人子宮内膜および内膜癌における性ステロイドホルモンレセプターに関する研究
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The estrogen receptor (ER) and progesterone receptor (PR) were investigated in normal uterine endometrium and uterine adenocarcinoma of human subjects. In the normal endometrial cytosols, either estradiol-17β (E<SUB>2</SUB>) or progesterone (P) bound to 8S proteins and the kinetic analysis by charcoal adsorption showed Kd (E<SUB>2</SUB>) = 2.5×10<SUP>-9</SUP>M and Kd (P) = 2.0×10<SUP>-9</SUP>M.<BR>In the cytosols of adenocarcinomas, Kd (E<SUB>2</SUB>) values were ranged from 2.5-0.6×10<SUP>-9</SUP>M in the presence of E<SUB>2</SUB>-8S protein binding, Kd (P) value in the presence of P-8S protein binding was the same as that in the normal endometrial cytosol, but Kd (P) value was 1.3×10<SUP>-8</SUP>M in the absence of P-8S protein. Even when E<SUB>2</SUB>-8S existed, P-8S was not always detected, but whenever P-8S existed, E<SUB>2</SUB>-8S was detected. These results indicate that the ER of the adenocarcinoma is altered in quality, resulting in no synthesis of PR in some cases.<BR>Steroid specificity of PR in the estrogen-primed endometrial cytosol was studied by kinetics. All steroids demonstrated competitive inhibition for PR binding. Especially did studies of the steroids related to progesterone demonstrate that the plane of ring A/B, _??_<SUP>4</SUP> double bond and C-3, 20 ketones were important for PR binding. The binding of PR was tolerated when the side chain of the acetyl group was replaced by the 17α-ethynyl-17β-hydroxy group. And the binding affinities of most steroids were related to their biological activities.<BR>In the menstrual cycle, the maximum binding site (Bm) of the steroid receptor was investigated by kinetics. The results were as follows; in the proliferative phase, Bm (E<SUB>2</SUB>) in creased from the early to the middle, and decreased in the late. Bm (E<SUB>2</SUB>) increased again in the ovulatory period, and in the secretory phase, Bm (E<SUB>2</SUB>) increased slightly in the middle and decreased in the late. Bm (P) also demonstrated almost the same alteration of Bm (E<SUB>2</SUB>).<BR>The nuclear binding quantities of steroids were measured by exchange assay. Nuclear E<SUB>2</SUB> bindings were at almost the same level in proliferative and secretory phases of the menstrual cycle, but nuclear P binding was detected slightly in the secretory phase and much less than nuclear E<SUB>2</SUB> bindings. These results suggested that the nuclear P-receptor may be metabolized rapidly in vivo and the nuclear E<SUB>2</SUB>-receptor may stay longer.
- 一般社団法人 日本内分泌学会の論文
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