| Characterization of BAG3 cleavage during apoptosis of pancreatic cancer cells. | |
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MedLine Citation:
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PMID: 20232307 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Caspases are a conserved family of cell death proteases that cleave intracellular substrates at Asp residues to modify their function and promote apoptosis. In this report, we identify BAG3 as a novel caspases substrate. Here, we show that one of these BAG proteins, BAG3, is cleaved during apoptosis. BAG3 cleavage is inhibited by several different caspase inhibitors. The analysis of BAG3 cleavage by recombinant caspase proteins shows that BAG3 is efficiently cleaved by caspase-3, to a smaller extent by caspases-1 and -8, and relatively inefficient by caspase-9. Cleavage of the BAG3 protein occurs in the C-terminal part of the protein majorly at Asp347 (KEVD347 downward arrow S) in vitro and in pancreatic cancer SW1990 and PANC-1 cells undergoing apoptosis. We also demonstrate that unlike cleavage of Bcl-2 and Bcl-XL, cleaved form of BAG3 does not result in pro-apoptotic fragments, however, cleavage of BAG3 lead to loss its per se anti-apoptotic property. This novel regulation of BAG3 may have important implications for its role in apoptosis. |
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Authors:
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Hua-Qin Wang; Xin Meng; Yan-Yan Gao; Bao-Qin Liu; Xiao-Fang Niu; Hai-Yan Zhang; Zhen-Xian Du |
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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 cellular physiology Volume: 224 ISSN: 1097-4652 ISO Abbreviation: J. Cell. Physiol. Publication Date: 2010 Jul |
Date Detail:
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Created Date: 2010-04-30 Completed Date: 2010-05-24 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0050222 Medline TA: J Cell Physiol Country: United States |
Other Details:
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Languages: eng Pagination: 94-100 Citation Subset: IM |
Copyright Information:
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(c) 2010 Wiley-Liss, Inc. |
Affiliation:
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Department of Biochemistry & Molecular Biology, China Medical University, Shenyang, China. wanghq_doctor@hotmail.com |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Adaptor Proteins, Signal Transducing
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chemistry,
genetics,
metabolism* Apoptosis* / drug effects, radiation effects Aspartic Acid Caspases / antagonists & inhibitors, metabolism* Cell Line, Tumor Cysteine Proteinase Inhibitors / pharmacology Etoposide / pharmacology Humans Leupeptins / pharmacology Mutation Pancreatic Neoplasms / enzymology*, pathology Peptide Fragments / metabolism Protein Processing, Post-Translational* / drug effects, radiation effects Protein Structure, Tertiary Recombinant Proteins / metabolism Staurosporine / pharmacology Time Factors Transfection Tumor Necrosis Factor-alpha / metabolism Ultraviolet Rays |
| Chemical | |
Reg. No./Substance:
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0/Adaptor Proteins, Signal Transducing; 0/BAG3 protein, human; 0/Cysteine Proteinase Inhibitors; 0/Leupeptins; 0/Peptide Fragments; 0/Recombinant Proteins; 0/Tumor Necrosis Factor-alpha; 133407-82-6/benzyloxycarbonylleucyl-leucyl-leucine aldehyde; 33419-42-0/Etoposide; 56-84-8/Aspartic Acid; 62996-74-1/Staurosporine; EC 3.4.22.-/Caspases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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