Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
50
pubmed:dateCreated
2000-1-13
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
274
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
35703-10
pubmed:dateRevised
2008-11-21
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
pubmed:year
1999
pubmed:articleTitle
Separate cis-acting DNA elements control cell type- and tissue-specific expression of collagen binding molecular chaperone HSP47.
pubmed:affiliation
Department of Molecular and Cellular Biology, Institute for Frontier Medical Sciences, Kyoto University, Kyoto 606-8507, Japan.
pubmed:publicationType
Journal Article