Fas ligand-induced apoptosis is regulated by nitric oxide through the inhibition of fas receptor clustering and the nitrosylation of protein kinase Cepsilon.

@article{Dash2007FasLA,
  title={Fas ligand-induced apoptosis is regulated by nitric oxide through the inhibition of fas receptor clustering and the nitrosylation of protein kinase Cepsilon.},
  author={Philip R. Dash and James McCormick and Mika J C B Thomson and Alan P. Johnstone and Judith E. Cartwright and Guy S Whitley},
  journal={Experimental cell research},
  year={2007},
  volume={313 16},
  pages={
          3421-31
        }
}
Apoptosis induced by the death-inducing ligand FasL (CD95L) is a major mechanism of cell death. Trophoblast cells express the Fas receptor yet survive in an environment that is rich in the ligand. We report that basal nitric oxide (NO) production is responsible for the resistance of trophoblasts to FasL-induced apoptosis. In this study we demonstrate that basal NO production resulted in the inhibition of receptor clustering following ligand binding. In addition NO also protected cells through… CONTINUE READING

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