Source:http://linkedlifedata.com/resource/pubmed/id/16309856
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:dateCreated |
2006-2-21
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| pubmed:abstractText |
The present study was undertaken to characterize structure-function relationships of the rat galectin-3 gene promoter especially focusing on the promoter binding proteins included in livers injured with CCl4. Transcription start site determination identified a 66-nucleotide-long exon 1 of this gene. Transient expression analysis using a reporter luciferase gene assigned a region between -161 and -15 to the proximal promoter within the 1-kb region flanking the 5'-end of exon 1. The rat galectin-3 gene promoter possesses a Runx2 binding site and inverted repeats of Sp1 binding motifs in separate regions downstream from -117 as structures resembling those of the mouse galectin-3 gene promoter. The -161/-118 region bound two different proteins. One is a novel protein, a rat version of Purbeta that binds to a guanine nucleotide pair at -145 and -144 to modulate constitutive galectin-3 gene transcription. Southwestern blot analysis using the -161/-118 ligand revealed a signal of a 50-kDa protein in liver nuclear extracts from rats 48-h post-treatment with CCl4, but not in those from Ac2F cells and normal rat livers. The inducible nature of this protein suggested its distinctive role in galectin-3 induction in a liver injured with CCl4. E-box and peroxisome proliferator response element-like motifs reside on separate DNA strands from -140 to -135. Contribution of this segment to the regulation of galectin-3 gene transcription under pathological conditions was suggested, since a DNA ligand with the two motifs simultaneously mutagenized at -136 and -137 was not bound by the 50-kDa protein.
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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/Carbon Tetrachloride,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Galectin 3,
http://linkedlifedata.com/resource/pubmed/chemical/Luciferases,
http://linkedlifedata.com/resource/pubmed/chemical/Purbeta protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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| pubmed:status |
MEDLINE
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| pubmed:month |
Feb
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| pubmed:issn |
0378-1119
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
15
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| pubmed:volume |
367
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
46-55
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| pubmed:dateRevised |
2008-11-21
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| pubmed:meshHeading |
pubmed-meshheading:16309856-Animals,
pubmed-meshheading:16309856-Base Sequence,
pubmed-meshheading:16309856-Binding Sites,
pubmed-meshheading:16309856-Carbon Tetrachloride,
pubmed-meshheading:16309856-Carcinoma, Hepatocellular,
pubmed-meshheading:16309856-Carrier Proteins,
pubmed-meshheading:16309856-Cell Line, Tumor,
pubmed-meshheading:16309856-DNA-Binding Proteins,
pubmed-meshheading:16309856-Electrophoretic Mobility Shift Assay,
pubmed-meshheading:16309856-Exons,
pubmed-meshheading:16309856-Galectin 3,
pubmed-meshheading:16309856-Genes, Reporter,
pubmed-meshheading:16309856-Liver,
pubmed-meshheading:16309856-Liver Neoplasms,
pubmed-meshheading:16309856-Luciferases,
pubmed-meshheading:16309856-Male,
pubmed-meshheading:16309856-Molecular Sequence Data,
pubmed-meshheading:16309856-Promoter Regions, Genetic,
pubmed-meshheading:16309856-Rats,
pubmed-meshheading:16309856-Rats, Wistar,
pubmed-meshheading:16309856-Sequence Deletion,
pubmed-meshheading:16309856-Sequence Homology, Amino Acid,
pubmed-meshheading:16309856-Structure-Activity Relationship,
pubmed-meshheading:16309856-Time Factors,
pubmed-meshheading:16309856-Transcription, Genetic,
pubmed-meshheading:16309856-Transcription Factors,
pubmed-meshheading:16309856-Transcription Initiation Site
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| pubmed:year |
2006
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| pubmed:articleTitle |
The galectin-3 gene promoter binding proteins in the liver of rats 48-h post-treatment with CCl4.
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| pubmed:affiliation |
The Department of Biochemistry, Toyama Medical and Pharmaceutical University School of Medicine, 2630 Sugitani, Toyama 930-0194, Japan.
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| pubmed:publicationType |
Journal Article
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