Sphingosine, sphingosylphosphorylcholine and sphingosine 1-phosphate modulate phosphatidylserine homeostasis in glioma C6 cells

• Autorzy: Wojcik M. , Baranska J.
• Języki publikacji: EN

Abstrakty

EN

The effect of sphingosine, sphingosylphosphorylcholine and sphingosine 1-phosphate on L-[U-14C]serine incorporation into phosphatidylserine and phosphatidylserine-derived phosphatidylethanolamine was investigated in intact glioma C6 cells. Sphingosine, sphingosylphosphorylcholine and sphingosine 1-phosphate are potent signalling molecules which, due to their physicochemical features, may function as amphiphilic compounds. It has been found that sphingosine and sphingosylphosphorylcholine (amphiphilic cations) significantly increase [14C]phosphatidylserine synthesis and decrease the amount of 14C-labeled phosphatidylethanolamine. Sphingosine 1-phosphate (an amphiphilic anion) was without effect on phosphatidylserine synthesis but, similarly as sphingosine and sphingosylphosphorylcholine, reduced the conversion of phosphatidylserine to phosphatidylethanolamine. These results strongly suggest that sphingosine, sphingosylphosphorylcholine and sphingosine 1-phosphate can modulate cellular phospholipid homeostasis by stimulation of phosphatidylserine synthesis and an interference with phosphatidylserine decarboxylase.

Słowa kluczowe

EN

phosphatidylethanolamine; homeostasis; sphingosine; sphingosylphosphorylcholine; phosphatidylserine; sphingosine 1-phosphate

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 1999
• Tom: 46
• Numer: 1
• Opis fizyczny: p.125-131,fig.

Twórcy

autor

Wojcik M.

• M.Nencki Institute of Experimental Biology, L.Pasteura 3, 02-093 Warsaw, Poland

autor

Baranska J.

Bibliografia

• 1. Brindley, D.N., Abousalham, A., Kikuchi, Y., Wang, C.-N. & Waggoner, D.W. (1996) Bio- chem. CeU Biol 74, 469-476.
• 2. Pyne, S., Tolan, D.G., Conway, A.-M. & Pyne, N. (1996) Biochem. Soc. Trans. 25,549-556.
• 3. Spiegel, S. & Merril, A.H., Jr. (1996) FASEB J. 10, 1388-1397.
• 4. Mayer zu Heringdorf, D., van Koppen, C.J. & Jacobs, K.H. (1997) FEBS Lett. 410, 34-38.
• 5. Van Brooklyn, J.R., Lee, M.-J., Menzeleev, R., Olivera, A., Edsall, L., Cuvillier, O., Thomas, D.M., Coopman, P.J.P., Thangada, S., Liu, C.h., Hla, T. & Spiegel, S. (1998) Cell Biol. 142, 229-240.
• 6. Igarashi, Y. & Yatomi, Y. (1998) Acta Biochim. Polon. 45, 299-309.
• 7. Liscovitch, M. & Lavie, Y. (1991) Biochem. Pharmacol. 42, 2071-2075.
• 8. Wiktorek-Wójcik, M., Banasiak, M., Czarny, M., Stępkowski, D. & Barańska, J. (1997) Bio­chem. Biophys. Res. Commun. 241, 73-78.
• 9. Barańska, J. (1982) Adv. Lipid Res. 19, 163- 184.
• 10. Zborowski, J., Dygas, A. & Wojtczak, L. (1983) FEBS Lett. 157, 179-182.
• 11. Czarny, M.f Sabala, P., Ucieklak, A., Kacz­marek, L. & Barańska, J. (1992) Biochem. Bio­phys. Res. Communl 194, 571-583.
• 12. Zhang, H., Buckley, N.E., Gibson, K. & Spiegel, S. (1990) J. Biol Chem. 265, 76-81.
• 13. Bligh, E.G. & Dyer, W.J. (1959) Can. J. Bio­chem. Physiol. 37, 911-917.
• 14. Kanfer, J. & McCartney. D.G. (1993) J. Neuro- chem. 60, 1228-1235.
• 15. Morikawa, S., Taniguchi, S., Mori, H., Fuji, K., Kaoru, K., Fujiwara, M. & Fujiwara, M. (1986) Biochem. Pharmacol 35, 4473-4477.
• 16. Fujiwara. M., Morikawa, S., Taniguchi, S., Mori, K. & Takori, S. (1986) J. Biochem. 99, 651-625.
• 17. Singh, I.N., Sorrentino, G., Massareli, R. & Kanfer, J.N. (1992) FEBS Lett. 296,166-168.
• 18. Singh, I.N., Massarelli, R. & Kanfer, J.N. (1992) J. Lipid Mediat. 5, 301-311.
• 19. Aussel, C., Pelassy, C. & Bernard, A. (1995) Int J. Biochem. Cell Biol 27, 597-602.
• 20. Brindley, D.N. & Waggoner, D.W. (1996) Chem. Physics Lipids 80, 45-57.
• 21. Wojtczak, L. & Nałęcz, M.J. (1979) Eur. J. Bio­chem. 94, 99-107.
• 22. Vance, J.E. (1991 ) J. Biol Chem. 266,89-97.
• 23. Dygas, A., Sidorko, M., Bobeszko, M. & Ba­rańska, J. (1999) Acta Biochim. Polon. 46, 99-106.
• 24. Nishizuka, Y. (1986) Science 233, 305-312.