Swapping between Fas and granulocyte colony-stimulating factor receptor

Tomohiro Takahashi, Masato Tanaka, Jun Ogasawara, Takashi Suda, Hiroshi Murakami, Shigekazu Nagata

Research output: Contribution to journalArticle

26 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)17555-17560
Number of pages6
JournalJournal of Biological Chemistry
Volume271
Issue number29
DOIs
Publication statusPublished - 1996
Externally publishedYes

Fingerprint

Granulocyte Colony-Stimulating Factor Receptors
CD95 Antigens
Fas Ligand Protein
Granulocyte Colony-Stimulating Factor
Bearings (structural)
Apoptosis
Nerve Growth Factor Receptor
Cell Line
T-cells
Growth Factor Receptors
Dimerization
Antibodies
Interleukin-3
Granulocytes
Anti-Idiotypic Antibodies
Tumor Necrosis Factor-alpha
Cells
T-Lymphocytes
Growth

ASJC Scopus subject areas

  • Biochemistry

Cite this

Swapping between Fas and granulocyte colony-stimulating factor receptor. / Takahashi, Tomohiro; Tanaka, Masato; Ogasawara, Jun; Suda, Takashi; Murakami, Hiroshi; Nagata, Shigekazu.

In: Journal of Biological Chemistry, Vol. 271, No. 29, 1996, p. 17555-17560.

Research output: Contribution to journalArticle

Takahashi, T, Tanaka, M, Ogasawara, J, Suda, T, Murakami, H & Nagata, S 1996, 'Swapping between Fas and granulocyte colony-stimulating factor receptor', Journal of Biological Chemistry, vol. 271, no. 29, pp. 17555-17560. https://doi.org/10.1074/jbc.271.29.17555
Takahashi, Tomohiro ; Tanaka, Masato ; Ogasawara, Jun ; Suda, Takashi ; Murakami, Hiroshi ; Nagata, Shigekazu. / Swapping between Fas and granulocyte colony-stimulating factor receptor. In: Journal of Biological Chemistry. 1996 ; Vol. 271, No. 29. pp. 17555-17560.
@article{9b4962c3ab2c47fc95bafc8767a29d80,
title = "Swapping between Fas and granulocyte colony-stimulating factor receptor",
abstract = "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.",
author = "Tomohiro Takahashi and Masato Tanaka and Jun Ogasawara and Takashi Suda and Hiroshi Murakami and Shigekazu Nagata",
year = "1996",
doi = "10.1074/jbc.271.29.17555",
language = "English",
volume = "271",
pages = "17555--17560",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "29",

}

TY - JOUR

T1 - Swapping between Fas and granulocyte colony-stimulating factor receptor

AU - Takahashi, Tomohiro

AU - Tanaka, Masato

AU - Ogasawara, Jun

AU - Suda, Takashi

AU - Murakami, Hiroshi

AU - Nagata, Shigekazu

PY - 1996

Y1 - 1996

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0030056050&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0030056050&partnerID=8YFLogxK

U2 - 10.1074/jbc.271.29.17555

DO - 10.1074/jbc.271.29.17555

M3 - Article

C2 - 8663376

AN - SCOPUS:0030056050

VL - 271

SP - 17555

EP - 17560

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 29

ER -