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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
2001-3-28
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pubmed:abstractText |
Cell death is achieved by two fundamentally different mechanisms: apoptosis and necrosis. Apoptosis is dependent on caspase activation, whereas the caspase-independent necrotic signaling pathway remains largely uncharacterized. We show here that Fas kills activated primary T cells efficiently in the absence of active caspases, which results in necrotic morphological changes and late mitochondrial damage but no cytochrome c release. This Fas ligand-induced caspase-independent death is absent in T cells that are deficient in either Fas-associated death domain (FADD) or receptor-interacting protein (RIP). RIP is also required for necrotic death induced by tumor necrosis factor (TNF) and TNF-related apoptosis-inducing ligand (TRAIL). In contrast to its role in nuclear factor kappa B activation, RIP requires its own kinase activity for death signaling. Thus, Fas, TRAIL and TNF receptors can initiate cell death by two alternative pathways, one relying on caspase-8 and the other dependent on the kinase RIP.
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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/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD95,
http://linkedlifedata.com/resource/pubmed/chemical/Apoptosis Regulatory Proteins,
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/Casp8 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Casp9 protein, mouse,
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/FADD protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/FASLG protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Fadd protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Fas Ligand Protein,
http://linkedlifedata.com/resource/pubmed/chemical/Fas-Associated Death Domain Protein,
http://linkedlifedata.com/resource/pubmed/chemical/Fasl protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RIPK1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor-Interacting Protein...,
http://linkedlifedata.com/resource/pubmed/chemical/Ripk1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/TNF-Related Apoptosis-Inducing...,
http://linkedlifedata.com/resource/pubmed/chemical/TNFSF10 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Tnfsf10 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Necrosis Factor-alpha
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
1529-2908
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
1
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
489-95
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:11101870-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:11101870-Animals,
pubmed-meshheading:11101870-Antigens, CD95,
pubmed-meshheading:11101870-Apoptosis,
pubmed-meshheading:11101870-Apoptosis Regulatory Proteins,
pubmed-meshheading:11101870-Carrier Proteins,
pubmed-meshheading:11101870-Caspase 8,
pubmed-meshheading:11101870-Caspase 9,
pubmed-meshheading:11101870-Caspases,
pubmed-meshheading:11101870-Cell Death,
pubmed-meshheading:11101870-Fas Ligand Protein,
pubmed-meshheading:11101870-Fas-Associated Death Domain Protein,
pubmed-meshheading:11101870-Humans,
pubmed-meshheading:11101870-Jurkat Cells,
pubmed-meshheading:11101870-Membrane Glycoproteins,
pubmed-meshheading:11101870-Mice,
pubmed-meshheading:11101870-Mice, Inbred BALB C,
pubmed-meshheading:11101870-Models, Biological,
pubmed-meshheading:11101870-Necrosis,
pubmed-meshheading:11101870-Proteins,
pubmed-meshheading:11101870-Receptor-Interacting Protein Serine-Threonine Kinases,
pubmed-meshheading:11101870-Signal Transduction,
pubmed-meshheading:11101870-T-Lymphocytes,
pubmed-meshheading:11101870-TNF-Related Apoptosis-Inducing Ligand,
pubmed-meshheading:11101870-Tumor Necrosis Factor-alpha
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pubmed:year |
2000
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pubmed:articleTitle |
Fas triggers an alternative, caspase-8-independent cell death pathway using the kinase RIP as effector molecule.
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pubmed:affiliation |
Institute of Biochemistry, University of Lausanne, BIL Biomedical Research Center, Chemin des Boveresses 155, CH-1066 Epalinges, Switzerland.
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pubmed:publicationType |
Journal Article,
In Vitro
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