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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
10
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pubmed:dateCreated |
2008-2-28
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pubmed:abstractText |
The BH3-only protein BIK normally induces apoptotic cell death. Here, we have investigated the role of BCL-2 in BIK-induced cell death using Bcl-2+/+ and Bcl-2-/- mouse embryo fibroblasts. Ectopic expression of BIK in Bcl-2-/- cells resulted in enhanced cell death compared to Bcl-2+/+ cells. In these cells, while caspase-8 was activated, there was no significant activation of caspase-9 and 3. There was no detectable mitochondrial to cytosolic release of cytochrome-c. However, there was significant redistribution of AIF from mitochondria to the nucleus. The extent of BIK-induced cell death was augmented by treatment with the pancaspase inhibitor, zVAD-fmk. The Bcl-2 null cells expressing BIK exhibited autophagic features such as cytosolic vacuoles, punctate distribution of LC3 and enhanced expression of Beclin-1. The survival of BIK-expressing Bcl-2-/- cells was enhanced in the presence of PI3 kinase inhibitors 3-methyladenine and Wortmannin and also by depletion of Atg5 and Beclin-1. Death of BIK-expressing Bcl-2-/- cells treated with zVAD-fmk was increased under caspase-8 depletion. Our results suggest enhanced expression of BIK in the Bcl-2 deficient cells leads to cell death with autophagic features and the extent of such cell death could be increased by inhibition of caspases.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/17873911-11060023,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17873911-11175264,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17873911-11326099,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17873911-11410528,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17873911-12067977,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17873911-12815463,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17873911-12952595,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17873911-15010700,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17873911-15068787,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17873911-15131264,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17873911-15205343,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17873911-15558033,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17873911-15592527,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17873911-15661804,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17873911-15680329,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17873911-15809295,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17873911-16007125,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17873911-16060964,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17873911-16148885,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17873911-16179260,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17873911-16247500,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17873911-16322756,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17873911-16547133,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17873911-16702227,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17873911-17064661,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17873911-17141506,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17873911-17194181,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17873911-17244528,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17873911-17337444,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17873911-7478623,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17873911-9305912
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
1476-5594
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
28
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pubmed:volume |
27
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1366-75
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pubmed:dateRevised |
2010-9-14
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pubmed:meshHeading |
pubmed-meshheading:17873911-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:17873911-Animals,
pubmed-meshheading:17873911-Apoptosis,
pubmed-meshheading:17873911-Autophagy,
pubmed-meshheading:17873911-Caspases,
pubmed-meshheading:17873911-Cell Line, Transformed,
pubmed-meshheading:17873911-Cells, Cultured,
pubmed-meshheading:17873911-Genes, bcl-2,
pubmed-meshheading:17873911-Mice,
pubmed-meshheading:17873911-Mitochondrial Proteins,
pubmed-meshheading:17873911-Protein Structure, Tertiary,
pubmed-meshheading:17873911-Proto-Oncogene Proteins c-bcl-2
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pubmed:year |
2008
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pubmed:articleTitle |
BH3-only protein BIK induces caspase-independent cell death with autophagic features in Bcl-2 null cells.
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pubmed:affiliation |
Institute for Molecular Virology, Saint Louis University Health Sciences Center, St Louis, MO 63110, USA.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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