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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
Pt 1
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pubmed:dateCreated |
2001-1-26
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pubmed:abstractText |
Proteolytic activation of caspases is a key step in the process of apoptosis. According to their primary structure, caspases can be divided into a group with a long prodomain and a group with a short prodomain. Whereas long prodomains play a role in autocatalytic processing, little is known about the function of the short prodomain, for example the prodomain of caspase-3. We constructed caspase-3 variants lacking the prodomain and overexpressed these in HeLa and yeast cells. We found that removal of the caspase-3 prodomain resulted in spontaneous proteolytic activation of the protein when expressed in HeLa cells. This processing was only partially autocatalytic, as demonstrated by a catalytically inactive caspase-3 mutant. Co-expression of the anti-apoptotic protein XIAP (X-chromosome-linked inhibitor of apoptosis protein) completely blocked the observed spontaneous activation, which excluded a direct involvement of caspase-8. Our findings indicate that the short prodomain of caspase-3 serves as a silencing component in mammalian cells by retaining this executioner caspase in an inactive state.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/10861221-10085063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10861221-10364241,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10861221-7538907,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10861221-7596430,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10861221-7774019,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10861221-7845238,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10861221-8642305,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10861221-8673606,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10861221-8681376,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10861221-8681377,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10861221-8861900,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10861221-8940132,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10861221-9092497,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10861221-9148968,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10861221-9184224,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10861221-9218414,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10861221-9230442,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10861221-9267021,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10861221-9270303,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10861221-9323209,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10861221-9337844,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10861221-9384571,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10861221-9390553,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10861221-9390557,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10861221-9446604,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10861221-9468483,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10861221-9501089,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10861221-9506977,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10861221-9545235,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10861221-9553057,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10861221-9651578,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10861221-9659928,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10861221-9753316,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10861221-9756894,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10861221-9760185,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10861221-9765224,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10861221-9837928,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10861221-9922454,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10861221-9949829
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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/CASP3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/CASP8 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 8,
http://linkedlifedata.com/resource/pubmed/chemical/Caspase 9,
http://linkedlifedata.com/resource/pubmed/chemical/Caspases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Luciferases,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/X-Linked Inhibitor of Apoptosis...,
http://linkedlifedata.com/resource/pubmed/chemical/XIAP protein, human
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0264-6021
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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 |
349
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
135-40
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:10861221-Apoptosis,
pubmed-meshheading:10861221-Blotting, Western,
pubmed-meshheading:10861221-Caspase 3,
pubmed-meshheading:10861221-Caspase 8,
pubmed-meshheading:10861221-Caspase 9,
pubmed-meshheading:10861221-Caspases,
pubmed-meshheading:10861221-Catalysis,
pubmed-meshheading:10861221-Cell Line,
pubmed-meshheading:10861221-DNA, Complementary,
pubmed-meshheading:10861221-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:10861221-Enzyme Activation,
pubmed-meshheading:10861221-HeLa Cells,
pubmed-meshheading:10861221-Humans,
pubmed-meshheading:10861221-Luciferases,
pubmed-meshheading:10861221-Protein Structure, Tertiary,
pubmed-meshheading:10861221-Proteins,
pubmed-meshheading:10861221-Transfection,
pubmed-meshheading:10861221-X-Linked Inhibitor of Apoptosis Protein
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pubmed:year |
2000
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pubmed:articleTitle |
The short prodomain influences caspase-3 activation in HeLa cells.
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pubmed:affiliation |
Biochemical Pharmacology, Faculty of Biology, University of Konstanz, POB 5560-M 668, D 78434 Konstanz, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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