Document Detail

Identification of an interleukin-1 beta converting enzyme-like activity that increases upon treatment of P19 cells with retinoic acid as the proteasome.
MedLine Citation:
PMID:  8947829     Owner:  NLM     Status:  MEDLINE    
We examined changes in proteinase activities in P19 embryonal carcinoma cells during retinoic acid-induced differentiation. The interleukin-1 beta converting enzyme (ICE)-like Ac-YVAD-MCA hydrolytic activity was increased about 6-fold by treatment with retinoic acid. This activity was inhibited by N-ethylmaleimide and Ac-YVAD-H but not by E-64, EDTA, PMSF, or amastatin. The ICE-like activity in P19 cells eluted as a single peak just after the void volume on gel filtration. No ICE-like activity was observed at a molecular mass of 30-50 kDa. Enzymatic purification, Western blot analysis, and an immunoabsorption study demonstrated that the ICE-like activity in P19 cells is caused by the proteasome, and is stimulated during retinoic acid-induced differentiation. The proteasome purified from mouse liver also cleaved Ac-YVAD-MCA. These results strongly suggest that the proteasome is a major ICE-like proteinase in P19 cells and may be involved in the neural differentiation and the apoptotic pathway.
T Kobayashi; A Shinozaki; T Momoi; K Arahata; T Tsukahara
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of biochemistry     Volume:  120     ISSN:  0021-924X     ISO Abbreviation:  J. Biochem.     Publication Date:  1996 Oct 
Date Detail:
Created Date:  1997-03-17     Completed Date:  1997-03-17     Revised Date:  2007-12-19    
Medline Journal Info:
Nlm Unique ID:  0376600     Medline TA:  J Biochem     Country:  JAPAN    
Other Details:
Languages:  eng     Pagination:  699-704     Citation Subset:  IM    
Department of Neuromuscular Research, Department of Development and Differentiation, National Institute of Neuroscience, NCNP Ogawahigashi-cho, Tokyo.
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MeSH Terms
Apoptosis / drug effects
Carcinoma, Embryonal / enzymology*,  pathology
Caspase 1
Cell Differentiation / drug effects
Coumarins / chemistry
Cysteine Endopeptidases / chemistry,  isolation & purification,  metabolism*
Edetic Acid / pharmacology
Ethylmaleimide / pharmacology
Liver / enzymology
Multienzyme Complexes / chemistry,  isolation & purification,  metabolism*
Oligopeptides / chemistry
Proteasome Endopeptidase Complex
Substrate Specificity
Tretinoin / pharmacology*
Tumor Cells, Cultured / drug effects,  enzymology
Reg. No./Substance:
0/Coumarins; 0/Multienzyme Complexes; 0/Oligopeptides; 0/acetyl-tyrosyl-valyl-alanyl-aspartyl-7-amino-4-methylcoumarinamide; 128-53-0/Ethylmaleimide; 302-79-4/Tretinoin; 60-00-4/Edetic Acid; EC 3.4.22.-/Cysteine Endopeptidases; EC 1; EC Endopeptidase Complex

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

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