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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2003-7-22
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pubmed:abstractText |
The nonclassical class I MHC molecule HLA-G is selectively expressed on extravillous cytotrophoblast cells at the maternal-fetal interface during pregnancy. HLA-G can inhibit the killing mediated by NK cells via interaction with the inhibitory NK cell receptor, leukocyte Ig-like receptor-1 (LIR-1). Comparison of the sequence of the HLA-G molecule to other class I MHC proteins revealed two unique cysteine residues located in positions 42 and 147. Mutating these cysteine residues resulted in a dramatic decrease in LIR-1 Ig binding. Accordingly, the mutated HLA-G transfectants were less effective in the inhibition of NK killing and RBL/LIR-1 induced serotonin release. Immunoprecipitation experiments demonstrated the involvement of the cysteine residues in the formation of HLA-G protein oligomers on the cell surface. The cysteine residue located at position 42 is shown to be critical for the expression of such complexes. These oligomers, unique among the class I MHC proteins, probably bind to LIR-1 with increased avidity, resulting in an enhanced inhibitory function of LIR-1 and an impaired killing function of NK cells.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine,
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/LILRB1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Immunologic
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0022-1767
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pubmed:author |
pubmed-author:AchdoutHagitH,
pubmed-author:BaniyashMichalM,
pubmed-author:GazitRoiR,
pubmed-author:Goldman-WohlDebraD,
pubmed-author:Gonen-GrossTsufitT,
pubmed-author:HannaJacobJ,
pubmed-author:HorejsíVáclavV,
pubmed-author:LevyOferO,
pubmed-author:MandelboimOferO,
pubmed-author:MarkelGalG,
pubmed-author:MizrahiSa'arS,
pubmed-author:YagelSimchaS
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
171
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1343-51
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:12874224-Amino Acid Sequence,
pubmed-meshheading:12874224-Animals,
pubmed-meshheading:12874224-Antigens, CD,
pubmed-meshheading:12874224-Binding, Competitive,
pubmed-meshheading:12874224-Cell Line, Transformed,
pubmed-meshheading:12874224-Cysteine,
pubmed-meshheading:12874224-Cytotoxicity, Immunologic,
pubmed-meshheading:12874224-Decidua,
pubmed-meshheading:12874224-Down-Regulation,
pubmed-meshheading:12874224-Female,
pubmed-meshheading:12874224-HLA Antigens,
pubmed-meshheading:12874224-HLA-G Antigens,
pubmed-meshheading:12874224-Histocompatibility Antigens Class I,
pubmed-meshheading:12874224-Humans,
pubmed-meshheading:12874224-Macromolecular Substances,
pubmed-meshheading:12874224-Membrane Glycoproteins,
pubmed-meshheading:12874224-Molecular Sequence Data,
pubmed-meshheading:12874224-Mutagenesis, Site-Directed,
pubmed-meshheading:12874224-Protein Binding,
pubmed-meshheading:12874224-Rats,
pubmed-meshheading:12874224-Receptors, Immunologic,
pubmed-meshheading:12874224-Transfection,
pubmed-meshheading:12874224-Tumor Cells, Cultured
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pubmed:year |
2003
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pubmed:articleTitle |
Complexes of HLA-G protein on the cell surface are important for leukocyte Ig-like receptor-1 function.
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pubmed:affiliation |
Lautenberg Center for General and Tumor Immunology, Hebrew University-Hadassah Medical School, Jerusalem, Israel.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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