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rdf:type |
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lifeskim:mentions |
umls-concept:C0017262,
umls-concept:C0017337,
umls-concept:C0033413,
umls-concept:C0033684,
umls-concept:C0205314,
umls-concept:C0205463,
umls-concept:C0679622,
umls-concept:C1419366,
umls-concept:C1442792,
umls-concept:C1882726,
umls-concept:C2266866
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pubmed:issue |
6
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pubmed:dateCreated |
2003-3-20
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pubmed:abstractText |
The binding activity of a novel regucalcin gene promoter region-related protein (RGPR-p117) to the TTGGC sequence of the rat regucalcin gene promoter region was investigated. The expression of RGPR-p117 mRNA was seen in the liver tissues of male and female rats. The sexual difference of this expression was not found. Liver RGPR-p117 mRNA expression was not changed with increasing age (1-50 weeks old), and its expression was not altered by fasting or refeeding. Nuclear factor I-A1 (NF1-A1) has been identified to be a transcription factor in stimulating the rat regucalcin gene promoter activity (Misawa and Yamaguchi [2002a] J Cell Biochem 84:795-802]. Recombinant nuclear factor I-A1 (NF1-A1) and RGPR-p117 proteins were used gel mobility shift assay. RGPR-p117 could not bind to TTGGC motif of the sequence between -525 and -504, which has been defined as a functional promoter element II-b. NF1-A1 was specifically bound to the II-b oligonucleotide. Moreover, RGPR-p117 was not bound to the II-b oligonucleotide in the presence of NF1-A1 or rat liver nuclear protein. The binding of NF1-A1 to the II-b oligonucleotide was not altered in the presence of RGPR-p117. This study demonstrates that RGPR-p117 mRNA, is expressed stably for physiologic change in rat liver, and that recombinant the protein does not directly bind to the TTGGC motif in rat regucalcin gene promoter.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Rgn protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Rgpr protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfotransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/alcohol sulfotransferase,
http://linkedlifedata.com/resource/pubmed/chemical/heat shock transcription factor
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0730-2312
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pubmed:author |
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pubmed:copyrightInfo |
Copyright 2003 Wiley-Liss, Inc.
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
88
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1092-100
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:12647292-Animals,
pubmed-meshheading:12647292-Base Sequence,
pubmed-meshheading:12647292-Calcium-Binding Proteins,
pubmed-meshheading:12647292-DNA-Binding Proteins,
pubmed-meshheading:12647292-Female,
pubmed-meshheading:12647292-Gene Expression Regulation,
pubmed-meshheading:12647292-Genes, Regulator,
pubmed-meshheading:12647292-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:12647292-Liver,
pubmed-meshheading:12647292-Male,
pubmed-meshheading:12647292-Molecular Sequence Data,
pubmed-meshheading:12647292-Promoter Regions, Genetic,
pubmed-meshheading:12647292-Protein Binding,
pubmed-meshheading:12647292-RNA, Messenger,
pubmed-meshheading:12647292-Rats,
pubmed-meshheading:12647292-Rats, Wistar,
pubmed-meshheading:12647292-Recombinant Proteins,
pubmed-meshheading:12647292-Sequence Analysis, DNA,
pubmed-meshheading:12647292-Sulfotransferases,
pubmed-meshheading:12647292-Transcription Factors
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pubmed:year |
2003
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pubmed:articleTitle |
Novel protein RGPR-p117: the gene expression in physiologic state and the binding activity to regucalcin gene promoter region in rat liver.
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pubmed:affiliation |
Laboratory of Endocrinology and Molecular Metabolism, Graduate School of Nutritional Sciences, University of Shizuoka, Shizuoka, Japan. yamaguch@fsn1.u-shizuoka-ken.ac.jp
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pubmed:publicationType |
Journal Article
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