Antisense-thioredoxin inhibits angiogenesis via pVHL-mediated hypoxia-inducible factor-1alpha degradation

Int J Oncol. 2005 Apr;26(4):1049-52.

Abstract

Thioredoxin (Trx), a small redox protein, is overexpressed in a number of tumors, however, its roles in tumor cells were not defined well. To investigate the effect of Trx, we transfected Trx or antisense Trx vectors into HT1080 cells. Trx-overexpressed HT1080 cells induced migration of endothelial cells through Flt-1 vascular endothelial growth factor (VEGF) receptor type-1. However, the migration was reduced by overexpression of antisense-Trx. To understand the relationship between Trx and hypoxia-induced angiogenesis, we observed the expression level of VEGF and hypoxia-inducible factor-1alpha (HIF-1alpha) after transfection of Trx. Overexpression of Trx also caused a significant increase of VEGF in protein and RNA levels under normoxic and hypoxic conditions. Moreover, transfection of Trx caused a dramatic increase in HIF-1alpha protein level under hypoxic condition. However, transfection of antisense-Trx markedly decreased HIF-1alpha and VEGF expression compared with controls. In addition, HIF-1alpha was not translocated from cytoplasm to nucleus in antisense-Trx overexpressing HT1080 cells. Further, we could detect the association of HIF-1alpha and pVHL in antisense-Trx transfectant HT1080 cells. Taken together, we suggest that Trx plays an important role in angiogenesis and, therefore, antisense-Trx might be applicable to the inhibition of tumor angiogenesis through the induction of pVHL-mediated HIF-1alpha degradation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Blotting, Northern
  • Blotting, Western
  • Cell Hypoxia
  • Cell Movement
  • Down-Regulation
  • Endothelial Cells
  • Genes, Tumor Suppressor
  • Humans
  • Hypoxia-Inducible Factor 1, alpha Subunit
  • Neoplasms / blood supply
  • Neovascularization, Pathologic*
  • Oligonucleotides, Antisense*
  • Reverse Transcriptase Polymerase Chain Reaction
  • Thioredoxins / genetics*
  • Thioredoxins / pharmacology*
  • Transcription Factors / metabolism
  • Transcription Factors / pharmacology*
  • Transfection
  • Tumor Suppressor Proteins / genetics*
  • Tumor Suppressor Proteins / pharmacology*
  • Ubiquitin-Protein Ligases / genetics*
  • Ubiquitin-Protein Ligases / pharmacology*
  • Umbilical Cord / cytology
  • Vascular Endothelial Growth Factor A / biosynthesis*
  • Von Hippel-Lindau Tumor Suppressor Protein

Substances

  • HIF1A protein, human
  • Hypoxia-Inducible Factor 1, alpha Subunit
  • Oligonucleotides, Antisense
  • Transcription Factors
  • Tumor Suppressor Proteins
  • Vascular Endothelial Growth Factor A
  • Thioredoxins
  • Ubiquitin-Protein Ligases
  • Von Hippel-Lindau Tumor Suppressor Protein
  • VHL protein, human