PuSH - Publication Server of Helmholtz Zentrum München: EBV latent membrane protein-1 protects B cells from apoptosis by inhibition of BAX.

Information

Clues to quality of journals

Open Access Policy of Helmholtz Association 2016

CC Licencences

Publication Metrics

Navigation

Home

Deutsch

EVA: Electronic Publishing

New EVA Application

Research

Advanced Search

Browse by ...

... HMGU-Authors/Consortia

... Organizational Structure

... Journal

... Publication Type

... Research Data

... Arbeitsgruppen

... Publication Year

Publication overview

Statistics

Statistics (last 5 years)

OA Publications

Publish

Submit Publication

Import publication from...

...EVA

Report missing publication

Highlights

Support & Contact

Contact persons

Help

Data protection

Helmholtz Open Science

JANE Journal Estimator

SHERPA/RoMEO

DOAJ

Export:

Text

Endnote (RIS) BIB

BibTeX

Grimm, T. ; Schneider, S. ; Naschberger, E. ; Huber, J.* ; Guenzi, E. ; Kieser, A. ; Reitmeir, P. ; Schulz, T.F.* ; Morris, C.A.* ; Stürzl, M.

EBV latent membrane protein-1 protects B cells from apoptosis by inhibition of BAX.

Blood 105, 3263-3269 (2005)

Publ. Version/Full Text

DOI

	Closed

Open Access Green as soon as Postprint is submitted to ZB.

Abstract
Metrics
Extra information

Latent membrane protein 1 (LMP-1) of Epstein-Barr virus (EBV) promotes tumorigenesis by inhibiting apoptosis. We show that an important antiapoptotic activity of LMP-1 is the inhibition of Bcl2-associated protein X (Bax), a potent proapoptotic protein. BAX expression was regulated by LMP-1 activation of nuclear factor κB (NF-κB) via the C-terminal activation region 1 (CTAR-1) and CTAR-2. Interestingly, p65/p50 inhibited, whereas p50/p50 increased, BAX promoter activity as demonstrated by overexpression and selective inhibition of these NF-κB isoforms. Electrophoretic mobility shift analysis revealed that LMP-1 activates 2 of the 3 NF-κB binding sites (κB1-κB3) in the BAX promoter. LMP-1 induced binding of the NF-κB heterodimer p65/p50 to the κB2 site and of the p50/p50 homodimer to the κB3 site. Promoter mutation analysis revealed that the κB2 site is necessary for inhibition of BAX promoter activity and the κB3 site, for its activation. However, the activation of the BAX promoter by LMP-1 was observed only in the presence of specific inhibitors of p65/p50. In all other cases, LMP-1 inhibited BAX promoter activity. Most importantly, the antiapoptotic activity of LMP-1 was considerably decreased in cells deficient for BAX. These results indicate that the inhibition of Bax may be an important antiapoptotic activity of LMP-1.

Impact Factor

Scopus SNIP

Web of Science
Times Cited

Scopus
Cited By

Altmetric

9.782

0.000