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Related Experiment Videos

Activin-binding protein is present in pituitary.

K Kogawa1, T Nakamura, K Sugino

  • 1Frontier Research Program, Institute of Physical and Chemical Research (RIKEN), Saitama, Japan.

Endocrinology
|March 1, 1991
PubMed
Summary

Researchers purified an activin-binding protein from bovine pituitary, identifying it as follistatin. This protein regulates follicle-stimulating hormone (FSH) release by forming inactive complexes with activin.

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Area of Science:

  • Endocrinology
  • Molecular Biology
  • Reproductive Biology

Background:

  • Activin plays a role in regulating pituitary hormone secretion.
  • Follistatin is known to inhibit follicle-stimulating hormone (FSH) release.

Purpose of the Study:

  • To purify and characterize the activin-binding protein from bovine pituitary.
  • To investigate the role of this binding protein in FSH secretion regulation.

Main Methods:

  • Affinity chromatography using dextran sulfate-Sepharose CL-4B and activin-Affi-Gel 10.
  • Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) for protein analysis.
  • Ligand blot analysis and binding competition studies to assess binding specificity.
  • Cultured pituitary cells to study FSH release inhibition.

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Main Results:

  • A protein with 52,700-fold purification was obtained, showing 36 and 33 kDa bands.
  • The purified protein's NH2-terminus sequence matched follistatin.
  • The binding protein inhibited spontaneous and activin-induced FSH release from pituitary cells.
  • An inactive equimolar complex of activin and the binding protein was formed.

Conclusions:

  • Activin-binding protein/follistatin is present in the pituitary.
  • This protein regulates FSH secretion by forming inactive complexes with activin.
  • The inhibitory mechanism of activin-binding protein differs from that of inhibin.