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The NPC derived C15 LMP1 protein confers enhanced activation of NF-kappa B and induction of the EGFR in epithelial cells.
Oncogene. 1998 Apr 09; 16(14):1869-77.O

Abstract

The Epstein-Barr Virus (EBV) LMP1 protein is frequently expressed in nasopharyngeal carcinoma and is essential for the transforming effects of EBV. Analysis of LMP1 genes isolated from tumor biopsies has revealed considerable sequence variation including deletion of amino acids 343-352. Several studies have suggested that this sequence variation could enhance the transforming potential of LMP1. LMP1 has profound effects on cellular gene expression mediated in part through activation of the NF-kappa B transcription factor. In addition, LMP1 engages the TRAF signaling pathway resulting in the induction of EGFR expression. In this study, the LMP1 proteins derived from the laboratory strain B95-8 and the NPC strain C15 were analysed for their ability to activate NF-kappa B and also to induce expression of the EGFR. The data suggest that the C15-LMP1 protein activates NF-kappa B more efficiently and induces higher levels of the EGFR. Analysis of chimeric LMP1 proteins indicates that the amino terminal 181 amino acids of C15-LMP1 confer this increased signaling capability, and that deletion of amino acids 343-352 does not affect these properties. Finally, these data provide evidence that five amino acid changes within the transmembrane domain in the C15-LMP1 protein lead to enhanced NF-kappa B activation and EGFR induction.

Authors+Show Affiliations

Department of Microbiology and Immunology, Lineberger Comprehensive Cancer Center, University of North Carolina School of Medicine, Chapel Hill 27599, USA.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

9583684

Citation

Miller, W E., et al. "The NPC Derived C15 LMP1 Protein Confers Enhanced Activation of NF-kappa B and Induction of the EGFR in Epithelial Cells." Oncogene, vol. 16, no. 14, 1998, pp. 1869-77.
Miller WE, Cheshire JL, Baldwin AS, et al. The NPC derived C15 LMP1 protein confers enhanced activation of NF-kappa B and induction of the EGFR in epithelial cells. Oncogene. 1998;16(14):1869-77.
Miller, W. E., Cheshire, J. L., Baldwin, A. S., & Raab-Traub, N. (1998). The NPC derived C15 LMP1 protein confers enhanced activation of NF-kappa B and induction of the EGFR in epithelial cells. Oncogene, 16(14), 1869-77.
Miller WE, et al. The NPC Derived C15 LMP1 Protein Confers Enhanced Activation of NF-kappa B and Induction of the EGFR in Epithelial Cells. Oncogene. 1998 Apr 9;16(14):1869-77. PubMed PMID: 9583684.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - The NPC derived C15 LMP1 protein confers enhanced activation of NF-kappa B and induction of the EGFR in epithelial cells. AU - Miller,W E, AU - Cheshire,J L, AU - Baldwin,A S,Jr AU - Raab-Traub,N, PY - 1998/5/16/pubmed PY - 2001/3/28/medline PY - 1998/5/16/entrez SP - 1869 EP - 77 JF - Oncogene JO - Oncogene VL - 16 IS - 14 N2 - The Epstein-Barr Virus (EBV) LMP1 protein is frequently expressed in nasopharyngeal carcinoma and is essential for the transforming effects of EBV. Analysis of LMP1 genes isolated from tumor biopsies has revealed considerable sequence variation including deletion of amino acids 343-352. Several studies have suggested that this sequence variation could enhance the transforming potential of LMP1. LMP1 has profound effects on cellular gene expression mediated in part through activation of the NF-kappa B transcription factor. In addition, LMP1 engages the TRAF signaling pathway resulting in the induction of EGFR expression. In this study, the LMP1 proteins derived from the laboratory strain B95-8 and the NPC strain C15 were analysed for their ability to activate NF-kappa B and also to induce expression of the EGFR. The data suggest that the C15-LMP1 protein activates NF-kappa B more efficiently and induces higher levels of the EGFR. Analysis of chimeric LMP1 proteins indicates that the amino terminal 181 amino acids of C15-LMP1 confer this increased signaling capability, and that deletion of amino acids 343-352 does not affect these properties. Finally, these data provide evidence that five amino acid changes within the transmembrane domain in the C15-LMP1 protein lead to enhanced NF-kappa B activation and EGFR induction. SN - 0950-9232 UR - https://www.unboundmedicine.com/medline/citation/9583684/The_NPC_derived_C15_LMP1_protein_confers_enhanced_activation_of_NF_kappa_B_and_induction_of_the_EGFR_in_epithelial_cells_ L2 - https://doi.org/10.1038/sj.onc.1201696 DB - PRIME DP - Unbound Medicine ER -