In Vitro Inhibition of Cell Growth, Collagen Synthesis, and Prolyl Hydroxylase Activity by Triamcinolone Acetonide

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Abstract
The effects of triamcinolone acetonide [TA] 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. The DNA content and cell division of normal fibroblasts were inhibited by 50 .mu.g/ml steroid to a greater extent than keloid fibroblasts. Collagen synthesis was inhibited by TA in a similar, dose-dependent manner in both keloid-derived and normal skin fibroblasts. Although TA decreased prolyl hydroxylase in all cultures, this inhibition did not correlate with the steroid-induced inhibition of collagen synthesis. TA increased the specific activity of radioactive proline in the amino acid cell pool 37-38% in all cultures. TA enhanced TCA[trichloroacetic acid]-soluble, [14C]hydroxyproline production in both cell types, suggesting that collagen degradation was increased by this corticosteroid.