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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 |
1996-8-16
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pubmed:databankReference |
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pubmed:abstractText |
Fas/APO-1 and p55 tumor necrosis factor (TNF) receptor (p55-R) activate cellular mechanisms that result in cell death. Upon activation of these receptors, Fas/APO-1 binds a protein called MORT1 (or FADD) and p55-R binds a protein called TRADD. MORT1 and TRADD can also bind to each other. We have cloned a novel protein, MACH, that binds to MORT1. This protein exists in multiple isoforms, some of which contain a region that has proteolytic activity and shows marked sequence homology to proteases of the ICE/CED-3 family. Cellular expression of the proteolytic MACH isoforms results in cell death. Expression of MACH isoforms that contain an incomplete ICE/CED-3 region provides effective protection against the cytotoxicity induced by Fas/APO-1 or p55-R triggering. These findings suggest that MACH is the most upstream enzymatic component in the Fas/APO-1- and p55-R-induced cell death signaling cascades.
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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, CD,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD95,
http://linkedlifedata.com/resource/pubmed/chemical/Caenorhabditis elegans Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Caspase 1,
http://linkedlifedata.com/resource/pubmed/chemical/Caspases,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/FADD protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Fas-Associated Death Domain Protein,
http://linkedlifedata.com/resource/pubmed/chemical/Helminth Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Tumor Necrosis Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Tumor Necrosis Factor...,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/TNF Receptor-Associated Factor 1,
http://linkedlifedata.com/resource/pubmed/chemical/ced-3 protein, C elegans
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0092-8674
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
14
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pubmed:volume |
85
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
803-15
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8681376-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:8681376-Amino Acid Sequence,
pubmed-meshheading:8681376-Antigens, CD,
pubmed-meshheading:8681376-Antigens, CD95,
pubmed-meshheading:8681376-Apoptosis,
pubmed-meshheading:8681376-Base Sequence,
pubmed-meshheading:8681376-Caenorhabditis elegans Proteins,
pubmed-meshheading:8681376-Carrier Proteins,
pubmed-meshheading:8681376-Caspase 1,
pubmed-meshheading:8681376-Caspases,
pubmed-meshheading:8681376-Cell Line,
pubmed-meshheading:8681376-Cloning, Molecular,
pubmed-meshheading:8681376-Cysteine Endopeptidases,
pubmed-meshheading:8681376-DNA-Binding Proteins,
pubmed-meshheading:8681376-Fas-Associated Death Domain Protein,
pubmed-meshheading:8681376-Helminth Proteins,
pubmed-meshheading:8681376-Humans,
pubmed-meshheading:8681376-Kidney,
pubmed-meshheading:8681376-Molecular Sequence Data,
pubmed-meshheading:8681376-Organ Specificity,
pubmed-meshheading:8681376-Protein Binding,
pubmed-meshheading:8681376-Proteins,
pubmed-meshheading:8681376-RNA, Messenger,
pubmed-meshheading:8681376-Receptors, Tumor Necrosis Factor,
pubmed-meshheading:8681376-Receptors, Tumor Necrosis Factor, Type I,
pubmed-meshheading:8681376-Recombinant Fusion Proteins,
pubmed-meshheading:8681376-Sequence Homology, Amino Acid,
pubmed-meshheading:8681376-Signal Transduction,
pubmed-meshheading:8681376-TNF Receptor-Associated Factor 1
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pubmed:year |
1996
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pubmed:articleTitle |
Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death.
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pubmed:affiliation |
Department of Membrane Research and Biophysics, The Weizmann Institute of Science, Rehovot, Israel.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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