Source:http://linkedlifedata.com/resource/pubmed/id/10203698
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
10
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| pubmed:dateCreated |
1999-5-6
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| pubmed:abstractText |
Caspases are cysteinyl aspartate-specific proteinases, many of which play a central role in apoptosis. Here, we report the identification of a new murine caspase homologue, viz. caspase-14. It is most related to human/murine caspase-2 and human caspase-9, possesses all the typical amino acid residues of the caspases involved in catalysis, including the QACRG box, and contains no or only a very short prodomain. Murine caspase-14 shows 83% similarity to human caspase-14. Human caspase-14 is assigned to chromosome 19p13.1. Northern blot analysis revealed that mRNA expression of caspase-14 is undetectable in all mouse adult tissues examined except for skin, while it is abundantly expressed in mouse embryos. In contrast to many other caspase family members, murine caspase-14 is not cleaved by granzyme B, caspase-1, caspase-2, caspase-3, caspase-6, caspase-7 or caspase-11, but is weakly processed into p18 and p11 subunits by murine caspase-8. No aspartase activity of murine caspase-14 could be generated by bacterial or yeast expression. Transient overexpression of murine caspase-14 in mammalian cells did not elicit cell death and did not interfere with caspase-8-induced apoptosis. In conclusion, caspase-14 is a member of the caspase family but no proteolytic or biological activities have been identified so far. The high constitutive expression levels in embryos and specific expression in adult skin suggest a role in ontogenesis and skin physiology.
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| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/CASP14 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Casp14 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Caspase 1,
http://linkedlifedata.com/resource/pubmed/chemical/Caspase 14,
http://linkedlifedata.com/resource/pubmed/chemical/Caspases,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
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| pubmed:status |
MEDLINE
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| pubmed:month |
Oct
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| pubmed:issn |
1350-9047
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
5
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
838-46
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:10203698-Amino Acid Sequence,
pubmed-meshheading:10203698-Animals,
pubmed-meshheading:10203698-Caspase 1,
pubmed-meshheading:10203698-Caspase 14,
pubmed-meshheading:10203698-Caspases,
pubmed-meshheading:10203698-Cell Line,
pubmed-meshheading:10203698-Cloning, Molecular,
pubmed-meshheading:10203698-HeLa Cells,
pubmed-meshheading:10203698-Humans,
pubmed-meshheading:10203698-Male,
pubmed-meshheading:10203698-Mice,
pubmed-meshheading:10203698-Molecular Sequence Data,
pubmed-meshheading:10203698-Organ Specificity,
pubmed-meshheading:10203698-Recombinant Proteins,
pubmed-meshheading:10203698-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:10203698-Sequence Alignment,
pubmed-meshheading:10203698-Sequence Homology, Amino Acid,
pubmed-meshheading:10203698-Transcription, Genetic,
pubmed-meshheading:10203698-Transfection
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| pubmed:year |
1998
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| pubmed:articleTitle |
Identification of a new caspase homologue: caspase-14.
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| pubmed:affiliation |
Department of Molecular Biology, Flanders Interuniversity Institute for Biotechnology and University of Ghent, Ghent, Belgium.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|