Source:http://linkedlifedata.com/resource/pubmed/id/11208560
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2001-3-14
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pubmed:abstractText |
We have previously reported that heat conditioning augments lipopolysaccharide (LPS)-induced fever in rats, which is accompanied by an accumulation of heat shock protein (HSP) in the liver and the reduction of the plasma level of tumor necrosis factor (TNF-alpha) (Kluger MJ, Rudolph K, Soszynski D, Conn CA, Leon LR, Kozak W, Wallen ES, and Moseley PL. Am J Physiol Regulatory Integrative Comp Physiol 273: R858-R863, 1997). In the present study we have tested whether inhibition of protein synthesis in the liver can reduce the effect of this heat conditioning on the LPS-induced febrile response in the rat. D-galactosamine (D-gal) was used to selectively inhibit liver protein synthesis. D-gal (500 mg/kg) or PBS as control was administered intraperitoneally 1 h before heat stress. LPS (50 microg/kg ip) was injected 24 h post-heat exposure. Treatment with D-gal blunted the febrile response to LPS. Moreover, heat-conditioned rats treated first with D-gal and subsequently with LPS demonstrated a profound fall in core temperature 10--18 h post-LPS. A significant increase of serum TNF-alpha accompanied this effect of D-gal on fever. Heat-conditioned animals receiving D-gal showed an inhibition in inducible HSP-70 in the liver. These data support the role of hepatic function in modulating the febrile response to LPS.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Galactosamine,
http://linkedlifedata.com/resource/pubmed/chemical/HSC70 Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/HSP70 Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Hspa8 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-6,
http://linkedlifedata.com/resource/pubmed/chemical/Lipopolysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Necrosis Factor-alpha
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0363-6119
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
280
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
R338-44
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:11208560-Animals,
pubmed-meshheading:11208560-Fever,
pubmed-meshheading:11208560-Galactosamine,
pubmed-meshheading:11208560-HSC70 Heat-Shock Proteins,
pubmed-meshheading:11208560-HSP70 Heat-Shock Proteins,
pubmed-meshheading:11208560-Hot Temperature,
pubmed-meshheading:11208560-Interleukin-6,
pubmed-meshheading:11208560-Lipopolysaccharides,
pubmed-meshheading:11208560-Liver,
pubmed-meshheading:11208560-Male,
pubmed-meshheading:11208560-Rats,
pubmed-meshheading:11208560-Rats, Sprague-Dawley,
pubmed-meshheading:11208560-Stress, Physiological,
pubmed-meshheading:11208560-Time Factors,
pubmed-meshheading:11208560-Tumor Necrosis Factor-alpha
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pubmed:year |
2001
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pubmed:articleTitle |
Effect of heat stress on LPS-induced febrile response in D-galactosamine-sensitized rats.
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pubmed:affiliation |
Department of Internal Medicine, University of New Mexico School of Medicine, Albuquerque, New Mexico 87131, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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