Requirement of the nuclear localization of transcription enhancer factor 3 for proliferation, migration, tube formation, and angiogenesis induced by vascular endothelial growth factor

FASEB J. 2011 Apr;25(4):1188-97. doi: 10.1096/fj.10-167619. Epub 2010 Dec 17.

Abstract

Transcription enhancer factor 3 (TEF3) is known to regulate the expression of muscle-specific genes and to play important roles in muscle development and diseases. However, little is known about its role in vascular endothelial growth factor (VEGF)-induced angiogenesis. Most recently, we discovered a novel function of TEF3, in which TEF3 is required for the up-regulation of a proangiogenic factor, Down syndrome candidate region 1 isoform 1L (DSCR1-1L), induced by VEGF-A(165) in endothelial cells. Overexpression of TEF3 isoform 1 (TEF3-1) is sufficient to induce DSCR1-1L expression. Here, we report that knocking down the expression of TEF3 almost completely inhibits VEGF-A(165)-induced proliferation, migration, tube formation, formation of F-actin stress fiber, and in vivo Matrigel angiogenesis. This inhibition cannot be rescued by DSCR1-1L overexpression. Further, overexpression of TEF3-1, but not its nuclear localization signal-deletion mutant (TEF3-ΔNLS), induces human umbilical vein endothelial cell proliferation, migration, tube formation, and formation of F-actin stress fiber, even in the absence of VEGF-A(165) stimulation, which is partially inhibited by DSCR1-1L silencing. Our data demonstrate that TEF3, mainly its nuclear localization, is required for VEGF-A(165)-induced endothelial proliferation, migration, tube formation, and in vivo Matrigel angiogenesis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / metabolism
  • Animals
  • Cell Movement / drug effects
  • Cell Proliferation / drug effects
  • Collagen
  • DNA-Binding Proteins / physiology*
  • Drug Combinations
  • Endothelial Cells / metabolism
  • Endothelium, Vascular / cytology
  • Endothelium, Vascular / metabolism*
  • Humans
  • Intracellular Signaling Peptides and Proteins / physiology
  • Laminin
  • Mice
  • Muscle Proteins / physiology*
  • Neovascularization, Pathologic / chemically induced
  • Neovascularization, Pathologic / physiopathology*
  • Nuclear Localization Signals / physiology
  • Proteoglycans
  • TEA Domain Transcription Factors
  • Transcription Factors / physiology*
  • Vascular Endothelial Growth Factor A / pharmacology*
  • Wound Healing / drug effects

Substances

  • Actins
  • DNA-Binding Proteins
  • Drug Combinations
  • Intracellular Signaling Peptides and Proteins
  • Laminin
  • Muscle Proteins
  • Nuclear Localization Signals
  • Proteoglycans
  • RCAN1 protein, human
  • TEA Domain Transcription Factors
  • TEAD4 protein, human
  • Transcription Factors
  • VEGFA protein, human
  • Vascular Endothelial Growth Factor A
  • matrigel
  • Collagen