Caspase-mediated inhibition of sphingomyelin synthesis is involved in FasL-triggered cell death

@article{Lafont2010CaspasemediatedIO,
  title={Caspase-mediated inhibition of sphingomyelin synthesis is involved in FasL-triggered cell death},
  author={Elodie Lafont and Delphine Milhas and St{\'e}phane Carpentier and Virginie Garcia and Z-X Jin and Hisanori Umehara and Toshiro Okazaki and Klaus Schulze-Osthoff and Thierry Levade and Herv{\'e} Benoist and Bruno S{\'e}gui},
  journal={Cell Death and Differentiation},
  year={2010},
  volume={17},
  pages={642-654}
}
Ceramide can be converted into sphingomyelin by sphingomyelin synthases (SMS) 1 and 2. In this study, we show that in human leukemia Jurkat cells, which express mainly SMS1, Fas ligand (FasL) treatment inhibited SMS activity in a dose- and time-dependent manner before nuclear fragmentation. The SMS inhibition elicited by FasL (1) was abrogated by benzyloxycarbonyl valyl-alanyl-aspartyl-(O-methyl)-fluoromethylketone (zVAD-fmk), a broad-spectrum caspase inhibitor; (2) did not occur in caspase-8… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 16 extracted citations

References

Publications referenced by this paper.
Showing 1-10 of 47 references

Identification of a family of animal sphingomyelin synthases

  • K Huitema, J van den Dikkenberg, JF Brouwers, JC. Holthuis
  • EMBO J
  • 2004
Highly Influential
6 Excerpts

Similar Papers

Loading similar papers…