Source:http://linkedlifedata.com/resource/pubmed/id/12781699
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
2003-6-3
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pubmed:abstractText |
In the central nervous system (CNS), cytokine-primed microglia play a central role in host's defense against Acanthamoeba castellanii infection. In this study, the effect of recombinant interferon (rIFN)-gamma and Salmonella enterica serovar enteritidis lipopolysaccharide (LPS), both inflammatory stimuli, on A. castellanii infection in murine microglia was examined. Priming of microglia with rIFN-gamma and LPS synergistically triggered, in a dose-dependent manner, amebastatic activity in these cells. More than 52%, 88% or 95% of this function was then abrogated by anti-IL-1beta (but not anti-IL-1alpha), IL-6 or TNF-alpha neutralizing antibodies, suggesting that these endogenously produced cytokines may participate in the antimicrobial capacity. Consistent with these findings, the priming of microglia with rIFN-gamma and LPS elicited the release of proinflammatory interleukin (IL)-1alpha, IL-1beta, IL-6 and tumor necrosis factor (TNF)-alpha. Since L-canavanine affected amebastatic activity only during the priming process but not during the infection process, NO-dependent pathway appears to be not the sole antiparasitic mechanism involved in this function. These data suggest that rIFN-gamma and LPS, likely through a proinflammatory network, up-regulate the release of IL-beta, IL-6 and TNF-alpha, which could trigger antimicrobial activity against A. castellanii infection in the brain.
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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/Antibodies, Blocking,
http://linkedlifedata.com/resource/pubmed/chemical/Canavanine,
http://linkedlifedata.com/resource/pubmed/chemical/Cytokines,
http://linkedlifedata.com/resource/pubmed/chemical/Indicators and Reagents,
http://linkedlifedata.com/resource/pubmed/chemical/Interferon-gamma,
http://linkedlifedata.com/resource/pubmed/chemical/Lipopolysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
1567-5769
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
3
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
825-34
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:12781699-Acanthamoeba,
pubmed-meshheading:12781699-Amebiasis,
pubmed-meshheading:12781699-Animals,
pubmed-meshheading:12781699-Antibodies, Blocking,
pubmed-meshheading:12781699-Canavanine,
pubmed-meshheading:12781699-Cell Division,
pubmed-meshheading:12781699-Cells, Cultured,
pubmed-meshheading:12781699-Cytokines,
pubmed-meshheading:12781699-Indicators and Reagents,
pubmed-meshheading:12781699-Interferon-gamma,
pubmed-meshheading:12781699-Lipopolysaccharides,
pubmed-meshheading:12781699-Mice,
pubmed-meshheading:12781699-Mice, Inbred BALB C,
pubmed-meshheading:12781699-Microglia,
pubmed-meshheading:12781699-Recombinant Proteins
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pubmed:year |
2003
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pubmed:articleTitle |
Defense mechanisms of IFN-gamma and LPS-primed murine microglia against Acanthamoeba castellanii infection.
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pubmed:affiliation |
Section of Microbiology and Clinical Microbiology, Department of Experimental Medicine, Faculty of Medicine and Surgery, Second University of the Studies of Naples, Naples, Italy. nunzia.benedetto@unina2.it
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pubmed:publicationType |
Journal Article
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