Source:http://linkedlifedata.com/resource/pubmed/id/17878377
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
7
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| pubmed:dateCreated |
2007-9-19
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| pubmed:abstractText |
Anaplasma phagocytophilum is an obligate intracellular pathogen that resides within neutrophils and can cause fever, pancytopenia, or death. IFN-gamma plays a critical role in the control of A. phagocytophilum; however, the mechanisms that regulate IFN-gamma production remain unclear. In this study, we demonstrate that apoptotic specklike protein with a caspase-activating recruiting domain (ASC)/PYCARD, a central adaptor molecule in the Nod-like receptor (NLR) pathway, regulates the IL-18/IFN-gamma axis during A. phagocytophilum infection through its effect on caspase-1. Caspase-1- and asc-null mice were more susceptible than control animals to A. phagocytophilum infection due to the absence of IL-18 secretion and reduced IFN-gamma levels in the peripheral blood. Moreover, caspase-1 and ASC deficiency reduced CD4+ T cell-mediated IFN-gamma after in vitro restimulation with A. phagocytophilum. The NLR family member IPAF/NLRC4, but not NALP3/NLRP3, was partially required for IFN-gamma production in response to A. phagocytophilum. Taken together, our data demonstrate that ASC and caspase-1 are critical for IFN-gamma-mediated control of A. phagocytophilum infection.
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| pubmed:grant | |
| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
AIM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Apoptosis Regulatory Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Caspase 1,
http://linkedlifedata.com/resource/pubmed/chemical/Interferon-gamma,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-18,
http://linkedlifedata.com/resource/pubmed/chemical/Ipaf protein, mouse
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| pubmed:status |
MEDLINE
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| pubmed:month |
Oct
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| pubmed:issn |
0022-1767
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
1
|
| pubmed:volume |
179
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| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
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| pubmed:pagination |
4783-91
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| pubmed:dateRevised |
2008-11-21
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| pubmed:meshHeading |
pubmed-meshheading:17878377-Amino Acid Motifs,
pubmed-meshheading:17878377-Anaplasma,
pubmed-meshheading:17878377-Anaplasmosis,
pubmed-meshheading:17878377-Animals,
pubmed-meshheading:17878377-Apoptosis Regulatory Proteins,
pubmed-meshheading:17878377-Calcium-Binding Proteins,
pubmed-meshheading:17878377-Caspase 1,
pubmed-meshheading:17878377-Disease Susceptibility,
pubmed-meshheading:17878377-Enzyme Activation,
pubmed-meshheading:17878377-HL-60 Cells,
pubmed-meshheading:17878377-Humans,
pubmed-meshheading:17878377-Interferon-gamma,
pubmed-meshheading:17878377-Interleukin-18,
pubmed-meshheading:17878377-Killer Cells, Natural,
pubmed-meshheading:17878377-Mice,
pubmed-meshheading:17878377-Mice, Inbred C57BL,
pubmed-meshheading:17878377-Mice, Knockout,
pubmed-meshheading:17878377-Phagocytosis,
pubmed-meshheading:17878377-Signal Transduction,
pubmed-meshheading:17878377-T-Lymphocytes, Regulatory,
pubmed-meshheading:17878377-Th1 Cells
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| pubmed:year |
2007
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| pubmed:articleTitle |
ASC/PYCARD and caspase-1 regulate the IL-18/IFN-gamma axis during Anaplasma phagocytophilum infection.
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| pubmed:affiliation |
Section of Infectious Diseases, Department of Internal Medicine, Yale University School of Medicine, New Haven, CT 06520, USA.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
|