The role of galectin-1 in trophoblast differentiation and signal transduction

J Reprod Immunol. 2011 Jun;90(1):35-40. doi: 10.1016/j.jri.2011.04.004. Epub 2011 May 31.

Abstract

Galectins are proteins with the ability to bind β-galactosides through a conserved carbohydrate recognition domain. Galectin-1 exerts its biological effects by binding glycan ligands on proteins involved in cell adhesion and growth regulation. Galectin-1 inhibits trophoblast cell proliferation and induces syncytium formation. Its down-regulation in the syncytiotrophoblast has been associated with early pregnancy loss. In the choriocarcinoma-derived BeWo cells the galectin-1 induced growth inhibition is apoptosis-independent, but rather appears to be mediated by binding to cell surface receptors, such as the receptor tyrosine kinases REarranged during Transfection (RET) and Janus Kinase (JAK) 2 as well as vascular endothelial growth factor receptor 3. On the syncytiotrophoblast and extravillous trophoblast galectin-1 binds the Thomsen-Friedenreich disaccharide on mucin-1. The cell differentiation processes induced by binding to these receptors ultimately lead to the inhibition of proliferation and syncytium formation.

MeSH terms

  • Cell Adhesion / physiology
  • Cell Differentiation*
  • Cell Proliferation
  • Female
  • Galactosides / metabolism
  • Galectin 1 / metabolism*
  • Giant Cells / metabolism
  • Humans
  • Janus Kinase 2 / metabolism
  • Pregnancy
  • Receptor Protein-Tyrosine Kinases / metabolism
  • Signal Transduction*
  • Trophoblasts / cytology
  • Trophoblasts / metabolism*
  • Vascular Endothelial Growth Factor Receptor-3 / metabolism

Substances

  • Galactosides
  • Galectin 1
  • Receptor Protein-Tyrosine Kinases
  • Vascular Endothelial Growth Factor Receptor-3
  • Janus Kinase 2