In the dermis, fibroblast plays an important role in the turnover of the dermal extracellular matrix. Collagen I and III, which are the most important dermal proteins of the extracellular matrix, function as a stabilizing scaffold of dermal connective tissues, as well as a regulator of differentiation and migration of dermal cells. In this study, we investigated the effect of various nutrients, such as ascorbic acid, silicon, Fe, lysine and proline which function as cofactors or building blocks on collagen synthesis. When the physiological concentrations of ascorbic acid (0-100 ${mu}M$), silicon (0-50 ${mu}M$), Fe (0-50 ${mu}M$), lysine (0-150 ${mu}M$) and proline (0-300 ${mu}M$) were treated at HS27 for either 3 or 5 days, 5 day treatment of ascorbic acid at the low concentration (5-10 ${mu}M$) increased the expression of collagen I and III protein by 115-1300% without increasing cell proliferation. 3 or 5 days treatment of Fe increased the expression of collagen I and III proteins up to 323% in parallel with cell proliferation by 164%. However, cell proliferation and expression of collagen I and III protein in silicon treated HS27 did not differ. Proline and lysine only increased cell proliferation up to 247.9%. Taken together, we demonstrate that the physiological concentrations of ascorbic acid and Fe enhance the expression of collagen I and III protein for treatment of 3 or 5 days.