Source:http://linkedlifedata.com/resource/pubmed/id/10381630
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
1999-7-14
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pubmed:abstractText |
The inhibitor-of-apoptosis (IAP) proteins are a novel family of antiapoptotic proteins that are thought to inhibit cell death via direct inhibition of caspases. Here, we report that human malignant glioma cell lines express XIAP, HIAP-1 and HIAP-2 mRNA and proteins. NAIP was not expressed. IAP proteins were not cleaved during CD95 ligand (CD95L)-induced apoptosis, and loss of IAP protein expression was not responsible for the potentiation of CD95L-induced apoptosis when protein synthesis was inhibited. LN-18 cells are highly sensitive to CD95-mediated apoptosis, whereas LN-229 cells require co-exposure to CD95L and a protein synthesis inhibitor, CHX, to acquire sensitivity to apoptosis. Adenoviral XIAP gene transfer blocked caspase 8 and 3 processing in both cell lines in the absence of CHX. Apoptosis was blocked in the absence and in the presence of CHX. However, XIAP failed to block caspase 8 processing in LN-229 cells in the presence of CHX. There was considerable overlap of the effects of XIAP on caspase processing with those of BCL-2 and the viral caspase inhibitor crm-A. These data define complex regulatory mechanisms for CD95-mediated apoptosis in glioma cells and indicate that there may be a distinct pathway of death receptor-mediated apoptosis that is readily activated when protein synthesis is inhibited. The constitutive expression of natural caspase inhibitors may play a role in the resistance of these cells to apoptotic stimuli that directly target caspases, including radiochemotherapy and immune-mediated tumor cell lysis.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD95,
http://linkedlifedata.com/resource/pubmed/chemical/Antisense Elements (Genetics),
http://linkedlifedata.com/resource/pubmed/chemical/Caspases,
http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/X-Linked Inhibitor of Apoptosis...,
http://linkedlifedata.com/resource/pubmed/chemical/XIAP protein, human
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
1350-9047
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pubmed:author | |
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 |
370-6
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pubmed:dateRevised |
2008-5-14
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pubmed:meshHeading |
pubmed-meshheading:10381630-Adenoviridae,
pubmed-meshheading:10381630-Antigens, CD95,
pubmed-meshheading:10381630-Antisense Elements (Genetics),
pubmed-meshheading:10381630-Apoptosis,
pubmed-meshheading:10381630-Brain Neoplasms,
pubmed-meshheading:10381630-Caspases,
pubmed-meshheading:10381630-Gene Expression Regulation, Neoplastic,
pubmed-meshheading:10381630-Gene Transfer Techniques,
pubmed-meshheading:10381630-Glioma,
pubmed-meshheading:10381630-Humans,
pubmed-meshheading:10381630-Neoplasm Proteins,
pubmed-meshheading:10381630-Proteins,
pubmed-meshheading:10381630-Tumor Cells, Cultured,
pubmed-meshheading:10381630-X-Linked Inhibitor of Apoptosis Protein
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pubmed:year |
1999
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pubmed:articleTitle |
Expression and biological activity of X-linked inhibitor of apoptosis (XIAP) in human malignant glioma.
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pubmed:affiliation |
Laboratory of Molecular Neuro-Oncology, Hoppe-Seyler-Strasse 3, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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