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Epstein-Barr virus-encoded LMP1 promotes cisplatin-induced caspase activation through JNK and NF-kappaB signaling pathways.
Biochem Biophys Res Commun. 2007 Aug 17; 360(1):263-8.BB

Abstract

Our previous studies have shown that Epstein-Barr virus (EBV)-encoded latent membrane protein 1 (LMP1) potentiates chemotherapeutic agent-induced apoptosis in human cell lines of epithelial origin: cervical carcinoma-derived HeLa cells and nasopharyngeal carcinoma-derived TW03 cells. LMP1 acted upstream of caspase-dependent mitochondrial perturbation, and the effect was mapped to the C-terminal signaling domain of LMP1, designated CTAR2. CTAR2 is known to engage the c-Jun N-terminal kinase (JNK) and NF-kappaB pathways, and we show here that SP600125, a selective JNK inhibitor, suppresses LMP1 potentiation of cisplatin-induced mitochondrial damage and caspase activation in HeLa cells. Moreover, the potentiation of cisplatin-triggered caspase activation was blocked by Bay11-7082, a potent inhibitor of NF-kappaB. Similar results were obtained when a dominant negative form of IkappaB, a specific repressor of NF-kappaB, was co-expressed with LMP1. The current data support the notion that LMP1 modifies stress-induced apoptosis in epithelial cells through molecular interactions downstream of its C-terminal signaling domain.

Authors+Show Affiliations

Department of Microbiology, Tumor and Cell Biology, Box 280, Karolinska Institutet, 171 77 Stockholm, Sweden.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

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

Language

eng

PubMed ID

17586463

Citation

Zhang, Xiangning, et al. "Epstein-Barr Virus-encoded LMP1 Promotes Cisplatin-induced Caspase Activation Through JNK and NF-kappaB Signaling Pathways." Biochemical and Biophysical Research Communications, vol. 360, no. 1, 2007, pp. 263-8.
Zhang X, Sanmun D, Hu L, et al. Epstein-Barr virus-encoded LMP1 promotes cisplatin-induced caspase activation through JNK and NF-kappaB signaling pathways. Biochem Biophys Res Commun. 2007;360(1):263-8.
Zhang, X., Sanmun, D., Hu, L., Fadeel, B., & Ernberg, I. (2007). Epstein-Barr virus-encoded LMP1 promotes cisplatin-induced caspase activation through JNK and NF-kappaB signaling pathways. Biochemical and Biophysical Research Communications, 360(1), 263-8.
Zhang X, et al. Epstein-Barr Virus-encoded LMP1 Promotes Cisplatin-induced Caspase Activation Through JNK and NF-kappaB Signaling Pathways. Biochem Biophys Res Commun. 2007 Aug 17;360(1):263-8. PubMed PMID: 17586463.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Epstein-Barr virus-encoded LMP1 promotes cisplatin-induced caspase activation through JNK and NF-kappaB signaling pathways. AU - Zhang,Xiangning, AU - Sanmun,Duangmanee, AU - Hu,LiFu, AU - Fadeel,Bengt, AU - Ernberg,Ingemar, Y1 - 2007/06/18/ PY - 2007/06/01/received PY - 2007/06/08/accepted PY - 2007/6/26/pubmed PY - 2007/9/6/medline PY - 2007/6/26/entrez SP - 263 EP - 8 JF - Biochemical and biophysical research communications JO - Biochem Biophys Res Commun VL - 360 IS - 1 N2 - Our previous studies have shown that Epstein-Barr virus (EBV)-encoded latent membrane protein 1 (LMP1) potentiates chemotherapeutic agent-induced apoptosis in human cell lines of epithelial origin: cervical carcinoma-derived HeLa cells and nasopharyngeal carcinoma-derived TW03 cells. LMP1 acted upstream of caspase-dependent mitochondrial perturbation, and the effect was mapped to the C-terminal signaling domain of LMP1, designated CTAR2. CTAR2 is known to engage the c-Jun N-terminal kinase (JNK) and NF-kappaB pathways, and we show here that SP600125, a selective JNK inhibitor, suppresses LMP1 potentiation of cisplatin-induced mitochondrial damage and caspase activation in HeLa cells. Moreover, the potentiation of cisplatin-triggered caspase activation was blocked by Bay11-7082, a potent inhibitor of NF-kappaB. Similar results were obtained when a dominant negative form of IkappaB, a specific repressor of NF-kappaB, was co-expressed with LMP1. The current data support the notion that LMP1 modifies stress-induced apoptosis in epithelial cells through molecular interactions downstream of its C-terminal signaling domain. SN - 0006-291X UR - https://www.unboundmedicine.com/medline/citation/17586463/Epstein_Barr_virus_encoded_LMP1_promotes_cisplatin_induced_caspase_activation_through_JNK_and_NF_kappaB_signaling_pathways_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0006-291X(07)01284-3 DB - PRIME DP - Unbound Medicine ER -