Studies on the pathogenesis of the incomplete forms of androgen resistance in man.
Studies on the pathogenesis of the incomplete forms of androgen resistance in man.
复制标题
人类不完全形式雄激素抵抗的发病机制的研究。
DOI：
10.1210/jcem-45-6-1137
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发表时间：
1977
期刊：
影响因子：
--
通讯作者：
Jean D. Wilson
中科院分区：
文献类型：
--
作者：
J. Griffin;Jean D. Wilson
特异性二氢睾酮结合蛋白的亲和力和周转率已在从来自各种对照受试者和来自4名患有由于雄激素抵抗导致的不完全遗传性男性假两性畸形（不完全睾丸女性化和赖芬斯坦综合征）的生殖器皮肤培养的成纤维细胞中进行了评估。尽管在4种突变细胞株中结合的二氢睾酮的量低，但通过半最大结合发生时的浓度（平均0.2nM）评估的蛋白质对二氢睾酮的亲和力和结合蛋白的转换（平均半衰期为11- 13小时）均在正常范围内。由于未检测到定性异常，因此这些数据表明这两种疾病中的突变影响双氢睾酮结合蛋白的合成。
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.