Evaluation of the dimerization profiles of HER tyrosine kinases by time-resolved Förster resonance energy transfer (TR-FRET)

Methods Mol Biol. 2015:1233:45-55. doi: 10.1007/978-1-4939-1789-1_5.

Abstract

Activation of receptor tyrosine kinases (RTK), such as those belonging to the human epidermal growth factor receptor (HER) family, occurs only after receptor dimerization, which is a crucial step for cellular signal transduction and diversification. The HER family includes four members (EGFR/HER1, HER2, HER3, and HER4) that can homodimerize or heterodimerize. Here, we describe immunoassays based on time-resolved Förster resonance energy transfer (TR-FRET) to profile EGFR-EGFR, HER2-HER2, and EGFR-HER2 dimers directly in tumor samples.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antibodies, Monoclonal, Humanized / chemistry
  • Cell Line, Tumor
  • Cetuximab
  • ErbB Receptors / chemistry*
  • ErbB Receptors / genetics
  • ErbB Receptors / metabolism
  • Female
  • Fluorescence Resonance Energy Transfer
  • Fluorescent Dyes
  • Gene Expression Regulation, Neoplastic*
  • Humans
  • Immunoassay*
  • Mice
  • Ovarian Neoplasms / chemistry*
  • Ovarian Neoplasms / genetics
  • Ovarian Neoplasms / metabolism
  • Ovarian Neoplasms / pathology
  • Protein Kinase Inhibitors / chemistry
  • Protein Multimerization
  • Receptor, ErbB-2 / chemistry*
  • Receptor, ErbB-2 / genetics
  • Receptor, ErbB-2 / metabolism
  • Signal Transduction
  • Trastuzumab
  • Xenograft Model Antitumor Assays

Substances

  • Antibodies, Monoclonal, Humanized
  • Fluorescent Dyes
  • Protein Kinase Inhibitors
  • EGFR protein, human
  • ERBB2 protein, human
  • ErbB Receptors
  • Receptor, ErbB-2
  • Trastuzumab
  • Cetuximab