Effects of Transforming Growth Factor-β1 on Decorin Expression by Undifferentiated Osteoblastic Cells

Abstract

Decorin is the predominant proteoglycan isolated from bone of several animal species. Bone matrix decorin appears to bind transforming growth factor β (TGF-β) and enhances its bioactivity. TGF-β is stored in bone matrix in abundant amounts and modulates the synthesis of bone matrix proteins by osteoblasts. Thus it appears to play a role in regulation of bone formation during the bone remodeling process. The effect of TGF-β on decorin expression in bone cells has been evaluated in murine osteoblastic cells, but the results are divergent depending on the experimental conditions and cell types used. The present study investigated the effect of TGF-βl on the expression of decorin mRNA in two clonal rat osteoblastic cell lines with different stages of differentiation, ROS-C26 (C26) and ROS-C20 (C20); C26 is a potential osteoblast precursor cell line that is also capable of differentiating into muscle cells and adipocytes; C20 is a more differentiated osteoblastic cell line.