Transformation of glucocorticoid receptors bound to the antagonist RU 486: effects of alkaline phosphatase.
Transformation of glucocorticoid receptors bound to the antagonist RU 486: effects of alkaline phosphatase.
复制标题
与拮抗剂 RU 486 结合的糖皮质激素受体的转化：碱性磷酸酶的作用。
DOI：
10.1021/bi00486a026
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发表时间：
1990
期刊：
影响因子：
2.9
通讯作者：
Wolfe,KA
中科院分区：
文献类型：
--
作者：
Gruol,DJ;Wolfe,KA
Revised Manuscript Received April 25, 1990 abstract: RU 486 is a synthetic steroid that binds avidly to glucocorticoid receptors without promoting their transformation into activated transcription factors. A significant part of this behavior has been shown to be due to a failure of the RU 486 bound receptor to be efficiently released from a larger (sedimenting at 8-9 S) multimeric complex containing the 90-kDa heat shock protein. Our studies have found that in vitro at 15 C the RU 486-receptor was slowly released from the 8-9S complex and converted into a DNA binding protein by a process that could be blocked by sodium fluoride. Moreover, this transition was significantly accelerated by treatment with alkaline phosphatase. High-resolution anion-exchange chro-matography showed that the profile of receptor subspecies released from the 8-9S complex (in the absence of phosphatase treatment) was different for the RU 486 bound receptor when compared to the receptor occupied by the agonist triamcinolone acetonide. Production of the earliest eluting receptor form (peak A) was inhibited withRU 486. Peak A had previously been shown to be the predominant form of the receptor possessing a capacity to bind DNA. Treatment of the RU 486-receptor with alkaline phosphatase increased the formation of thepeak A subspecies as well as the capacity of receptor to bind DNA-cellulose. Taken together, the results indicate that phosphorylation of the receptor or a tightly bound factor contributes to defining the capacitywith which individual steroids can promote dissociation of the 8-9S complex and conversion of the glucocorticoid receptor into a DNA-binding protein. e steroid antagonist RU 4861 binds avidly to glucocorticoid receptors (Jung-Testas & Baulieu, 1983; Bourgeois et al., 1984) but does not provoke the response normally manifested by agonist hormones at the level of gene expression (Baulieu, 1987; Becker et al., 1986; Chasserot-Golaz & Beck, 1984). This behavior is indicative of the antagonist’s failure to promote one or more critical steps in the receptor’s transition into an activated transcription factor (Baulieu et al., 1989).
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完整细胞中糖皮质激素受体的激动剂依赖性磷酸化和核去磷酸化。
DOI：
--
发表时间：
1989
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Ortí,E;Mendel,DB;Smith,LI;Munck,A
通讯作者：
Munck,A
转化的糖皮质激素受体由具有不同 DNA-纤维素结合能力的多个亚种组成。
影响因子：
2.9
作者：
Gruol,DJ;Wolfe,KA
通讯作者：
Wolfe,KA
从大鼠肝细胞质中鉴定出一种增强糖皮质激素受体激活的蛋白质。
DOI：
10.1042/bj2560047
发表时间：
1988
期刊：
The Biochemical journal
影响因子：
--
作者：
JohnL . Tymoczko;Alison L. Unger;Jennifer L. Colby
通讯作者：
Jennifer L. Colby
鸡胚神经视网膜无细胞胞质中糖皮质激素受体的转化：转化过程中受体复合物的大小和电荷的变化表明这是一个多阶段的过程。
DOI：
--
发表时间：
1988
期刊：
Journal of Steroid Biochemistry
影响因子：
--
作者：
S. Ben;A. Chrambach
通讯作者：
A. Chrambach
小牛肠道碱性磷酸酶、磷酸酶抑制剂和磷酸化化合物对糖皮质激素受体复合物激活率的影响。
影响因子：
2.9
作者：
Barnett,CA;Schmidt,TJ;Litwack,G
通讯作者：
Litwack,G