| Bcl-2 blocks apoptosis caused by pierisin-1, a guanine-specific ADP-ribosylating toxin from the cabbage butterfly. | |
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MedLine Citation:
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PMID: 12147221 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Pierisin-1, a 98-kDa protein that induces apoptosis in mammalian cell lines, is capable of being incorporated into cells where it ADP-ribosylates guanine residues in DNA. To investigate the apoptotic pathway induced by this unique protein, the bcl-2 gene was transfected into HeLa cells. Cy2-fluorescent pierisin-1 was incorporated into the resultant cells expressing Bcl-2 protein and ADP-ribosylated dG was detected to almost the same extent as in parent cells. However, bcl-2-transfected HeLa cells did not display apoptotic morphological changes, PARP cleavage, and DNA fragmentation, indicating acquisition of resistance. In parent HeLa cells, activation of caspase-9 and release of cytochrome c were observed after 8h treatment with 0.5ng/ml pierisin-1. Caspase substrate assays revealed further cleavage of Ac-DEVD-pNA, Ac-VDVAD-pNA, and Ac-VEID-pNA, suggesting activation of caspase-2, -3, and -6 in pierisin-1-treated HeLa cells. The caspase-3 inhibitor, Ac-DEVD-CHO, was also found to inhibit apoptosis. In contrast, this caspase activation was not observed in bcl-2-transfected HeLa cells. Our results thus indicate that pierisin-1-induced apoptosis is mediated primarily via a mitochondrial pathway involving Bcl-2 and caspases. |
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Authors:
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Takashi Kanazawa; Takuo Kono; Masahiko Watanabe; Yuko Matsushima-Hibiya; Tsuyoshi Nakano; Kotaro Koyama; Noriaki Tanaka; Takashi Sugimura; Keiji Wakabayashi |
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: 296 ISSN: 0006-291X ISO Abbreviation: Biochem. Biophys. Res. Commun. Publication Date: 2002 Aug |
Date Detail:
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Created Date: 2002-07-30 Completed Date: 2002-09-06 Revised Date: 2007-11-15 |
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: 20-5 Citation Subset: IM |
Affiliation:
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Cancer Prevention Division, National Cancer Center Research Institute, 5-1-1 Tsukiji, Chuo-ku, 104-0045, Tokyo, Japan. tkanazaw@gan2.ncc.go.jp |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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ADP Ribose Transferases Adenosine Diphosphate / metabolism* Animals Apoptosis / drug effects, genetics* Butterflies Caspases / metabolism Cytochrome c Group / metabolism Enzyme Activation Genes, bcl-2* Hela Cells Humans Insect Proteins / pharmacology* |
| Chemical | |
Reg. No./Substance:
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0/Cytochrome c Group; 0/Insect Proteins; 0/pierisin protein, insect; 58-64-0/Adenosine Diphosphate; EC 2.4.2.-/ADP Ribose Transferases; EC 3.4.22.-/Caspases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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