Swapping between Fas and granulocyte colony-stimulating factor receptor.


Fas belongs to the tumor necrosis factor/nerve growth factor receptor family. The Fas ligand binds to its receptor, Fas, and induces apoptosis in Fas-bearing cells. The granulocyte colony-stimulating factor receptor (G-CSFR) is a member of the hemopoietic growth factor receptor family. G-CSF induces its dimerization and regulates the proliferation and differentiation of neutrophilic granulocytes. We constructed hybrid receptors between Fas and G-CSFR and expressed them in the mouse T cell line WR19L or the mouse myeloid interleukin-3-dependent FDC-P1 cell line. The Fas ligand or an agonistic anti-Fas antibody stimulated proliferation of the FDC-P1 transformants expressing a chimera consisting of the Fas extracellular and G-CSFR cytoplasmic regions. On the other hand, G-CSF could not induce apoptosis in the transformants expressing the chimera consisting of the G-CSFR extracellular and Fas cytoplasmic regions, but these cells were killed by a polyclonal antibody against G-CSFR. These results indicated that receptors belonging to different receptor families can be functionally exchanged and confirm that a homodimer of G-CSFR can transduce the growth signal, whereas Fas must be oligomerized (probably trimerized) to transduce the apoptotic signal.


Citations per Year

497 Citations

Semantic Scholar estimates that this publication has 497 citations based on the available data.

See our FAQ for additional information.

Cite this paper

@article{Takahashi1996SwappingBF, title={Swapping between Fas and granulocyte colony-stimulating factor receptor.}, author={Toru Takahashi and Masashi Tanaka and Jun-etsu Ogasawara and Tatsuo Suda and Hideyuki Murakami and Shinji Nagata}, journal={The Journal of biological chemistry}, year={1996}, volume={271 29}, pages={17555-60} }