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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
1999-4-15
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
16
pubmed:volume
38
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3355-61
pubmed:dateRevised
2005-11-17
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
pubmed:year
1999
pubmed:articleTitle
A binding protein to the DNase I hypersensitive site II in HLA-DR alpha gene was identified as NF90.
pubmed:affiliation
Laboratory of Molecular Biology, Medical Research Center, Kochi Medical School, Japan.
pubmed:publicationType
Journal Article