Evidence for receptor-dependent response to dihydrotestosterone in cultured human fibroblasts

The effect of dihydrotestosterone on the production of proteins and collagen and the synthesis of DNA was studied in cultured fibroblasts obtained from a normal woman and from a patient with complete testicular feminization. The concentration of dihydrotestosterone binding sites in fibroblasts from vulvar skin of a normal woman and from perineal skin of a patient with complete testicular feminization was 35.9 +/- 1.7 fmoles/mg protein and 4.61 +/- 0.37 fmoles/mg protein, respectively. The apparent dissociation constant was 0.24 +/- 0.015 nM for fibroblasts from a normal woman and 0.21 +/- 0.031 nM for fibroblasts from a patient with complete testicular feminization. Fibroblasts grown to confluence were exposed to DHT in the concentrations of 10, 100 and 1000 ng/ml of the culture medium and cultures were maintained for up to six days thereafter. These hormone treatments brought about a significant elevation in the production of proteins and collagen by fibroblasts from a normal woman but failed to produce any perceivable changes in fibroblasts from a patient with complete testicular feminization. The synthesis of DNA in fibroblasts from either subject was unaffected by hormone treatment. These results suggest that augmented production of proteins and collagen in cultured human fibroblasts which follows stimulation by dihydrotestosterone occurs via a receptor system.