelt, D. R., Scott, M., Taraboulos, A., Stahl, N., and Prusiner, S. B. (1990) J. Cell Biol. 110, 743-752)) formation of the scrapie prion protein PrPSc from its normal conformer PrPC (Taraboulos, A., Scott, M., Semenov, A., Avrahami, D., Laszlo, L., Prusiner, S. B., and Avraham, D. (1995) J. Cell Biol. 129, 121-132). We investigated the importance of sphingolipids in the metabolism of the PrP isoforms in scrapie-infected ScN2a cells. The ceramide synthase inhibitor fumonisin B1 (FB1) reduced both sphingomyelin (SM) and ganglioside GM1 in cells by up to 50%, whereas PrPSc increased by 3-4-fold. Whereas FB1 profoundly altered the cell lipid composition, the raft residents PrPC, PrPSc, caveolin 1, and GM1 remained insoluble in Triton X-100. Metabolic radiolabeling demonstrated that PrPC production was either unchanged or slightly reduced in FB1-treated cells, whereas PrPSc formation was augmented by 3-4-fold. To identify the sphingolipid species the decrease of which correlates with increased PrPSc, we used two other reagents. When cells were incubated with sphingomyelinase for 3 days, SM levels decreased, GM1 was unaltered, and PrPSc increased by 3-4-fold. In contrast, the glycosphingolipid inhibitor PDMP reduced PrPSc while increasing SM. Thus, PrPSc seems to correlate inversely with SM levels. The effects of SM depletion contrasted with those previously obtained with the cholesterol inhibitor lovastatin, which reduced PrPSc and removed it from detergent-insoluble complexes.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.


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