Induction of cell death by myristylated death domain of p55 TNF receptor is not abolished by lpr(cg)-like point mutation in death domain

C. H. Kim, Y. H. Song, K. Park, Y. Oh, T. H. Lee

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

We transiently expressed the intracellular domains of p55 TNF receptor (TNFR1) as either a cytosolic- or a membrane-associated form and examined their effects on the endogenous receptor-mediated gene expression as well as on cell viability. We found that gene expression as measured by luciferase activity under NF-κB-controlling elements was blocked by all forms of the intracellular domain of TNFR1. The blockade of reporter gene expression was due to the cell death induced by the intracellular domain of TNFR1 per se. The killing mechanism of the intracellular domain peptides appeared to be apoptotic. Interestingly, myristylated form of the intracellular domain, consisting of mainly death domain showed the most potent cell-killing activity. Moreover, this myristylated death domain could still induce cell death even if lpr(cg)-like point mutation (Leu351 to Ala), which has been reported to abrogate TNF-induced cytotoxicity, was introduced. This result suggests that the myristylated death domain activates an additional death signaling pathway which is not involved in TNF-induced cell death.

Original languageEnglish
Pages (from-to)312-322
Number of pages11
JournalJournal of Inflammation
Volume45
Issue number4
Publication statusPublished - 1995

All Science Journal Classification (ASJC) codes

  • Cardiology and Cardiovascular Medicine

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