| Protease signalling in cell death: caspases versus cysteine cathepsins. | |
| | |
MedLine Citation:
|
PMID: 17544407 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
|
Proteases were, for a long time, mainly considered as protein degrading enzymes. However, in the last decade this view has changed dramatically, and the focus is now on proteases as signalling molecules. One of the best examples is apoptosis, the major mechanism used by eukaryotes to remove superfluous, damaged and potentially dangerous cells, in which a number of proteases have been found to play a central role. Of these the caspases have been considered to be the major players. However, more recently, other proteases have been increasingly suggested as being important in apoptosis, in particular the cysteine cathepsins. In this review the roles of caspases and cysteine cathepsins in apoptosis signalling are compared and discussed. |
| | |
Authors:
|
Boris Turk; Veronika Stoka |
Related Documents
:
|
18515717 - Extensive apoptosis and abnormal morphogenesis in pro-caspase-3 transgenic zebrafish du... 17163597 - Molecular mechanism of matrine-induced apoptosis in leukemia k562 cells. 10861457 - Apoptosis induced by immunotoxins used in the treatment of hematologic malignancies. 7500007 - Dna-dependent protein kinase is one of a subset of autoantigens specifically cleaved ea... 15350837 - Apoptosome formation and caspase activation: is it different in the heart? 12563297 - Interleukin-12 and the regulation of innate resistance and adaptive immunity. |
Publication Detail:
|
Type: Journal Article; Research Support, Non-U.S. Gov't; Review Date: 2007-05-25 |
Journal Detail:
|
Title: FEBS letters Volume: 581 ISSN: 0014-5793 ISO Abbreviation: FEBS Lett. Publication Date: 2007 Jun |
Date Detail:
|
Created Date: 2007-06-11 Completed Date: 2007-08-30 Revised Date: - |
Medline Journal Info:
|
Nlm Unique ID: 0155157 Medline TA: FEBS Lett Country: Netherlands |
Other Details:
|
Languages: eng Pagination: 2761-7 Citation Subset: IM |
Affiliation:
|
Department of Biochemistry, Molecular and Structural Biology, J. Stefan Institute, Jamova 39, SI-1000 Ljubljana, Slovenia. boris.turk@ijs.si |
Export Citation:
|
APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
|
Apoptosis
/
physiology* Caspases / metabolism Cathepsins / metabolism Enzyme Activation Humans Peptide Hydrolases / metabolism* Signal Transduction / physiology |
| Chemical | |
Reg. No./Substance:
|
EC 3.4.-/Cathepsins; EC 3.4.-/Peptide Hydrolases; EC 3.4.22.-/Caspases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
Previous Document: Chimeric phosphofructokinases involving exchange of the N- and C-terminal halves of mammalian isozym...
Next Document: Contributions of Zn(II)-binding to the structural stability of endostatin.