배양한 피부섬유아세포에서 bFGF와 TGF-β가 탄력소와 제1형 교원질 유전자의 전사조절에 미치는 영향

Abstract

Basic fibroblast growth factor(bFGF), a member of the fibroblast growth factor family, potentially induces increased vascular smooth muscle cell proliferation and decreased synthesis of collagen. A large number of extracellular matrix proteins including collagens, proteoglycans, elastin, fibronectin and fibrillins are produced by skin dermal fibroblasts. Skin fibroblasts have been extensively utilized for the diagnosis of connective tissue disease as well as aging. Elastin is one of the major extracellular matrix components of the dermis and plays an important role in providing elasticity and resilience of the skin. For investigation of the effect of bFGF on extracellular matrix homeostasis in the skin, we evaluated the expression of elastin and type I collagen from cultured dermal fibroblast at the transcriptional level. Using Northern blot analysis, transient transfection and CAT assay, we found that bFGF treatment caused decreases of elastin and type I collagen gene expression with dose and time dependent pattern. The effects of TGF-β, known as a potent fibrogenic cytokine, were inhibited by bFGF. Taken together, these results indicated that recombinant human bFGF decreased the elastin and type I collagen gene expression at pretranscriptional level and it showed antagonistic effect to TGF-β.