rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2000-8-31
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pubmed:abstractText |
The adenovirus E1B 19K gene product is an inhibitor of apoptosis induced by tumor necrosis factor-alpha (TNF-alpha) during viral infection. We report that E1B 19K inhibited neither caspase-8 activation nor caspase-8-dependent Bid cleavage by TNF-alpha. Rather, TNF-alpha induced a tBid-dependent conformational change in Bax that allowed an interaction between E1B 19K and conformationally altered Bax, which caused inhibition of cytochrome c release and caspase-9 activation. E1B 19K expression interrupted caspase-3 processing, permitting cleavage to remove the p12 subunit but not the prodomain consistent with caspase-8 and not caspase-9 enzymatic activity. Thus, E1B 19K blocks TNF-alpha-mediated death signaling by inhibiting a specific form of Bax that interrupts caspase activation downstream of caspase-8 and upstream of caspase-9.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenovirus E1B Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/BAX protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/BH3 Interacting Domain Death...,
http://linkedlifedata.com/resource/pubmed/chemical/BID protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/CASP3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/CASP8 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/CASP9 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Caspase 3,
http://linkedlifedata.com/resource/pubmed/chemical/Caspase 8,
http://linkedlifedata.com/resource/pubmed/chemical/Caspase 9,
http://linkedlifedata.com/resource/pubmed/chemical/Caspases,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome c Group,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-bcl-2,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Necrosis Factor-alpha,
http://linkedlifedata.com/resource/pubmed/chemical/bcl-2-Associated X Protein
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
1097-2765
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
6
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
53-63
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:10949027-Adenovirus E1B Proteins,
pubmed-meshheading:10949027-Apoptosis,
pubmed-meshheading:10949027-BH3 Interacting Domain Death Agonist Protein,
pubmed-meshheading:10949027-Carrier Proteins,
pubmed-meshheading:10949027-Caspase 3,
pubmed-meshheading:10949027-Caspase 8,
pubmed-meshheading:10949027-Caspase 9,
pubmed-meshheading:10949027-Caspases,
pubmed-meshheading:10949027-Cytochrome c Group,
pubmed-meshheading:10949027-Enzyme Activation,
pubmed-meshheading:10949027-Enzyme Precursors,
pubmed-meshheading:10949027-HeLa Cells,
pubmed-meshheading:10949027-Humans,
pubmed-meshheading:10949027-Protein Conformation,
pubmed-meshheading:10949027-Proto-Oncogene Proteins,
pubmed-meshheading:10949027-Proto-Oncogene Proteins c-bcl-2,
pubmed-meshheading:10949027-Signal Transduction,
pubmed-meshheading:10949027-Transfection,
pubmed-meshheading:10949027-Tumor Necrosis Factor-alpha,
pubmed-meshheading:10949027-bcl-2-Associated X Protein
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pubmed:year |
2000
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pubmed:articleTitle |
TNF-alpha signals apoptosis through a bid-dependent conformational change in Bax that is inhibited by E1B 19K.
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pubmed:affiliation |
Howard Hughes Medical Institute, Rutgers University, Piscataway, New Jersey 08854, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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