Science · 1990 · 878 citations · 36 references
Life SciencesBiochemistryEndocrinologyHormone BiochemistryReproductive EndocrinologyReproductive PhysiologyGonadal Axis RegulationGonadal HormonesHormone Binding ProteinsHypothalamic-pituitary-gonadal AxisOvarian FunctionPituitary HormonesActivin RegulationFollicle-stimulating Hormone SecretionFollicle-stimulating Hormone SignalingInhibitor SpecificityNeoplastic DiseaseTransforming Growth Factor Beta RegulationTransforming Growth Factor-beta Signaling
Activin, a TGF‑β family protein isolated from gonadal fluids, stimulates FSH release and has diverse cellular functions, yet its molecular binding partners remain unidentified. A rat ovarian activin‑binding protein was purified and found to be identical to follistatin, a specific inhibitor of FSH release, suggesting it mediates activin’s regulatory effects.
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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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
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Purification and characterization of an FSH releasing protein from porcine ovarian follicular fluid
Wylie Vale, Jean Rivier, Joan Vaughan et al. · Nature · 1986 · 1.2K citations
Medicine, Endocrinology, Physiology +11
Pituitary FSH is released by a heterodimer of the β-subunits from the two forms of inhibin
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