Regulation of collagen metabolism and cell growth by epidermal growth factor and ascorbate in cultured human skin fibroblasts
Article first published online: 3 MAR 2005
European Journal of Biochemistry
Volume 173, Issue 2, pages 261–267, April 1988
How to Cite
HATA, R.-i., SUNADA, H., ARAI, K., SATO, T., NINOMIYA, Y., NAGAI, Y. and SENOO, H. (1988), Regulation of collagen metabolism and cell growth by epidermal growth factor and ascorbate in cultured human skin fibroblasts. European Journal of Biochemistry, 173: 261–267. doi: 10.1111/j.1432-1033.1988.tb13993.x
- Issue published online: 3 MAR 2005
- Article first published online: 3 MAR 2005
- (Received October 26, 1987/January 11, 1988) – EJB 87 1190
Epidermal growth factor (2–50 ng/ml), prepared from mouse submaxillary glands, stimulated growth and the synthesis of non-collagenous proteins and hyaluronic acid, but inhibited collagen synthesis in cultured human skin fibroblasts, both stimulation and inhibition being dose-dependent. All these effects may be intrinsic functions of the epidermal growth factor molecule, because these effects were cancelled by the co-presence of antiserum specific for epidermal growth factor and because they were also observed following the addition of human epidermal growth factor produced urogastrone cDNA. On the other hand, l-ascorbate (vitamin C) stimulated growth and collagen synthesis, as well as synthesis of non-collagenous proteins, with no significant effect on hyaluronic acid synthesis.
Co-presence of epidermal growth factor and ascorbate gave additive effects on growth and protein synthesis of the cells. These results suggest that the two growth-promoting factors, epidermal growth factor and l-ascorbate, modulate metabolism of extracellular matrix components as well as cell growth in a quite different manner in human skin fibroblasts.