Stimulation of arylsulfotransferase activity by progestins in human endometrium in vitro.
Stimulation of arylsulfotransferase activity by progestins in human endometrium in vitro.
复制标题
孕激素在体外刺激人子宫内膜中的芳基磺基转移酶活性。
DOI：
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发表时间：
1981
影响因子：
5.8
通讯作者：
H. Liu
中科院分区：
文献类型：
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作者：
L. Tseng;H. Liu
在两种培养系统中研究了黄体酮对人子宫内膜雌二醇（E2）硫酸化率的影响：1)完整子宫内膜组织碎片和2)离体子宫内膜上皮腺和间质细胞。将人子宫内膜组织片段在存在和不存在黄体酮(P)的培养基中培养24-48小时。在存在过量底物和辅助因子（腺苷-3'-磷酸-5'-硫酸磷酸）的情况下，通过测量E2到E2-3硫酸盐（E2S）的转化率来测定组织匀浆细胞质中的芳基硫转移酶活性。经磷处理后，酶活性受到刺激，活性的增加与磷剂量和培养时间有关。P对子宫内膜雌二醇脱氢酶活性的刺激，在之前的一系列出版物中都有报道，在本研究中也很明显。在有和无醋酸甲羟孕酮（MPA）的培养基中分别培养人子宫内膜腺上皮细胞和间质细胞。将培养的细胞与E2 （0.4 ~ 0.6 nM）孵育2 h，经MPA培养的所有增生腺上皮细胞中硫酸雌激素、[硫酸雌酮（E1S）和E2S]的形成均显著增加。然而，在分泌性子宫内膜的基质细胞和腺上皮细胞中，MPA对硫酸化率没有明显影响。在这些培养细胞中E2的氧化也受到P的影响，但没有影响到硫酸化的程度。这些结果表明子宫内膜的芳基硫转移酶起源于腺上皮细胞，并可被黄体酮刺激。
The effect of progestin on the rate of estradiol (E2) sulfurylation in human endometrium was studied in two culture systems: 1) in intact endometrial tissue fragments and 2) in isolated endometrial epithelial glands and stromal cells. Human endometrial tissue fragments were cultured in medium in the presence and absence of progesterone (P) for 24-48 h. The arylsulfotransferase activity was determined in the cytosol of the tissue homogenate by measuring the rate of conversion of E2 to E2-3 sulfate (E2S) in the presence of an excess amount of substrate and cofactor (adenosine-3'-phosphate-5'-phosphosulfate). The enzyme activity was found to be stimulated in the sample cultured with P. The increase in activity correlated with the dose of P and period of culture. Stimulation of endometrial estradiol dehydrogenase activity by P, which has been reported in a series of previous publications, was also evident in the current study. Human endometrial glandular epithelial and stromal cells were cultured separately in medium in the presence and absence of medroxyprogesterone acetate (MPA). The cultured cells were incubated with E2 (0.4-0.6 nM) for 2 h. The formation of estrogen sulfates, [estrone sulfate (E1S) and E2S] was greatly increased in all the proliferative glandular epithelial cells cultured with MPA. However, the rate of sulfurylation was not appreciably affected by MPA in stromal cells and in glandular epithelial cells from secretory endometrium. The oxidation of E2 in these cultured cells was also influenced by P but not to the extent of sulfurylation. These results indicate that arylsulfotransferase in endometrium originates from glandular epithelial cells and can be stimulated by progestin.