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B Activation, and c-Jun Kinase Activation1
Cytokine Research Section, Department of Molecular Oncology, University of Texas M. D. Anderson Cancer Center, Houston, TX 77030; and * Roche Biosciences, Palo Alto, CA 94304
Because they have distinct intracellular domains, it has been
proposed that the p60 and p80 forms of the TNF receptor mediate
different signals. Several signaling proteins have been isolated that
associate with either the p60 or the p80 receptor. By using TNF muteins
specific to the p60 and p80 receptors, we have previously shown that
cytotoxicity and nuclear factor-
B (NF-B) activation are mediated
through the p60 form of the endogenous receptor. What signals are
mediated through the p80 receptor is less clear. This study was an
effort to answer that question. HeLa cells, which express only p60
receptors, were transfected with p80 receptor cDNA and then examined
for apoptosis, NF-B activation, and c-Jun kinase activation induced
by TNF and by p60 or p80 receptor-specific muteins. The p80 mutein,
like TNF and the p60 mutein, induced apoptosis and activation of
NF-B and c-Jun kinase in cells overexpressing recombinant p80
receptor but had no effect on cells expressing a high level of
endogenous p80 receptor. The apoptosis mediated through the p60
receptor was also potentiated after overexpression of the p80 receptor,
suggesting a synergistic relationship between the two receptors.
Interestingly, Abs to the p80 receptor blocked apoptosis induced by all
ligands but by itself activated NF-B in the p80-transfected cells.
Overall, our results show that the p80 receptor, which lacks the death
domain, mediated apoptosis, NF-B activation, and c-Jun kinase
activation, but only when it was overexpressed, whereas endogenous p60
receptor mediated similar signals without overexpression.
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