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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6662
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pubmed:dateCreated |
1998-1-15
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pubmed:databankReference |
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pubmed:abstractText |
The homeostasis of animals is regulated not only by the growth and differentiation of cells, but also by cell death through a process known as apoptosis. Apoptosis is mediated by members of the caspase family of proteases, and eventually causes the degradation of chromosomal DNA. A caspase-activated deoxyribonuclease (CAD) and its inhibitor (ICAD) have now been identified in the cytoplasmic fraction of mouse lymphoma cells. CAD is a protein of 343 amino acids which carries a nuclear-localization signal; ICAD exists in a long and a short form. Recombinant ICAD specifically inhibits CAD-induced degradation of nuclear DNA and its DNase activity. When CAD is expressed with ICAD in COS cells or in a cell-free system, CAD is produced as a complex with ICAD: treatment with caspase 3 releases the DNase activity which causes DNA fragmentation in nuclei. ICAD therefore seems to function as a chaperone for CAD during its synthesis, remaining complexed with CAD to inhibit its DNase activity; caspases activated by apoptotic stimuli then cleave ICAD, allowing CAD to enter the nucleus and degrade chromosomal DNA.
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pubmed:commentsCorrections |
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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/Apoptosis Regulatory Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/CASP3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Casp3 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Caspase 3,
http://linkedlifedata.com/resource/pubmed/chemical/Caspases,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/DNA fragmentation factor, human,
http://linkedlifedata.com/resource/pubmed/chemical/Deoxyribonucleases,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/caspase-activated DNase inhibitor,
http://linkedlifedata.com/resource/pubmed/chemical/caspase-activated deoxyribonuclease
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0028-0836
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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 |
391
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
43-50
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9422506-Amino Acid Sequence,
pubmed-meshheading:9422506-Animals,
pubmed-meshheading:9422506-Apoptosis,
pubmed-meshheading:9422506-Apoptosis Regulatory Proteins,
pubmed-meshheading:9422506-COS Cells,
pubmed-meshheading:9422506-Caspase 3,
pubmed-meshheading:9422506-Caspases,
pubmed-meshheading:9422506-Cloning, Molecular,
pubmed-meshheading:9422506-Cysteine Endopeptidases,
pubmed-meshheading:9422506-DNA,
pubmed-meshheading:9422506-Deoxyribonucleases,
pubmed-meshheading:9422506-Enzyme Activation,
pubmed-meshheading:9422506-Enzyme Inhibitors,
pubmed-meshheading:9422506-Escherichia coli,
pubmed-meshheading:9422506-Humans,
pubmed-meshheading:9422506-Mice,
pubmed-meshheading:9422506-Molecular Sequence Data,
pubmed-meshheading:9422506-Proteins,
pubmed-meshheading:9422506-Recombinant Fusion Proteins,
pubmed-meshheading:9422506-Sequence Homology, Amino Acid,
pubmed-meshheading:9422506-Tumor Cells, Cultured
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pubmed:year |
1998
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pubmed:articleTitle |
A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD.
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pubmed:affiliation |
Department of Genetics, Osaka University Medical School, Suita, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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