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Overexpression of the p80 TNF receptor leads to TNF-dependent apoptosis, nuclear factor-kappa B activation, and c-Jun kinase activation.
J Immunol. 1998 Apr 01; 160(7):3152-62.JI

Abstract

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-kappa B (NF-kappa 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-kappa 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-kappa 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-kappa B in the p80-transfected cells. Overall, our results show that the p80 receptor, which lacks the death domain, mediated apoptosis, NF-kappa B activation, and c-Jun kinase activation, but only when it was overexpressed, whereas endogenous p60 receptor mediated similar signals without overexpression.

Authors+Show Affiliations

Department of Molecular Oncology, University of Texas M. D. Anderson Cancer Center, Houston 77030, USA.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Comparative Study
Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

9531270

Citation

Haridas, V, et al. "Overexpression of the P80 TNF Receptor Leads to TNF-dependent Apoptosis, Nuclear Factor-kappa B Activation, and c-Jun Kinase Activation." Journal of Immunology (Baltimore, Md. : 1950), vol. 160, no. 7, 1998, pp. 3152-62.
Haridas V, Darnay BG, Natarajan K, et al. Overexpression of the p80 TNF receptor leads to TNF-dependent apoptosis, nuclear factor-kappa B activation, and c-Jun kinase activation. J Immunol. 1998;160(7):3152-62.
Haridas, V., Darnay, B. G., Natarajan, K., Heller, R., & Aggarwal, B. B. (1998). Overexpression of the p80 TNF receptor leads to TNF-dependent apoptosis, nuclear factor-kappa B activation, and c-Jun kinase activation. Journal of Immunology (Baltimore, Md. : 1950), 160(7), 3152-62.
Haridas V, et al. Overexpression of the P80 TNF Receptor Leads to TNF-dependent Apoptosis, Nuclear Factor-kappa B Activation, and c-Jun Kinase Activation. J Immunol. 1998 Apr 1;160(7):3152-62. PubMed PMID: 9531270.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Overexpression of the p80 TNF receptor leads to TNF-dependent apoptosis, nuclear factor-kappa B activation, and c-Jun kinase activation. AU - Haridas,V, AU - Darnay,B G, AU - Natarajan,K, AU - Heller,R, AU - Aggarwal,B B, PY - 1998/4/8/pubmed PY - 1998/4/8/medline PY - 1998/4/8/entrez SP - 3152 EP - 62 JF - Journal of immunology (Baltimore, Md. : 1950) JO - J Immunol VL - 160 IS - 7 N2 - 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-kappa B (NF-kappa 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-kappa 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-kappa 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-kappa B in the p80-transfected cells. Overall, our results show that the p80 receptor, which lacks the death domain, mediated apoptosis, NF-kappa B activation, and c-Jun kinase activation, but only when it was overexpressed, whereas endogenous p60 receptor mediated similar signals without overexpression. SN - 0022-1767 UR - https://www.unboundmedicine.com/medline/citation/9531270/Overexpression_of_the_p80_TNF_receptor_leads_to_TNF_dependent_apoptosis_nuclear_factor_kappa_B_activation_and_c_Jun_kinase_activation_ L2 - http://www.jimmunol.org/cgi/pmidlookup?view=long&pmid=9531270 DB - PRIME DP - Unbound Medicine ER -