|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
24
|
|
pubmed:dateCreated |
2001-6-11
|
|
pubmed:abstractText |
Mammalian caspases are a family of cysteine proteases that plays a critical role in apoptosis. We have analyzed caspase-2 processing in human cell lines containing defined mutations in caspase-3 and caspase-9. Here we demonstrate that caspase-2 processing, during cell death induced by UV irradiation, depends both on caspase-9 and caspase-3 activity, while, during TNF-alpha-dependent apoptosis, capase-2 processing is independent of caspase-9 but still requires caspase-3. In vitro procaspase-2 is the preferred caspase cleaved by caspase-3, while caspase-7 cleaves procaspase-2 with reduced efficiency. We have also demonstrated that caspase-2-mediated apoptosis requires caspase-9 and that cells co-expressing caspase-2 and a dominant negative form of caspase-9 are impaired in activating a normal apoptotic response and release cytochrome c into the cytoplasm. Our findings suggest a role played by caspase-2 as a regulator of the mitochondrial integrity and open questions on the mechanisms responsible for its activation during cell death.
|
|
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/CASP7 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/CASP9 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Caspase 2,
http://linkedlifedata.com/resource/pubmed/chemical/Caspase 3,
http://linkedlifedata.com/resource/pubmed/chemical/Caspase 7,
http://linkedlifedata.com/resource/pubmed/chemical/Caspase 9,
http://linkedlifedata.com/resource/pubmed/chemical/Caspases,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Necrosis Factor-alpha
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Jun
|
|
pubmed:issn |
0021-9258
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
15
|
|
pubmed:volume |
276
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
21907-15
|
|
pubmed:dateRevised |
2006-11-15
|
|
pubmed:meshHeading |
pubmed-meshheading:11399776-Amino Acid Substitution,
pubmed-meshheading:11399776-Animals,
pubmed-meshheading:11399776-Apoptosis,
pubmed-meshheading:11399776-Caspase 2,
pubmed-meshheading:11399776-Caspase 3,
pubmed-meshheading:11399776-Caspase 7,
pubmed-meshheading:11399776-Caspase 9,
pubmed-meshheading:11399776-Caspases,
pubmed-meshheading:11399776-Cell Death,
pubmed-meshheading:11399776-Cell Line,
pubmed-meshheading:11399776-Female,
pubmed-meshheading:11399776-Fibroblasts,
pubmed-meshheading:11399776-Fluorescent Antibody Technique, Indirect,
pubmed-meshheading:11399776-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:11399776-Gene Library,
pubmed-meshheading:11399776-Humans,
pubmed-meshheading:11399776-Mammals,
pubmed-meshheading:11399776-Mutagenesis, Site-Directed,
pubmed-meshheading:11399776-Recombinant Proteins,
pubmed-meshheading:11399776-Transfection,
pubmed-meshheading:11399776-Tumor Necrosis Factor-alpha,
pubmed-meshheading:11399776-Ultraviolet Rays
|
|
pubmed:year |
2001
|
|
pubmed:articleTitle |
Caspase-2-induced apoptosis is dependent on caspase-9, but its processing during UV- or tumor necrosis factor-dependent cell death requires caspase-3.
|
|
pubmed:affiliation |
Dipartimento di Scienze e Tecnologie Biomediche, Sezione di Biologia, Universita' di Udine, P. le Kolbe 4, Udine 33100, Italy.
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
