Linked Life Data

15301553

Source:http://linkedlifedata.com/resource/pubmed/id/15301553

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
32
pubmed:dateCreated
2004-8-10
pubmed:abstractText
Caspase-14 is a developmentally regulated and tissue restricted member of the caspase family present in mammals. It is mainly found in epidermal keratinocytes and has been hypothesized to be involved in a tissue-specific form of cell senescence, leading to the differentiation of keratinocytes that form the cornified cell layer. However, the substrate specificity, activation mechanism, and function of this caspase have yet to be revealed. We report that caspase-14, in contrast to other caspases, is not produced in active form following expression in Escherichia coli but can be activated by high concentrations of kosmotropic salts. Moreover, proteolytic cleavage is also required since the kosmotropic salts were only effective on the cleaved enzyme. We propose that caspase-14 requires proteolytic cleavage within the catalytic domain, followed by dimerization and ordering of mobile active site loops, to generate a competent enzyme. In the presence of kosmotropic salt, we were able to determine the substrate specificities of mouse and human caspase-14. Surprisingly, the substrate preferences for the human and mouse enzyme are dissimilar. The results obtained with human caspase-14 classify this enzyme as a cytokine activator, but the mouse enzyme shows preferences similar to apical apoptotic caspases.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
17
pubmed:volume
43
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
10560-9
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Activation and substrate specificity of caspase-14.
pubmed:affiliation
The Program in Apoptosis and Cell Death Research, The Burnham Institute, 10901 North Torrey Pines Road, La Jolla, California 92037, USA.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't