| Identification of an interleukin-1 beta converting enzyme-like activity that increases upon treatment of P19 cells with retinoic acid as the proteasome. | |
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MedLine Citation:
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PMID: 8947829 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
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Authors:
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T Kobayashi; A Shinozaki; T Momoi; K Arahata; T Tsukahara |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Journal of biochemistry Volume: 120 ISSN: 0021-924X ISO Abbreviation: J. Biochem. Publication Date: 1996 Oct |
Date Detail:
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Created Date: 1997-03-17 Completed Date: 1997-03-17 Revised Date: 2007-12-19 |
Medline Journal Info:
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Nlm Unique ID: 0376600 Medline TA: J Biochem Country: JAPAN |
Other Details:
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Languages: eng Pagination: 699-704 Citation Subset: IM |
Affiliation:
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Department of Neuromuscular Research, Department of Development and Differentiation, National Institute of Neuroscience, NCNP Ogawahigashi-cho, Tokyo. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Animals 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 Mice Multienzyme Complexes / chemistry, isolation & purification, metabolism* Oligopeptides / chemistry Proteasome Endopeptidase Complex Substrate Specificity Tretinoin / pharmacology* Tumor Cells, Cultured / drug effects, enzymology |
| Chemical | |
Reg. No./Substance:
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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 3.4.22.36/Caspase 1; EC 3.4.25.1/Proteasome Endopeptidase Complex |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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