Symposium
Binding of androgens and progestins in the human testis

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Abstract

Receptor-like androgen binding has been studied in normal human testis tissue and human testicular tumours. In cytosol an exchange assay with [3H]-methyltrienolone ([3H]-R 1881) has been used. Determination of nuclear binding sites was performed by a [3H]-testosterone exchange method. In normal testis cytosol a concentration of 119 ± 60 fmol/mg protein low-capacity high-affinity, heat labile androgen-binding activity was found. In only two out of five tumour specimens (seminomas) a relatively low (23–33 fmol/mg protein) exchange activity could be detected. Sucrose gradient centrifugation revealed two apparently separate peaks rather close to each other in the 4 S region. Incubation with 100-fold excess of radioinert progesterone resulted in a complete inhibition of [3H]-R 1881 binding at the position of one of the peaks. Androgen exchange activity was detected in the nuclear fractions of both normal and neoplastic tumour tissue. The highest nuclear exchange values were found in the tumour samples which had no detectable cytosol receptor activity.

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NORAD Research Fellow. Present address: Edirne Faculty of Medicine, Istanbul University, Fatih, Istanbul, Turkey.

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