Abstract
HSP47 is a 47-kDa collagen-binding heat shock protein, the expression of which is always correlated with that of collagens in various cell lines. We examined the effects of TGF-β1, which is reported to induce the collagen genes, on the expression of HSP47 in mouse osteoblast MC3T3-E1 cells. Treatment of the cells with 5 ng/ml TGF-β1 for 24 h increased the level of HSP47 mRNA three-fold. Dose-dependent induction by TGF-β1 was observed for both HSP47 mRNA and collagen α1(I) mRNA, and actinomycin D inhibited this increase of HSP47 mRNA. To elucidate the TGF-β1 responsive element(s) in the mouse HSP47 gene, we generated a series of 5′-deletion promoters fused to luciferase reporter constructs. Transient transfection assays showed that TGF-β1 induced 4-6 fold the promoter activity of a region approximately −5.5 kbp upstream of the HSP47 gene. Two upstream regions, −3.9 to −2.7 kbp and −280 to −50 bp were shown to be involved in the activation in response to TGF-β1 treatment.
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