Source:http://linkedlifedata.com/resource/pubmed/id/15878889
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2005-8-22
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pubmed:abstractText |
Nonclassical human leukocyte antigen (HLA) class I molecule HLA-G and indoleamine 2,3 dioxygenase (INDO) in humans and mice, respectively, have been shown to play crucial immunosuppressive roles in fetal-maternal tolerance. HLA-G inhibits natural killer and T cell function by high-affinity interaction with inhibitory receptors, and INDO acts by depleting the surrounding microenvironment of the essential amino acid tryptophan, thus inhibiting T cell proliferation. We investigated whether HLA-G expression and INDO function were linked. Working with antigen-presenting cell (APC) lines and monocytes, we found that functional inhibition of INDO by 1-methyl-tryptophan induced cell surface expression of HLA-G1 by HLA-G1-negative APCs that were originally cell-surface negative, and that in reverse, the functional boost of INDO by high concentrations of tryptophan induced a complete loss of HLA-G1 cell surface expression by APCs that were originally cell-surface HLA-G1-positive. This mechanism was shown to be posttranslational because HLA-G protein cell contents remained unaffected by the treatments used. Furthermore, HLA-G cell surface expression regulation by INDO seems to relate to INDO function, but not to tryptophan catabolism itself. Potential implications in fetal-maternal tolerance are discussed.
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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/1-methyl-tryptophan,
http://linkedlifedata.com/resource/pubmed/chemical/HLA Antigens,
http://linkedlifedata.com/resource/pubmed/chemical/HLA-G Antigens,
http://linkedlifedata.com/resource/pubmed/chemical/Histocompatibility Antigens Class I,
http://linkedlifedata.com/resource/pubmed/chemical/Tryptophan,
http://linkedlifedata.com/resource/pubmed/chemical/Tryptophan Oxygenase
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0006-3363
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
73
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
571-8
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:15878889-Cell Line,
pubmed-meshheading:15878889-HLA Antigens,
pubmed-meshheading:15878889-HLA-G Antigens,
pubmed-meshheading:15878889-Histocompatibility Antigens Class I,
pubmed-meshheading:15878889-Humans,
pubmed-meshheading:15878889-Monocytes,
pubmed-meshheading:15878889-Protein Processing, Post-Translational,
pubmed-meshheading:15878889-Tryptophan,
pubmed-meshheading:15878889-Tryptophan Oxygenase,
pubmed-meshheading:15878889-Up-Regulation
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pubmed:year |
2005
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pubmed:articleTitle |
Linking two immuno-suppressive molecules: indoleamine 2,3 dioxygenase can modify HLA-G cell-surface expression.
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pubmed:affiliation |
Clínica Universitaria de Navarra, 31080 Pamplona, Navarra, Spain.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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