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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2004-11-15
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pubmed:abstractText |
Serum withdrawal represents a potent trigger to induce caspase-dependent apoptosis in a series of cell culture models. In rat 423-cells, caspase-8 and caspase-3 were apparently sufficient to initiate and proceed apoptosis without involving the intrinsic amplification loop via caspase-9. To assess the reasons for this inactivity of an otherwise crucial initiator caspase, we examined the ability for apoptosome assembly in 423-cells. Caspase-9 and Apaf-1 were expressed and cytochrome c released from mitochondria upon serum withdrawal. Although functional apoptosomes were assembled successfully in vitro, caspase-9 processing was found essentially refrained during apoptosis in 423-cells. Cell fractionation experiments revealed that sequestration of caspase-9 to cytoskeletal structures in 423-cells contributed to the observed impairment of apoptosome formation. Altogether, these findings provide evidence that serum starvation-induced apoptosis may occur independently of the intrinsic pathway and that caspase-9 sequestration potentially represents a novel biological antiapoptotic strategy.
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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/APAF1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Apaf1 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Apoptotic Protease-Activating...,
http://linkedlifedata.com/resource/pubmed/chemical/Blood Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/CASP9 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Casp9 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Caspase 9,
http://linkedlifedata.com/resource/pubmed/chemical/Caspases,
http://linkedlifedata.com/resource/pubmed/chemical/Culture Media, Serum-Free,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochromes c,
http://linkedlifedata.com/resource/pubmed/chemical/Growth Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Keratins,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0014-4827
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
302
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
115-28
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:15541731-Animals,
pubmed-meshheading:15541731-Apoptosis,
pubmed-meshheading:15541731-Apoptotic Protease-Activating Factor 1,
pubmed-meshheading:15541731-Blood Proteins,
pubmed-meshheading:15541731-Caspase 9,
pubmed-meshheading:15541731-Caspases,
pubmed-meshheading:15541731-Cell Line,
pubmed-meshheading:15541731-Culture Media, Serum-Free,
pubmed-meshheading:15541731-Cytochromes c,
pubmed-meshheading:15541731-Cytoskeleton,
pubmed-meshheading:15541731-Growth Substances,
pubmed-meshheading:15541731-HeLa Cells,
pubmed-meshheading:15541731-Humans,
pubmed-meshheading:15541731-Inclusion Bodies,
pubmed-meshheading:15541731-Keratins,
pubmed-meshheading:15541731-Mitochondria,
pubmed-meshheading:15541731-Proteins,
pubmed-meshheading:15541731-Rats,
pubmed-meshheading:15541731-Signal Transduction
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pubmed:year |
2005
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pubmed:articleTitle |
Caspase-9 plays a marginal role in serum starvation-induced apoptosis.
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pubmed:affiliation |
Institute of Cancer Research, Medical University of Vienna, 1090 Vienna, Austria. chantal.schamberger@meduniwien.ac.at
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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