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抑制素:1985年关于作用及纯化的最新进展。

Inhibin: 1985 update on action and purification.

作者信息

de Jong F H, Robertson D M

出版信息

Mol Cell Endocrinol. 1985 Sep;42(2):95-103. doi: 10.1016/0303-7207(85)90096-6.

Abstract

Inhibin is a gonadal hormone, which exerts a specific negative feedback action on the pituitary secretion of follitropin (FSH) in male and female animals. The existence of inhibin was postulated over 60 years ago. Yet, until recently, little progress has been made in its isolation and characterisation. This lack of progress may be attributed to several factors: first, the use of a variety of assay systems of ill-defined specificity, secondly, the use of a variety of sources for unpurified inhibin, and thirdly, the inability of investigators to purify inhibin using classical purification procedures. During the last few years, and in particular during the last year, several publications on the isolation and characterisation of inhibin have appeared. This review attempts to place the various reports on the nature of inhibin into perspective. It is concluded that there are at least 2 classes of proteins with inhibin-like activity: a relatively large molecular weight material with apparent molecular mass between 40 and 70 kDa found in gonadal extracts and fluids, and a smaller material, with molecular mass between 5 and 20 kDa, found in seminal plasma. However, the observations that various purified seminal plasma inhibin preparations are either inactive in in vitro assays used to characterize gonadal inhibin or have been shown to be prostatic in origin suggest that they are unlikely to be involved in the gonadal regulation of FSH secretion. It has yet to be established if the purified gonadal inhibin preparations are the biological active forms involved in controlling FSH secretion in vivo.

摘要

抑制素是一种性腺激素,对雄性和雌性动物垂体促卵泡激素(FSH)的分泌发挥特定的负反馈作用。60多年前就有人提出了抑制素的存在。然而,直到最近,其分离和特性鉴定方面进展甚微。缺乏进展可能归因于几个因素:第一,使用了特异性不明确的多种检测系统;第二,使用了多种来源的未纯化抑制素;第三,研究人员无法使用经典纯化程序纯化抑制素。在过去几年中,特别是在去年,出现了几篇关于抑制素分离和特性鉴定的出版物。这篇综述试图对关于抑制素性质的各种报告进行综合分析。得出的结论是,至少有两类具有抑制素样活性的蛋白质:一类是在性腺提取物和体液中发现的相对大分子质量的物质,表观分子质量在40至70 kDa之间;另一类是在精浆中发现的较小物质,分子质量在5至20 kDa之间。然而,各种纯化的精浆抑制素制剂在用于鉴定性腺抑制素的体外试验中无活性,或者已被证明起源于前列腺,这些观察结果表明它们不太可能参与性腺对FSH分泌的调节。纯化的性腺抑制素制剂是否是体内控制FSH分泌的生物活性形式,还有待确定。

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