Identification and characterization of follistatin as a novel angiogenin-binding protein

FEBS Lett. 2007 Nov 27;581(28):5505-10. doi: 10.1016/j.febslet.2007.10.059. Epub 2007 Nov 6.


Angiogenin enhances tumorigenesis. However, the mechanisms of angiogenin-induced angiogenesis and cancer cell proliferation remain elusive. In this study, follistatin was identified as a binding partner of angiogenin by a yeast two-hybrid screen and confirmed by a pull-down experiment. The interaction of fluorescently tagged angiogenin and follistatin was monitored in real time by a laser confocal microscope and shown to localize at the sub-nuclear region of HeLa cells. Additional yeast two-hybrid analysis revealed that domains 2 and 3 of follistatin were the minimal structure requirement for angiogenin binding. These findings provide new clues for further studies on the mechanisms of angiogenin-induced angiogenesis or cancer cell growth.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Nucleus / metabolism
  • Fluorescence Resonance Energy Transfer
  • Follistatin / genetics
  • Follistatin / metabolism*
  • HeLa Cells
  • Humans
  • Protein Binding
  • Ribonuclease, Pancreatic / metabolism*
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae / metabolism
  • Two-Hybrid System Techniques


  • Follistatin
  • angiogenin
  • Ribonuclease, Pancreatic