|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
1
|
|
pubmed:dateCreated |
1996-11-7
|
|
pubmed:abstractText |
DNA-dependent protein kinase (DNA-PK) is composed of a 460-kDa catalytic component (p460) and a DNA-binding component Ku protein. Immunoblot analysis after treatment of Jurkat cells with anti-Fas antibody demonstrated the cleavage of p460 concomitantly with an increase in CPP32/Yama/apopain activity. Recombinant CPP32/Yama/apopain specifically cleaved p460 in the DNA-PK preparation that had been purified from Raji cells into 230- and 160-kDa polypeptides, the latter of which was detected in anti-Fas-treated Jurkat cells. The regulatory component Ku protein was not significantly affected by CPP32/Yama/apopain. DNA-PK activity was decreased with the disappearance of p460 in the incubation of DNA-PK with CPP32/Yama/apopain. These results suggest that the catalytic component of DNA-PK is one of the target proteins for CPP32/Yama/apopain in Fas-mediated apoptosis.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/CASP3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Caspase 3,
http://linkedlifedata.com/resource/pubmed/chemical/Caspases,
http://linkedlifedata.com/resource/pubmed/chemical/Coenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Activated Protein Kinase,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/PRKDC protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Sep
|
|
pubmed:issn |
0014-5793
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
9
|
|
pubmed:volume |
393
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
1-6
|
|
pubmed:dateRevised |
2009-11-19
|
|
pubmed:meshHeading |
pubmed-meshheading:8804412-Amino Acid Sequence,
pubmed-meshheading:8804412-Animals,
pubmed-meshheading:8804412-Caspase 3,
pubmed-meshheading:8804412-Caspases,
pubmed-meshheading:8804412-Catalysis,
pubmed-meshheading:8804412-Cattle,
pubmed-meshheading:8804412-Coenzymes,
pubmed-meshheading:8804412-Cysteine Endopeptidases,
pubmed-meshheading:8804412-DNA,
pubmed-meshheading:8804412-DNA-Activated Protein Kinase,
pubmed-meshheading:8804412-DNA-Binding Proteins,
pubmed-meshheading:8804412-Enzyme Precursors,
pubmed-meshheading:8804412-Humans,
pubmed-meshheading:8804412-Molecular Sequence Data,
pubmed-meshheading:8804412-Nuclear Proteins,
pubmed-meshheading:8804412-Protein-Serine-Threonine Kinases,
pubmed-meshheading:8804412-Substrate Specificity,
pubmed-meshheading:8804412-Time Factors,
pubmed-meshheading:8804412-Tumor Cells, Cultured
|
|
pubmed:year |
1996
|
|
pubmed:articleTitle |
CPP32/Yama/apopain cleaves the catalytic component of DNA-dependent protein kinase in the holoenzyme.
|
|
pubmed:affiliation |
Department of Pathological Biochemistry, Tokyo Medical and Dental University, Japan. hteraoka.pbc@mri1.mri.tmd.ac.jp
|
|
pubmed:publicationType |
Journal Article
|
