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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2007-12-31
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pubmed:abstractText |
During infection, damage can occur to the host as an outcome of both pathogen virulence mechanisms and host defense strategies. Using aggregation of a model polyglutamine-containing protein as an indicator in Caenorhabditis elegans, we show that protein damage occurs specifically at the site of the host-pathogen interaction, the intestine, in response to various bacterial pathogens. We demonstrate that the insulin signaling pathway and the heat shock transcription factor (HSF-1) influence the amount of aggregation that occurs, in addition to heat shock proteins and oxidative stress enzymes. We also show that addition of the antioxidants epigallocatechin gallate and alpha-lipoic acid reduces polyglutamine aggregation. The influence of oxidative stress enzymes and exogenous antioxidants on protein aggregation suggests that reactive oxygen species produced by the host are a source of protein damage during infection. We propose a model in which heat shock proteins and oxidative stress enzymes regulated by insulin signaling and HSF-1 are required for tissue protection during infection, to minimize the effects of protein damage occurring as a result of host-pathogen interactions.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antioxidants,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Caenorhabditis elegans Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Catechin,
http://linkedlifedata.com/resource/pubmed/chemical/Insulin,
http://linkedlifedata.com/resource/pubmed/chemical/Luminescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Thioctic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/epigallocatechin gallate,
http://linkedlifedata.com/resource/pubmed/chemical/heat shock factor-1, C elegans,
http://linkedlifedata.com/resource/pubmed/chemical/polyglutamine,
http://linkedlifedata.com/resource/pubmed/chemical/yellow fluorescent protein, Bacteria
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
4
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pubmed:volume |
283
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
194-201
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:17951251-Animals,
pubmed-meshheading:17951251-Animals, Genetically Modified,
pubmed-meshheading:17951251-Antioxidants,
pubmed-meshheading:17951251-Bacteria,
pubmed-meshheading:17951251-Bacterial Proteins,
pubmed-meshheading:17951251-Caenorhabditis elegans,
pubmed-meshheading:17951251-Caenorhabditis elegans Proteins,
pubmed-meshheading:17951251-Catechin,
pubmed-meshheading:17951251-Homeostasis,
pubmed-meshheading:17951251-Hot Temperature,
pubmed-meshheading:17951251-Insulin,
pubmed-meshheading:17951251-Intestines,
pubmed-meshheading:17951251-Luminescent Proteins,
pubmed-meshheading:17951251-Microscopy, Fluorescence,
pubmed-meshheading:17951251-Muscles,
pubmed-meshheading:17951251-Neurons,
pubmed-meshheading:17951251-Oxidative Stress,
pubmed-meshheading:17951251-Peptides,
pubmed-meshheading:17951251-Signal Transduction,
pubmed-meshheading:17951251-Thioctic Acid,
pubmed-meshheading:17951251-Transcription Factors
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pubmed:year |
2008
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pubmed:articleTitle |
Insulin signaling and the heat shock response modulate protein homeostasis in the Caenorhabditis elegans intestine during infection.
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pubmed:affiliation |
Department of Microbiology and Molecular Genetics, University of Texas Health Science Center, 6431 Fannin Street, Houston, TX 77030, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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