Isolation and partial characterization of follistatin: a single-chain Mr 35,000 monomeric protein that inhibits the release of follicle-stimulating hormone.
Isolation and partial characterization of follistatin: a single-chain Mr 35,000 monomeric protein that inhibits the release of follicle-stimulating hormone.
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DOI：
10.1073/pnas.84.23.8282
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发表时间：
1987-12
影响因子：
11.1
通讯作者：
Naoto Ueno;N. Ling;Shao-Yao Ying;F. Esch;Shunichi Shimasaki;R. Guillemin
中科院分区：
文献类型：
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作者：
Naoto Ueno;N. Ling;Shao-Yao Ying;F. Esch;Shunichi Shimasaki;R. Guillemin
通过肝素-Sepharose亲和层析、Sephacryl S-200凝胶过滤和多步高效液相色谱，从猪卵泡液中分离到一个Mr为35，000的具有促卵泡激素释放抑制活性的蛋白。分离的分子高度富集半胱氨酸，并且由单个多肽链组成。此外，它与先前表征的卵泡液中的促卵泡激素释放素没有序列同源性，促卵泡激素释放素是Mr 32，000的异二聚体蛋白质，具有促卵泡激素释放抑制活性。在大鼠垂体前叶单层培养系统中，该蛋白特异性地抑制卵泡刺激素的基础分泌，但不抑制黄体生成素的基础分泌，半最大有效剂量为2.5-6.0 ng/ml。还分离出另一种形式的Mr 32，000分子，其在卵泡液中的浓度低得多。它可能在糖基化或羧基末端截短方面不同于Mr 35，000形式。我们建议将该化合物命名为“卵泡抑素”，以表明其结构与Escherichin不同。
A Mr 35,000 protein with follicle-stimulating hormone release-inhibitory activity was isolated from porcine ovarian follicular fluid by heparin-Sepharose affinity chromatography, gel filtration on Sephacryl S-200, and multiple steps of high-performance liquid chromatography. The isolated molecule is highly enriched in cysteines and is composed of a single polypeptide chain. In addition, it has no sequence homology with the previously characterized follicular fluid inhibins, which are heterodimeric proteins of Mr 32,000 with follicle-stimulating hormone release-inhibiting activity. This protein specifically inhibits the basal secretion of follicle-stimulating hormone, but not that of luteinizing hormone, in the rat anterior pituitary monolayer culture system with a half-maximal effective dose of 2.5-6.0 ng/ml. Another form of the molecule of Mr 32,000 present in much lower concentration in follicular fluid was also isolated. It may differ from the Mr 35,000 form in glycosylation or carboxyl-terminal truncation. We suggest that this compound be called "follistatin" to signify its structural difference from inhibin.