Source:http://linkedlifedata.com/resource/pubmed/id/15684817
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
11
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| pubmed:dateCreated |
2005-2-1
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| pubmed:abstractText |
Interferon (IFN)-stimulated gene (15 kDa) (ISG15) is a ubiquitin-like protein that forms covalent conjugates with cellular proteins. ISG15 is induced by IFN, microbial challenge, and p53, suggesting that it represents a genetic response that is shared among diverse stress stimuli. To investigate the regulation of this posttranslational modification pathway by a genotoxic chemotherapeutic agent, we examined ISG15 induction and conjugation in cells treated with the topoisomerase I (topoI) poison, camptothecin (CPT). CPT induced ISG15mRNA, and induction required protein synthesis and a functional p53 protein. However, IFN and the Jak-Stat components of the IFN signaling pathway were dispensable for CPT induction of ISG15. CPT induced free ISG15 and conjugates in a dose-dependent and time-dependent manner. A single 55-kDa protein was the prominent CPT-induced ISG15 conjugate and localized to the nuclear compartment. CPT-induced ISG15 conjugates were distinct from those induced by IFN; however, CPT treatment dramatically enhanced ISG15 conjugation in response to IFN. These findings provide the first evidence of a stimulus-specific induction of discrete ISG15 conjugate species and demonstrate that treatment with a combination of cancer therapeutic agents can cooperate to enhance ISG15 conjugation. Identification of the specific ISG15 conjugates induced by chemotherapeutic agents may reveal novel molecular targets.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antineoplastic Agents, Phytogenic,
http://linkedlifedata.com/resource/pubmed/chemical/Camptothecin,
http://linkedlifedata.com/resource/pubmed/chemical/Cycloheximide,
http://linkedlifedata.com/resource/pubmed/chemical/Cytokines,
http://linkedlifedata.com/resource/pubmed/chemical/ISG15 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Interferons,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Topoisomerase I Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitins
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| pubmed:status |
MEDLINE
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| pubmed:month |
Nov
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| pubmed:issn |
1079-9907
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
24
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
647-54
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| pubmed:dateRevised |
2010-11-18
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| pubmed:meshHeading |
pubmed-meshheading:15684817-Antineoplastic Agents, Phytogenic,
pubmed-meshheading:15684817-Blotting, Northern,
pubmed-meshheading:15684817-Blotting, Western,
pubmed-meshheading:15684817-Camptothecin,
pubmed-meshheading:15684817-Cell Line, Tumor,
pubmed-meshheading:15684817-Cell Nucleus,
pubmed-meshheading:15684817-Cycloheximide,
pubmed-meshheading:15684817-Cytokines,
pubmed-meshheading:15684817-Dose-Response Relationship, Drug,
pubmed-meshheading:15684817-Humans,
pubmed-meshheading:15684817-Interferons,
pubmed-meshheading:15684817-Protein Binding,
pubmed-meshheading:15684817-Protein Processing, Post-Translational,
pubmed-meshheading:15684817-RNA, Messenger,
pubmed-meshheading:15684817-Signal Transduction,
pubmed-meshheading:15684817-Time Factors,
pubmed-meshheading:15684817-Topoisomerase I Inhibitors,
pubmed-meshheading:15684817-Ubiquitins
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| pubmed:year |
2004
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| pubmed:articleTitle |
Camptothecin induces the ubiquitin-like protein, ISG15, and enhances ISG15 conjugation in response to interferon.
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| pubmed:affiliation |
Program in Molecular and Cell Biology, University of Maryland, School of Medicine, Baltimore, MD 21201, USA.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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