Beta A versus beta B: Is it merely a matter of expression?

Thomas B. Thompson, Robert W. Cook, Stacey C. Chapman, Theodore S. Jardetzky, Teresa K. Woodruff*

*Corresponding author for this work

Research output: Contribution to journalConference articlepeer-review

58 Scopus citations


Activins are members of the transforming growth factor (TGF) beta (β) superfamily of proteins that function in a wide array of physiological processes. Like other TGFβ ligands, activins are biologically active as dimers. An activin molecule is comprised of two β-subunits, of which four isoforms have been identified: βA, βB, βC, and βE. The most widely studied activins to date are activin A (βA/βA), activin B (βB/βB), and activin AB (βA/βB). Inhibin is a naturally occurring activin antagonist that consists of an α-subunit disulfide-linked to one of the activin β-subunits, producing inhibin A (α/βA), or inhibin B (α/βB). The development of assays distinguishing between different forms of activins and inhibins, along with knock-in and knock-out models, have provided evidence that the βA- and βB-subunits have independent and separate roles physiologically. Additionally, evaluation of ligand-receptor interactions indicates significant differences in receptor affinity between activin isoforms, as well as between inhibin isoforms. In this review we explore the differences between activin/inhibin βA- and βB-subunits, including expression patterns, binding properties, and the specific structural aspects of each. From the growing pool of knowledge regarding activins and inhibins, the emerging data support the hypothesis that βA- and βB-subunits are functionally differently.

Original languageEnglish (US)
Pages (from-to)9-17
Number of pages9
JournalMolecular and Cellular Endocrinology
Issue number1-2
StatePublished - Oct 15 2004
EventProceedings of the International Workshop on Inhibins, - Siena, Italy
Duration: Jul 3 2003Jul 4 2003


  • Activin
  • Inhibin
  • Ovary
  • Structure
  • TGF

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Endocrinology


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