Integrin alpha5/beta1 expression mediates HER-2 down-regulation in colon cancer cells

J Biol Chem. 2005 May 13;280(19):19027-35. doi: 10.1074/jbc.M410540200. Epub 2005 Mar 9.

Abstract

HER-2 is constitutively activated and overexpressed in many cancers, and its inhibition in colon cancer cells diminishes tumorigenicity and induces apoptosis. Little is known about the regulation of HER-2 signaling in colon cancer cells. Integrin alpha5/beta1 expression is frequently lost in colorectal cancer cells compared with normal intestinal epithelium, and colon cancer cells lacking integrin alpha5/beta1 expression utilize HER-2 signaling for proliferation and tumorigenicity. Re-expression of integrin alpha5/beta1 in colon cancer cells abrogated their tumorigenicity, but how this occurs is not well known. Stable expression of integrin alpha5/beta1 in colon cancer cells with little or no detectable integrin alpha5/beta1 protein expression resulted in the post-transcriptional down-regulation of HER-2 protein. Integrin alpha5/beta1 was found to interact with HER-2, and the cytoplasmic domain of integrin alpha5/beta1 was sufficient to mediate HER-2 down-regulation. Integrin alpha5/beta1-mediated down-regulation of HER-2 was the result of increased lysosomal targeting. The inhibition of HER-2 signaling represents a potential mechanism by which integrin alpha5/beta1 exerts its tumor suppressor-like activity in colon cancer cells. These results also suggest that a novel function for integrin alpha5/beta1 is the control of HER-2 expression.

MeSH terms

  • Agar / chemistry
  • Biotinylation
  • Blotting, Northern
  • Caco-2 Cells
  • Cell Line, Tumor
  • Cell Membrane / metabolism
  • Cell Proliferation
  • Colonic Neoplasms / pathology*
  • Cytoplasm / metabolism
  • Down-Regulation*
  • Extracellular Matrix / metabolism
  • Gene Expression Regulation, Neoplastic*
  • Green Fluorescent Proteins / metabolism
  • Humans
  • Immunoblotting
  • Immunoprecipitation
  • Integrin alpha5beta1 / biosynthesis*
  • Lysosomes / metabolism
  • Mutagenesis, Site-Directed
  • Phosphorylation
  • Protein Structure, Tertiary
  • RNA Processing, Post-Transcriptional
  • RNA, Messenger / metabolism
  • Receptor, ErbB-2 / biosynthesis*
  • Signal Transduction
  • Time Factors
  • Transcription, Genetic
  • Transfection

Substances

  • Integrin alpha5beta1
  • RNA, Messenger
  • Green Fluorescent Proteins
  • Agar
  • Receptor, ErbB-2