Activin-Binding Protein from Rat Ovary Is Follistatin
Takanori Nakamura(RIKEN), Koji Takio(RIKEN), Yuzuru Eto(Ajinomoto (Japan)), Hiroshiro Shibai(Ajinomoto (Japan)), Koiti Titani(Fujita Health University), Hiromu Sugino(RIKEN)
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Abstract
Activin, a member of the transforming growth factor beta protein family, was originally isolated from gonadal fluids and stimulates the release of pituitary follicle-stimulating hormone (FSH). Activin has numerous functions in both normal and neoplastic cells. Various cells synthesize activin and have a specific binding site for this peptide. However, the molecular basis for its actions is unknown. A binding protein for activin was purified from rat ovary and was identical to follistatin, a specific inhibitor of FSH release. It is likely that the binding protein participates in the diverse regulatory actions of activin.
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