Isolation and Partial Characterization of Follistatin: a Single-chain Mr 35,000 Monomeric Protein That Inhibits the Release of Follicle-stimulating Hormone

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 1987 Dec 1

PMID 3120188

Citations 65

Authors

N Ueno

N Ling

S Y Ying

F Esch

S Shimasaki

R Guillemin

Affiliations

Soon will be listed here.

Abstract

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.

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