Document Detail


In the cut and thrust of apoptosis, serine proteases come of age.
MedLine Citation:
PMID:  14555223     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Proteolysis is central to the systematic cellular degradation that occurs during apoptosis. Predominantly, caspases have been studied in this regard. However, increasing evidence suggests that certain serine proteases may also play a significant role in apoptosis. Not only are these serine proteases involved in apoptosis signalling pathways independently, but they may also interact with more classical mediators of apoptosis such as the caspases or Bcl-2 family proteins. Isolation of apoptosis-associated serine proteases and the use of specific inhibitors have helped to shed light on potential pathways in which they are involved. Despite the recent developments in the field, knowledge regarding the role of serine proteases in apoptosis remains limited, but it is clear that investigations are gathering momentum and such studies may herald a new and exciting departure in apoptosis research.
Authors:
Catherine Stenson-Cox; Una FitzGerald; Afshin Samali
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Review    
Journal Detail:
Title:  Biochemical pharmacology     Volume:  66     ISSN:  0006-2952     ISO Abbreviation:  Biochem. Pharmacol.     Publication Date:  2003 Oct 
Date Detail:
Created Date:  2003-10-13     Completed Date:  2003-11-20     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0101032     Medline TA:  Biochem Pharmacol     Country:  England    
Other Details:
Languages:  eng     Pagination:  1469-74     Citation Subset:  IM    
Affiliation:
Cell Stress and Apoptosis Research Group, Department of Biochemistry, National Centre of Biomedical Engineering Science, National University of Ireland, Galway, Ireland.
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MeSH Terms
Descriptor/Qualifier:
Animals
Apoptosis / physiology*
Caspases / metabolism
Humans
Serine Endopeptidases / metabolism*
Serine Proteinase Inhibitors / pharmacology
Chemical
Reg. No./Substance:
0/Serine Proteinase Inhibitors; EC 3.4.21.-/Serine Endopeptidases; EC 3.4.22.-/Caspases

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