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J Biol Chem, Vol. 274, Issue 50, 35703-35710, December 10, 1999

Separate Cis-acting DNA Elements Control Cell Type- and Tissue-specific Expression of Collagen Binding Molecular Chaperone HSP47^*

Hiromi Hirata^§, Isao Yamamura, Kunihiko Yasuda, Akio Kobayashi^¶, Norihiro Tada^¶, Misao Suzuki, Kazunori Hirayoshi, Nobuko Hosokawa^§, and Kazuhiro Nagata^§**

From the  Department of Molecular and Cellular Biology, Institute for Frontier Medical Sciences, Kyoto University, Kyoto 606-8507, ^§ Core Research for Evolutional Science and Technology (CREST), Japan Science and Technology Corporation (JST), ^¶ Molecular Biology Laboratory, Medicinal Research Laboratories, Taisho Pharmaceutical Co., Ltd., Oomiya, 330-0031, and  Center for Animal Resources and Development, Kumamoto University, Kumamoto 860-0811, Japan

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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