DOI QR코드

DOI QR Code

Activation of Phospholipase D in Rat Thymocytes by Sphingosine


Abstract

Sphingosine is known to regulate a wide range of cell physiology including growth, differentiation, and apoptosis. In this study, we examined the effect of sphingosine on the phospholipase D (PLD) activity in rat thymocytes. Sphingosine potently stimulated PLD in the absence of extracellular calcium, while depletion of intracellular calcium by BAPTA/AM treatment completely blocked activation of PLD by sphingosine. Sphingosine-induced increase of the intracellular calcium concentration was confirmed using a fluorescent calcium indicator Fluo-3/AM. A phosphoinositide-specific phospholipase C inhibitor U73122 partially inhibited the stimulation of PLD by sphingosine. When mouse PLD2 gene was transfected into mouse thymoma EL4 cells, which lack intrinsic PLD activity, sphingosine could stimulate PLD2 significantly while overexpression of human PLD1 had no effect. Taken together, the sphingosine-stimulated PLD activity in rat thymocytes is dependent on the mobilization of intracellular calcium and appears to be due to the PLD2 isoform.

Keywords

References

  1. Spiegel, S.; Merrill, A. H. Jr. Faseb J. 1996, 10, 1388.
  2. Igarashi, Y. J. Biochem. (Tokyo) 1997, 122, 1080. https://doi.org/10.1093/oxfordjournals.jbchem.a021865
  3. Alessenko, A. V. Biochemistry (Mosc) 1998, 63, 62.
  4. Hannun, Y. A.; Bell, R. M. Science 1987, 235, 670. https://doi.org/10.1126/science.3101176
  5. Spiegel, S.; Milstien, S. Chem. Phys. Lipids 1996, 80, 27. https://doi.org/10.1016/0009-3084(96)02543-1
  6. Chao, C. P.; Laulederkind, S. J.; Ballou, L. R. J. Biol. Chem. 1994, 269, 5849.
  7. Sakano, S.; Takemura, H.; Yamada, K.; Imoto, K.; Kaneko, M.; Ohshika, H. J. Biol. Chem. 1996, 271, 11148. https://doi.org/10.1074/jbc.271.19.11148
  8. Lavie, Y.; Liscovitch, M. J. Biol. Chem. 1990, 265, 3868.
  9. Meacci, E.; Vasta, V.; Neri, S.; Farnararo, M.; Bruni, P. Biochem. Biophys. Res. Commun. 1996, 225, 392. https://doi.org/10.1006/bbrc.1996.1185
  10. Taher, M. M.; Abd-Elfattah, A. S.; Sholley, M. M. Biochem. Mol. Biol. Int. 1998, 46, 993.
  11. Exton, J. H. Physiol. Rev. 1997, 77, 303.
  12. Liscovitch, M.; Czarny, M.; Fiucci, G.; Tang, X. Biochem. J. 2000, 345, 401. https://doi.org/10.1042/0264-6021:3450401
  13. Jung, K.; Koh, E.; Choi, M.-U. Bull. Korean Chem. Soc. 1989, 10, 585.
  14. Errasfa, M.; Rothhut, B.; Russo-Marie, F. Biochem. Biophys. Res. Commun. 1989, 159, 53. https://doi.org/10.1016/0006-291X(89)92403-0
  15. Lee, S. Y.; Yeo, E. J.; Choi, M.-U. Biochem. Biophys. Res. Commun. 1998, 244, 825. https://doi.org/10.1006/bbrc.1998.8348
  16. Yoshimura, S.; Sakai, H.; Ohguchi, K.; Nakashima, S.; Banno, Y.; Nishimura, Y.; Sakai, N.; Nozawa, Y. J. Neurochem. 1997, 69, 713.
  17. Li, L.; Guerini, D.; Carafoli, E. J. Biol. Chem. 2000, 275, 20903. https://doi.org/10.1074/jbc.M000995200
  18. Kullmann, M.; Schneikert, J.; Moll, J.; Heck, S.; Zeiner, M.; Gehring, U.; Cato, A. C. J. Biol. Chem. 1998, 273, 14620. https://doi.org/10.1074/jbc.273.23.14620
  19. Gibbs, T. C.; Meier, K. E. J. Cell. Physiol. 2000, 182, 77. https://doi.org/10.1002/(SICI)1097-4652(200001)182:1<77::AID-JCP9>3.0.CO;2-B
  20. Martinova, E. A. Biochemistry (Mosc) 1998, 63, 102.
  21. Melendez, A. J.; Allen, J. M. Semin. Immunol. 2002, 14, 49. https://doi.org/10.1006/smim.2001.0341
  22. Reid, P. A.; Gardner, S. D.; Williams, D. M.; Harnett, M. M. Immunology 1997, 90, 250. https://doi.org/10.1046/j.1365-2567.1997.00150.x