The androgen resistance syndromes are generally felt to be due to quantitative or qualitative abnormalities of the androgen receptor. Some patients with testicular feminization have no demonstrable fibroblast cytosol androgen binding, whereas others have androgen binding in cultured fibrobalsts that is thermolabile or fails to be stabilized by sodium molybdate. I describe here familial incomplete testicular feminization associated with reduced nuclear androgen retention. Fibroblasts, cultured from pubic skin biopsies of two phenotypic female 46XY siblings, were assayed for whole cell and nuclear uptake of [3H]dihydrotestosterone in dispersed, intact cells. Whole cell binding of [3H]dihydrotestosterone at 22°C in the patients' fibroblasts was in the normal range. However, no high affinity, saturable binding of [3H]dihydrotestosterone was demonstrable in crude nuclear pellets prepared from the patients' fibroblasts incubated at 37°C with the hormone. Incubating the patients' cells with [3H]methyltrienolone or examining the nuclear uptake of [3H]dihydrotestosterone in these cells at 22°C did not alter these findings. Although cytosol from the patients' cells revealed a quantitatively diminished 8S peak for [3H]dihydrotestosterone after centrifugation on sodium molybdate-containing sucrose gradients, there was no peak of 3H in the 4S region from 0.3 M KCl nuclear extracts of the patients' cells after they had been incubated with [3H]dihydrotestosterone at 37°C.
Charles Eil
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