Abstract
Summary
The effects of triamcinolone acetonide on fibroblasts isolated from normal dermis and keloids were tested by measuring cell division, DNA content, collagen synthesis, and prolyl hydroxylase activity following steroid treatment. In the present study, the DNA content and cell division of normal fibroblasts were inhibited by 50 μg/ml steroid to a greater extent than keloid fibroblasts. Collagen synthesis was inhibited by triamcinolone acetonide in a similar, dose-dependent manner in both keloid-derived and normal skin fibroblasts. Although triamcinolone acetonide decreased prolyl hydroxylase in all cultures, this inhibition did not correlate with the steroid-induced inhibition of collagen synthesis. In addition, triamcinolone acetonide increased the specific activity of radioactive proline in the amino acid cell pool 37–38% in all cultures. Triamcinolone acetonide enhanced TCA-soluble, [14C]hydroxyproline production in both cell types, suggesting that collagen degradation was increased by this corticosteroid.
The authors wish to thank Rae Spivey for her excellent clerical assistance in the preparation of this manuscript and Ira Flax, M.D., for his help with the prolyl hydroxylase analyses.
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