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从猪卵巢卵泡液中纯化及鉴定一种促卵泡激素释放蛋白。

Purification and characterization of an FSH releasing protein from porcine ovarian follicular fluid.

作者信息

Vale W, Rivier J, Vaughan J, McClintock R, Corrigan A, Woo W, Karr D, Spiess J

出版信息

Nature. 1986;321(6072):776-9. doi: 10.1038/321776a0.

DOI:10.1038/321776a0
PMID:3012369
Abstract

A variety of hypophysiotropic peptides or proteins have been reported to be present in mammalian gonads. Inhibin, a hormone that under most circumstances selectively suppresses the secretion of follicle-stimulating hormone (FSH) but not luteinizing hormone (LH), has been isolated from the gonadal fluids of several species and characterized as a heterodimeric protein consisting of alpha- and beta-polypeptides associated by disulphide bonds. The complete amino-acid sequences of the precursors of porcine and human inhibin alpha-subunits and two distinct porcine inhibin beta-subunits (beta A and beta B) have been deduced from complementary DNA sequences. Gonadotropin releasing peptides have also been found in the gonad and have generally been shown to be active in radioreceptor assays for gonadotropin releasing hormone (GnRH) but to exhibit different chromatographic and immunological characteristics from those of GnRH. During our purification of inhibin from porcine follicular fluid, we noted fractions that could stimulate the secretion of FSH by cultured anterior pituitary cells. We report here the purification of an FSH releasing protein (FRP) and its characterization by SDS-polyacrylamide gel electrophoresis under non-reducing and reducing conditions and by partial sequence analysis. Our results indicate that porcine gonadal FRP is a homodimer consisting of two inhibin beta A-chains linked by disulphide bonds. FRP is highly potent (50% effective concentration (EC50) approximately 25 pM) in stimulating the secretion and biosynthesis of FSH but not of LH or any other pituitary hormone. In contrast to the effects of GnRH and other reported gonadal gonadotropin releasing fractions, the action of FRP is not mediated by GnRH receptors.

摘要

据报道,多种促垂体肽或蛋白质存在于哺乳动物性腺中。抑制素是一种在大多数情况下能选择性抑制促卵泡激素(FSH)分泌但不抑制促黄体生成素(LH)分泌的激素,已从几种物种的性腺液中分离出来,并被鉴定为一种由α和β多肽通过二硫键相连的异二聚体蛋白。猪和人抑制素α亚基前体以及两种不同的猪抑制素β亚基(βA和βB)的完整氨基酸序列已从互补DNA序列推导出来。促性腺激素释放肽也在性腺中被发现,并且通常在促性腺激素释放激素(GnRH)的放射受体测定中显示有活性,但在色谱和免疫特性上与GnRH不同。在我们从猪卵泡液中纯化抑制素的过程中,我们注意到一些组分能够刺激培养的垂体前叶细胞分泌FSH。我们在此报告一种促卵泡激素释放蛋白(FRP)的纯化及其在非还原和还原条件下通过SDS-聚丙烯酰胺凝胶电泳以及部分序列分析的表征。我们的结果表明,猪性腺FRP是一种由两个通过二硫键相连的抑制素βA链组成的同二聚体。FRP在刺激FSH的分泌和生物合成方面具有高效性(50%有效浓度(EC50)约为25 pM),但对LH或任何其他垂体激素无此作用。与GnRH和其他报道的性腺促性腺激素释放组分的作用相反,FRP的作用不是由GnRH受体介导的。

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Purification and characterization of an FSH releasing protein from porcine ovarian follicular fluid.从猪卵巢卵泡液中纯化及鉴定一种促卵泡激素释放蛋白。
Nature. 1986;321(6072):776-9. doi: 10.1038/321776a0.
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