|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
4
|
|
pubmed:dateCreated |
1997-12-23
|
|
pubmed:abstractText |
We report here the purification of the third protein factor, Apaf-3, that participates in caspase-3 activation in vitro. Apaf-3 was identified as a member of the caspase family, caspase-9. Caspase-9 and Apaf-1 bind to each other via their respective NH2-terminal CED-3 homologous domains in the presence of cytochrome c and dATP, an event that leads to caspase-9 activation. Activated caspase-9 in turn cleaves and activates caspase-3. Depletion of caspase-9 from S-100 extracts diminished caspase-3 activation. Mutation of the active site of caspase-9 attenuated the activation of caspase-3 and cellular apoptotic response in vivo, indicating that caspase-9 is the most upstream member of the apoptotic protease cascade that is triggered by cytochrome c and dATP.
|
|
pubmed:grant |
|
|
pubmed:commentsCorrections |
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/2'-deoxyadenosine triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/APAF1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Apoptotic Protease-Activating...,
http://linkedlifedata.com/resource/pubmed/chemical/CASP3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/CASP9 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Caspase 3,
http://linkedlifedata.com/resource/pubmed/chemical/Caspase 9,
http://linkedlifedata.com/resource/pubmed/chemical/Caspases,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome c Group,
http://linkedlifedata.com/resource/pubmed/chemical/Deoxyadenine Nucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Nov
|
|
pubmed:issn |
0092-8674
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
14
|
|
pubmed:volume |
91
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
479-89
|
|
pubmed:dateRevised |
2007-11-14
|
|
pubmed:meshHeading |
pubmed-meshheading:9390557-Amino Acid Sequence,
pubmed-meshheading:9390557-Apoptosis,
pubmed-meshheading:9390557-Apoptotic Protease-Activating Factor 1,
pubmed-meshheading:9390557-Binding Sites,
pubmed-meshheading:9390557-Breast Neoplasms,
pubmed-meshheading:9390557-Caspase 3,
pubmed-meshheading:9390557-Caspase 9,
pubmed-meshheading:9390557-Caspases,
pubmed-meshheading:9390557-Cell Line,
pubmed-meshheading:9390557-Cysteine Endopeptidases,
pubmed-meshheading:9390557-Cytochrome c Group,
pubmed-meshheading:9390557-Deoxyadenine Nucleotides,
pubmed-meshheading:9390557-Enzyme Activation,
pubmed-meshheading:9390557-Epithelial Cells,
pubmed-meshheading:9390557-HeLa Cells,
pubmed-meshheading:9390557-Humans,
pubmed-meshheading:9390557-Kidney,
pubmed-meshheading:9390557-Models, Chemical,
pubmed-meshheading:9390557-Molecular Sequence Data,
pubmed-meshheading:9390557-Multienzyme Complexes,
pubmed-meshheading:9390557-Mutation,
pubmed-meshheading:9390557-Protein Binding,
pubmed-meshheading:9390557-Proteins,
pubmed-meshheading:9390557-Tumor Cells, Cultured
|
|
pubmed:year |
1997
|
|
pubmed:articleTitle |
Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade.
|
|
pubmed:affiliation |
Howard Hughes Medical Institute, and Department of Biochemistry, University of Texas Southwestern Medical Center at Dallas, 75235, USA.
|
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|
