Studies on the Pathogenesis of the Incomplete Forms of Androgen Resistance in Man

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Abstract
The affinity and turnover of the specific dihydrotestosterone [DHT] binding protein were assessed in fibroblasts cultured from genital skin from a variety of control subjects and from 4 patients with incomplete hereditary male pseudohermaphroditism due to androgen resistance (incomplete testicular feminization and Reifenstein syndrome). Whereas the amound of DHT binding in the 4 mutant cell strains is low, both the affinity of the protein for DHT as assessed by the concentration at which half-maximal binding occurs (averaging 0.2 nM) and the turnover of the binding protein (average half-life of 11-13 h) are within the normal range. Since no qualitative abnormality could be detected, these data suggest that the mutations in these 2 disorders affect the synthesis of the DHT binding protein.