Evidence for an androgen binding protein in the testis of a teleost fish ( Salmo gairdneri R.): A potential marker of sertoli cell function

A factor binding tritiated testosterone was detected using “steady-state” polyacrylamide-gel electrophoresis, in rainbow trout genital tract. It migrated with a R f identical to that of rat ABP. This binding was thermolabile, and was competitively inhibited by unlabelled testosterone. The steroid binding protein was found in cytosols from trout testes which had been previously perfused to avoid blood contamination, trout seminal plasma and in testicular explants incubation media. Using a quantitative assay and a Scatchard analysis, 25–50 pmol binding sites per gram gonad were found in testis cytosol. Binding affinity constant for testosterone in the various samples was close to 4 × 10 8 M −1. The dissociation of steroid-protein complex was rapid ( t 1 2 ≈ 1.5 min). Hormonal specificity was studied by the competition of 3H-T binding with several concentrations of unlabelled competitors and the following order for affinities was obtained: dihydrotestosterone ≈ androstenedione > testosterone > oestradiol > 17α, 20β DHP > 11KT > cyproterone acetate > cortisol. High testicular cytosol and seminal plasma concentrations and apparent in vitro production indicate that the testis may synthesize an ABP-like protein in the trout. Such a factor would provide a unique marker of Sertoli cell activity and regulation in various physiological or experimental situations.