Studies on the pathogenesis of the incomplete forms of androgen resistance in man.
The affinity and turnover of the specific dihydrotestosterone binding protein have been 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 amount of dihydrotestosterone binding in the 4 mutant cell strains is low, both the affinity of the protein for dihydrotestosterone 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 two disorders affect the synthesis of the dihydrotestosterone binding protein.
D013734:Androgen-Insensitivity Syndrome / Q000378:metabolism; D002352:Carrier Proteins / Q000096:biosynthesis; D002478:Cells, Cultured; D013196:Dihydrotestosterone / Q000378:metabolism; D012734:Disorders of Sex Development / Q000209:etiology / Q000378:metabolism*; D005260:Female; D006801:Humans; D008297:Male; D011944:Receptors, Androgen / Q000378:metabolism*; D011987:Receptors, Steroid / Q000378:metabolism*
D002352:Carrier Proteins; D011944:Receptors, Androgen; D011987:Receptors, Steroid; D013196:Dihydrotestosterone