Document Detail


Caspase-1 activity is required for neuronal differentiation of PC12 cells: cross-talk between the caspase and calpain systems.
MedLine Citation:
PMID:  15843036     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Previously, we have found that caspase-1 activity is increased during myoblast differentiation to myotubes. Here we show that caspase-1 activity is required for PC12 differentiation to neuronal-like cells. Caspase-1 is shown to be activated (by immunoblotting and by assessing activity in cell extracts) in the PC12 cells following the initial stage of differentiation. The inhibition of caspase-1 arrests PC12 cells at an intermediate stage of differentiation and prevents neurite outgrowth in these cells; the inhibition is reversed upon the removal of the inhibitor. Calpastatin (calpain endogenous specific inhibitor, and a known caspase substrate) is diminished at the later stages of PC12 cell differentiation, and diminution is prevented by caspase-1 inhibition. The degradation of fodrin (a known caspase and calpain substrate) is found in the advanced stage of differentiation. Caspase-1 has been implicated in the activation of proinflammatory cytokines, and in cell apoptosis. The involvement of caspase-1 in two distinct differentiation processes (myoblast fusion and neuronal differentiation of PC12 cells) indicates a function for this caspase in differentiation processes, and suggests some common mechanisms underlying caspase roles in such processes.
Authors:
T Vaisid; N S Kosower; S Barnoy
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Biochimica et biophysica acta     Volume:  1743     ISSN:  0006-3002     ISO Abbreviation:  Biochim. Biophys. Acta     Publication Date:  2005 Apr 
Date Detail:
Created Date:  2005-04-21     Completed Date:  2005-06-09     Revised Date:  2005-11-17    
Medline Journal Info:
Nlm Unique ID:  0217513     Medline TA:  Biochim Biophys Acta     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  223-30     Citation Subset:  IM    
Affiliation:
Department of Human Genetics and Molecular Medicine, Sackler School of Medicine, Tel-Aviv University, Ramat-Aviv, Tel-Aviv 69978, Israel.
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MeSH Terms
Descriptor/Qualifier:
Animals
Calcium-Binding Proteins / metabolism
Calpain / antagonists & inhibitors,  metabolism*
Carrier Proteins / metabolism
Caspase 1 / antagonists & inhibitors,  metabolism*
Cell Differentiation*
Immunoblotting
Microfilament Proteins / metabolism
PC12 Cells
Protease Inhibitors / pharmacology
Rats
Chemical
Reg. No./Substance:
0/Calcium-Binding Proteins; 0/Carrier Proteins; 0/Microfilament Proteins; 0/Protease Inhibitors; 0/fodrin; 79079-11-1/calpastatin; EC 3.4.22.-/Calpain; EC 3.4.22.36/Caspase 1

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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