Source:http://linkedlifedata.com/resource/pubmed/id/15381187
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2004-9-21
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pubmed:abstractText |
The extract from Ascaris suum worms (Asc) impairs Th1 and Th2 responses to a non-related antigen, i.e. ovalbumin (OVA). Its suppressive capacity is due to high molecular weight components present in a gel filtration fraction (PI). This fraction is able to elicit IL-4 and IL-10 secretion. Interestingly enough, it induces anti-PI non-anaphylactic IgG1 synthesis through the action of IL-12/IFN-gamma. Here, we investigated the down-regulation of the immune response to OVA by PI in IL-12, IFN-gamma, IL-4 or IL-10 C57BL/6 knockout mice immunized with OVA+PI in adjuvant. OVA-induced delayed-type hypersensitivity (DTH) reactions, secretion of IL-2 and IFN-gamma, and IgG1, IgG2c and IgE antibody production were suppressed by PI in wild-type mice, as well as in IL-12- or IFN-gamma-deficient mice. In contrast, PI had no effect on anti-OVA IgE production and DTH, and induced only a partial suppression of IgG1 and IFN-gamma in IL-10(-/-) mice. The experiments also showed that IL-4 was involved in the PI-induced suppression of IgG2c antibodies and IL-2 secretion. Finally, down-regulation of IFN-gamma was not seen in mice lacking both IL-4 and IL-10, i.e. IL-4(-/-) mice treated with anti-IL-10 antibodies before immunization. These results exclude the participation of IL-12 and IFN-gamma in PI-induced immunosuppression, and highlight the essential role of IL-10 in the suppression of OVA-specific Th2-related parameters, as well as the cooperation between IL-10 and IL-4 in the suppression of Th1-related parameters.
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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/Helminth Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Interferon-gamma,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-10,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-12,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-4,
http://linkedlifedata.com/resource/pubmed/chemical/Ovalbumin
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
1043-4666
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
21
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pubmed:volume |
28
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
92-100
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:15381187-Animals,
pubmed-meshheading:15381187-Ascaris suum,
pubmed-meshheading:15381187-Helminth Proteins,
pubmed-meshheading:15381187-Immune Tolerance,
pubmed-meshheading:15381187-Interferon-gamma,
pubmed-meshheading:15381187-Interleukin-10,
pubmed-meshheading:15381187-Interleukin-12,
pubmed-meshheading:15381187-Interleukin-4,
pubmed-meshheading:15381187-Mice,
pubmed-meshheading:15381187-Mice, Knockout,
pubmed-meshheading:15381187-Models, Molecular,
pubmed-meshheading:15381187-Molecular Weight,
pubmed-meshheading:15381187-Ovalbumin
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pubmed:year |
2004
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pubmed:articleTitle |
IL-4 and IL-10 are essential for immunosuppression induced by high molecular weight proteins from Ascaris suum.
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pubmed:affiliation |
Department of Immunology, Institute of Biomedical Sciences, University of São Paulo, Av. Prof. Lineu Prestes, 1730, 05508-900 São Paulo, SP, Brazil.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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