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Follistatin Binds to both Activin and Inhibin through the Common Beta-Subunit

Shimonaka, Motoyuki, Inouye, Satoshi, Shimasaki, Shunichi, Ling, Nicholas·1991·Endocrinology

Abstract

Inhibin, activin, and follistatin are three families of polypeptides originally isolated and characterized from ovarian follicular fluid based on their modulation of FSH release from pituitary cell culture. In addition to their effects on FSH synthesis and secretion, inhibin and activin have other biological functions. By contrast, the physiological significance of follistatin was obscure, until it was discovered that follistatin is a binding protein to activin. Since activin binds to follistatin, it is imperative to determine the nature of the activin/follistatin binding complex. Moreover, because inhibin contains a beta-subunit derived from activin, it is important to determine whether inhibin will also bind follistatin. Using a double-ligand blotting technique, we have determined that activin-A has two binding sites for follistatin, whereas inhibin-A has only one binding site for follistatin. Therefore, these results suggest that follistatin binds to both activin and inhibin through the common beta-subunit.

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Metadata

Authors
Shimonaka, M., Inouye, S., Shimasaki, S., & Ling, N.
Venue
Endocrinology
Published
1991-06
Volume
128
Issue
6
Pages
3313-3315
ISSN
  • 0013-7227 (ISSN-L)
  • 1945-7170
OpenAlex
W2044804295
Cited by
258
References
0
FWCI
5.45
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Follistatin Binds to both Activin and Inhibin through the Common Beta-Subunit. https://app.cochat.ai/papers/10.1210/endo-128-6-3313
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Shimonaka, M., Inouye, S., Shimasaki, S., & Ling, N. (1991). Follistatin Binds to both Activin and Inhibin through the Common Beta-Subunit. Endocrinology. https://doi.org/10.1210/endo-128-6-3313

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