Source:http://linkedlifedata.com/resource/pubmed/id/10585450
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
50
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pubmed:dateCreated |
2000-1-13
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pubmed:abstractText |
HSP47 is a collagen-binding heat shock protein and is assumed to act as a molecular chaperone in the biosynthesis and secretion of procollagen. As the synthesis of HSP47 is closely correlated with that of collagen in various cell lines and tissues, we performed a promoter/reporter assay using HSP47-producing and nonproducing cells. 280 base pairs (bp(s)) of upstream promoter were shown to be necessary for the basal expression but not to be enough for the cell type-specific expression. When the first and the second introns were introduced downstream of this 280-bp region, marked up-regulation of the reporter activity was observed in HSP47-producing cells but not in nonproducing cells. This was confirmed in transgenic mice by staining the lacZ gene product under the control of the 280-bp upstream promoter and the introns. Staining was observed in skin, chondrocytes, precursor of bone, and other HSP47/collagen-producing tissues. A putative Sp1-binding site at -210 bp in the promoter, to which Sp3 and an unidentified protein bind, was shown to be responsible for this up-regulation when combined with the introns. However no difference in the binding to this probe was observed between HSP47-producing and nonproducing cells. The responsible region for cell type-specific up-regulation was found to be located in a 500-bp segment in the first intron. On electrophoresis mobility shift assay using this 500-bp probe, specific DNA-protein complexes were only observed in HSP47-producing cell extracts. These results suggest that two separate elements are necessary for the cell type-specific expression of the hsp47 gene; one is a putative Sp1-binding site at -210 bp necessary for basal expression, and the other is a 500-bp region within the first intron, required for cell type-specific 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/Collagen,
http://linkedlifedata.com/resource/pubmed/chemical/HSP47 Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Luciferases,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SERPINH1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Serpinh1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/beta-Galactosidase
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
274
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
35703-10
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:10585450-3T3 Cells,
pubmed-meshheading:10585450-Animals,
pubmed-meshheading:10585450-Collagen,
pubmed-meshheading:10585450-Embryonic and Fetal Development,
pubmed-meshheading:10585450-Gene Expression Regulation,
pubmed-meshheading:10585450-Gene Expression Regulation, Developmental,
pubmed-meshheading:10585450-Genomic Library,
pubmed-meshheading:10585450-HSP47 Heat-Shock Proteins,
pubmed-meshheading:10585450-HeLa Cells,
pubmed-meshheading:10585450-Heat-Shock Proteins,
pubmed-meshheading:10585450-Humans,
pubmed-meshheading:10585450-Introns,
pubmed-meshheading:10585450-Luciferases,
pubmed-meshheading:10585450-Mice,
pubmed-meshheading:10585450-Mice, Inbred C3H,
pubmed-meshheading:10585450-Mice, Inbred C57BL,
pubmed-meshheading:10585450-Mice, Transgenic,
pubmed-meshheading:10585450-Organ Specificity,
pubmed-meshheading:10585450-Promoter Regions, Genetic,
pubmed-meshheading:10585450-Recombinant Fusion Proteins,
pubmed-meshheading:10585450-Restriction Mapping,
pubmed-meshheading:10585450-Transfection,
pubmed-meshheading:10585450-Tumor Cells, Cultured,
pubmed-meshheading:10585450-beta-Galactosidase
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pubmed:year |
1999
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pubmed:articleTitle |
Separate cis-acting DNA elements control cell type- and tissue-specific expression of collagen binding molecular chaperone HSP47.
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pubmed:affiliation |
Department of Molecular and Cellular Biology, Institute for Frontier Medical Sciences, Kyoto University, Kyoto 606-8507, Japan.
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pubmed:publicationType |
Journal Article
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