Fortunati N, Fissore F, Fazzari A, Berta L, Giudici M, Frairia R
Dipartimento di Fisiopatologia Clinica, Università di Torino, Italy.
Steroids. 1991 Jun;56(6):341-6. doi: 10.1016/0039-128x(91)90058-4.
Sex steroid-binding protein receptor was detected on membranes prepared from human premenopausal endometrium. The binding of sex steroid-binding protein to membranes was specific, saturable, and high affinity. Scatchard analysis showed the presence of two binding sites at different affinities. The addition of estradiol (10(-8) M) did not produce any inhibition of binding; indeed, it resulted in a modification of binding characteristics. The demonstration of sex steroid-binding protein receptor on membranes of human premenopausal endometrium indicates that the expression of receptor on membranes is not an effect of estrogen over stimulation on target tissues. Estradiol could act as a modulating factor of the binding, probably reflecting the sensitivity of tissues to different steroids.
在人绝经前子宫内膜制备的膜上检测到性类固醇结合蛋白受体。性类固醇结合蛋白与膜的结合具有特异性、饱和性和高亲和力。Scatchard分析显示存在两个不同亲和力的结合位点。加入雌二醇（10^(-8) M）并未产生任何结合抑制；实际上，它导致了结合特性的改变。人绝经前子宫内膜膜上性类固醇结合蛋白受体的证明表明，膜上受体的表达不是雌激素对靶组织过度刺激的结果。雌二醇可能作为结合的调节因子，这可能反映了组织对不同类固醇的敏感性。
