Source:http://linkedlifedata.com/resource/pubmed/id/10079079
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
11
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pubmed:dateCreated |
1999-4-15
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pubmed:abstractText |
We previously observed that IFN gamma-inducible expression of the human MHC class II, HLA-DR alpha, gene was enhanced by treatment with 12-O-tetradecanoylphorbol-13-acetate (TPA) only in human monocytic leukemia THP-1 cells, but not in HeLa cells. In the HLA-DR alpha gene, three DNase I hypersensitive sites (DHS) are known to be present in the promoter region (DHS-I) and first intron (DHS-II and -III) and are assumed to be involved in HLA-DR alpha gene regulation. In this study, we found a binding factor which recognized a unique palindrome sequence (DHS-22) in the region of the DHS II site of the HLA-DR alpha gene in THP-1 cells and HeLa cells. The binding activity of this factor was decreased by TPA treatment in THP-1 cells, but not in HeLa cells. This binding activity was also detectable in nuclear extracts of bovine brains. Thus, we isolated the DHS-22 binding factor from bovine brain nuclear extracts and finally identified it as NF90 on the basis of molecular mass analysis of Lys-C-digested fragments and amino acid sequences of the two peptides of the trypsin-digested binding protein. The DHS-22 binding protein(s) in THP-1 cells is (are) further confirmed by reactivity to an antibody against NF90, and we have demonstrated that the GST fusion protein of NF90 interacts with DHS-22 by electrophoretic gel mobility shift assay (EMSA). The mRNA of NF90 was decreased by TPA treatment in THP-1 cells but not in HeLa cells. These results suggest that the binding of NF90 to the DNase I hypersensitive site II of HLA-DR alpha gene seems to negatively regulate HLA-DR alpha gene expression.
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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/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Deoxyribonuclease I,
http://linkedlifedata.com/resource/pubmed/chemical/HLA-DR Antigens,
http://linkedlifedata.com/resource/pubmed/chemical/NFATC Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Factor 90 Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tetradecanoylphorbol Acetate,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
16
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pubmed:volume |
38
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3355-61
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pubmed:dateRevised |
2005-11-17
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pubmed:meshHeading |
pubmed-meshheading:10079079-Animals,
pubmed-meshheading:10079079-Base Sequence,
pubmed-meshheading:10079079-Binding Sites,
pubmed-meshheading:10079079-Blotting, Western,
pubmed-meshheading:10079079-Cattle,
pubmed-meshheading:10079079-Cell Line,
pubmed-meshheading:10079079-DNA-Binding Proteins,
pubmed-meshheading:10079079-Deoxyribonuclease I,
pubmed-meshheading:10079079-Genes, MHC Class II,
pubmed-meshheading:10079079-HLA-DR Antigens,
pubmed-meshheading:10079079-HeLa Cells,
pubmed-meshheading:10079079-Humans,
pubmed-meshheading:10079079-Molecular Sequence Data,
pubmed-meshheading:10079079-NFATC Transcription Factors,
pubmed-meshheading:10079079-Nuclear Factor 90 Proteins,
pubmed-meshheading:10079079-Nuclear Proteins,
pubmed-meshheading:10079079-Phosphorylation,
pubmed-meshheading:10079079-Protein Binding,
pubmed-meshheading:10079079-Tetradecanoylphorbol Acetate,
pubmed-meshheading:10079079-Transcription Factors
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pubmed:year |
1999
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pubmed:articleTitle |
A binding protein to the DNase I hypersensitive site II in HLA-DR alpha gene was identified as NF90.
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pubmed:affiliation |
Laboratory of Molecular Biology, Medical Research Center, Kochi Medical School, Japan.
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pubmed:publicationType |
Journal Article
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