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Volume 270, Number 29, Issue of July 21, pp. 17482-17487, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.

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Cross-linking of the p55 Tumor Necrosis Factor Receptor Cytoplasmic Domain by a Dimeric Ligand Induces Nuclear Factor-B and Mediates Cell Death

(Received for publication, March 3, 1995)

Dieter Adam , Ulrike Keler , Martin Krönke

From the Institut für Medizinische Mikrobiologie und Hygiene, Technische Universität München, Trogerstrasse 32, 81675 München, Germany

We have fused the cytoplasmic domain of the p55 tumor necrosis factor (TNF) receptor to the extracellular and transmembrane domain of the mouse platelet-derived growth factor (PDGF) receptor. Mouse mammary gland epithelial (NMuMG) cells were stably transfected with the PDGFR-TR55 chimeric receptor. These cells lack endogenous PDGF receptor expression and do not respond to PDGF. In the PDGFR-TR55 transfectants, PDGF elicited a cytotoxic response, which is indistinguishable from that induced by the wild type p55 TNF receptor. In addition, PDGF-induced activation of the PDGFR-TR55 chimeric receptor resulted in nuclear translocation of NF-B. The data presented suggest that cross-linking of the p55 TNF receptor cytoplasmic domain by a dimeric ligand such as PDGF is sufficient to generate cellular responses that do not differ from those observed with the trimeric ligand TNF.

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