Angiogenin-induced protein kinase B/Akt activation is necessary for angiogenesis but is independent of nuclear translocation of angiogenin in HUVE cells

Biochem Biophys Res Commun. 2007 Jan 12;352(2):509-13. doi: 10.1016/j.bbrc.2006.11.047. Epub 2006 Nov 17.


Angiogenin, a potent angiogenic factor, binds to endothelial cells and is endocytosed and rapidly translocated to and concentrated in the nucleolus where it binds to DNA. In this study, we report that angiogenin induces transient phosphorylation of protein kinase B/Akt in cultured human umbilical vein endothelial (HUVE) cells. LY294002 inhibits the angiogenin-induced protein kinase B/Akt activation and also angiogenin-induced cell migration in vitro as well as angiogenesis in chick embryo chorioallantoic membrane in vivo without affecting nuclear translocation of angiogenin in HUVE cells. These results suggest that cross-talk between angiogenin and protein kinase B/Akt signaling pathways is essential for angiogenin-induced angiogenesis in vitro and in vivo, and that angiogenin-induced PKB/Akt activation is independent of nuclear translocation of angiogenin in HUVE cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Active Transport, Cell Nucleus / physiology
  • Cell Nucleus / metabolism*
  • Cells, Cultured
  • Dose-Response Relationship, Drug
  • Endothelial Cells / drug effects
  • Endothelial Cells / metabolism*
  • Humans
  • Neovascularization, Physiologic / physiology*
  • Oncogene Protein v-akt / metabolism*
  • Proto-Oncogene Proteins c-akt / metabolism*
  • Ribonuclease, Pancreatic / administration & dosage*
  • Ribonuclease, Pancreatic / metabolism*
  • Umbilical Cord / cytology
  • Umbilical Cord / drug effects
  • Umbilical Cord / metabolism


  • Oncogene Protein v-akt
  • Proto-Oncogene Proteins c-akt
  • angiogenin
  • Ribonuclease, Pancreatic