PSPC1, NONO, and SFPQ are expressed in mouse sertoli cells and may function as coregulators of androgen receptor-mediated transcription
PSPC1, NONO, and SFPQ are expressed in mouse sertoli cells and may function as coregulators of androgen receptor-mediated transcription
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DOI：
10.1095/biolreprod.106.051136
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发表时间：
2006-09-01
影响因子：
3.6
通讯作者：
Kurihara, Yasuyuki
中科院分区：
文献类型：
--
作者：
Kuwahara, Sho;Ikei, Asako;Kurihara, Yasuyuki
在睾丸支持细胞中，雄激素受体调控的基因转录在维持精子发生中起着不可或缺的作用。雄激素受体活性受许多与雄激素受体相关的辅助调节因子调节。非POU结构域八聚体结合蛋白（NONO）是含DBHS蛋白的一员，与雄激素受体复合，并作为受体的共激活剂发挥作用。Paraspeckle蛋白1 α亚型（PSPC 1，以前称为PSP 1）和剪接因子，脯氨酸和谷氨酰胺丰富（SFPQ，以前称为PSF），其他成员的DBHS含有蛋白质，也发现在雄激素受体复合物，这表明这些DBHS含有蛋白质可以协同调节雄激素受体介导的基因转录。我们证明了PSPC 1，NONO和SFPQ在Sertoli细胞系TTE 3中共表达，并相互作用。使用含有雄激素应答元件和荧光素酶基因的构建体评估含DBHS蛋白对转录活性的影响。结果表明，所有含DBHS的蛋白都能激活雄激素受体介导的转录，PSPC 1是其中最有效的共激活因子。此外，我们证实了PSPC 1，NONO和SFPQ蛋白在成年小鼠睾丸切片的支持细胞中的存在。这些观察结果表明，PSPC1，NONO，和SFPQ形成复合物与对方在支持细胞，并可能调节雄激素受体介导的转录活性。
In Sertoli cells of testis, androgen receptor-regulated gene transcription plays an indispensable role in maintaining spermatogenesis. Androgen receptor activity is modulated by a number of coregulators which are associated with the androgen receptor. Non-POU-domain-containing, octamer binding protein (NONO), a member of the DBHS-containing proteins, complexes with androgen receptor and functions as a coactivator for the receptor. Paraspeckle protein 1 alpha isoform (PSPC1, previously known as PSP1) and Splicing factor, proline- and glutamine-rich (SFPQ, previously known as PSF), other members of the DBHS-containing proteins, are also found in androgen receptor complexes, suggesting that these DBHS-containing proteins may cooperatively regulate androgen receptor-mediated gene transcription. We demonstrated that PSPC1, NONO, and SFPQ are coexpressed in Sertoli cell line TTE3 and interact reciprocally. The effect of the DBHS-containing proteins on the transcriptional activity was assessed using the construct containing androgen-responsive elements followed by a luciferase gene. The results showed that all the DBHS-containing proteins activate androgen receptor-mediated transcription, and PSPC1 is the most effective coactivator among them. Furthermore, we confirmed the presence of PSPC1, NONO, and SFPQ proteins in Sertoli cells of adult mouse testis sections. These observations suggest that PSPC1, NONO, and SFPQ form complexes with each other in Sertoli cells and may regulate androgen receptor-mediated transcriptional activity.