| Specific cleavage of the large subunit of replication factor C in apoptosis is mediated by CPP32-like protease. | |
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MedLine Citation:
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PMID: 9144536 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Recent evidence suggests that the growing family of cysteine proteases related to the interleukin-1beta-converting enzyme (ICE) is of central importance in mediating apoptosis. Proteolytic cleavage of a small group of cellular substrates by these enzymes in association with the onset of apoptosis has been reported. In the present study, we searched a protein data base for potential death substrates possessing the CPP32 cleavage site, DEVD, and identified several candidates including RFC140, the large subunit of replication factor C, which we subsequently demonstrated to be specifically cleaved in a variety of cell types undergoing apoptosis in response to different cytotoxic agents, whereas no degradation is observed in a cell line resistant to etoposide-induced apoptosis. The abrogation of RFC140 cleavage in apoptotic extracts by Ac-DEVD-CHO, a potent inhibitor of CPP32, together with the finding that a CPP32 consensus cleavage sequence, DEVD, exists in RFC140, suggests that CPP32 or a close relative is responsible for RFC140 degradation in apoptosis. |
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Authors:
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Q Song; H Lu; N Zhang; B Luckow; G Shah; G Poirier; M Lavin |
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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: Biochemical and biophysical research communications Volume: 233 ISSN: 0006-291X ISO Abbreviation: Biochem. Biophys. Res. Commun. Publication Date: 1997 Apr |
Date Detail:
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Created Date: 1997-06-05 Completed Date: 1997-06-05 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 0372516 Medline TA: Biochem Biophys Res Commun Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 343-8 Citation Subset: IM |
Affiliation:
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Queensland Institute of Medical Research, University of Queensland, P.O. Royal Brisbane Hospital, Australia. qizhongS@qimr.edu.au |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Animals Apoptosis* Caspase 1 Caspase 3 Caspases* Cysteine Endopeptidases / metabolism* Cysteine Proteinase Inhibitors / metabolism DNA Replication* DNA-Binding Proteins / metabolism* Enzyme Precursors / metabolism Homeodomain Proteins* Interleukin-1 / metabolism Oligopeptides / metabolism Proto-Oncogene Proteins c-bcl-2 / metabolism* Replication Protein C Repressor Proteins* Saccharomyces cerevisiae Proteins* Tumor Cells, Cultured |
| Chemical | |
Reg. No./Substance:
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0/BCL2-related protein A1; 0/Cysteine Proteinase Inhibitors; 0/DNA-Binding Proteins; 0/Enzyme Precursors; 0/Homeodomain Proteins; 0/Interleukin-1; 0/MATA1 protein, S cerevisiae; 0/Oligopeptides; 0/Proto-Oncogene Proteins c-bcl-2; 0/Replication Protein C; 0/Repressor Proteins; 0/Saccharomyces cerevisiae Proteins; 0/acetyl-aspartyl-glutamyl-valyl-aspartal; EC 3.4.22.-/Caspase 3; EC 3.4.22.-/Caspases; EC 3.4.22.-/Cysteine Endopeptidases; EC 3.4.22.36/Caspase 1 |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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