Novel high-throughput screening system for identifying STAT3-SH2 antagonists

Biochem Biophys Res Commun. 2009 Mar 13;380(3):627-31. doi: 10.1016/j.bbrc.2009.01.137. Epub 2009 Jan 27.

Abstract

Constitutive activation of the oncogenic transcription factor STAT3 frequently occurs in various human malignancies. STAT3 activation involves dimerization via intermolecular pTyr-SH2 interaction. Thus, antagonizing this interaction is a feasible approach to inhibit STAT3 activation for cancer therapy. In order to identify selective STAT3 inhibitors, we developed a biochemical HTS system based on AlphaScreen technology, which measures the abilities of test compounds to antagonize pTyr-SH2 interactions. We screened our chemical libraries using this system and identified 5,15-diphenylporphyrin (5,15-DPP) as a selective STAT3-SH2 antagonist. Selective inhibition of STAT3 nuclear translocation and DNA biding activity was observed in cells treated with 5,15-DPP. IL-6-dependent dimerization of STAT3, c-myc promoter binding and c-myc protein expression were all suppressed by 5,15-DPP, whereas no decrement in either expression or phosphorylation level of STAT3 was observed. Thus, the HTS assay system represented herein may be useful for identifying novel STAT3-SH2 antagonists.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Antineoplastic Agents / isolation & purification*
  • Antineoplastic Agents / pharmacology
  • Dimerization
  • Drug Screening Assays, Antitumor / methods
  • Humans
  • STAT3 Transcription Factor / antagonists & inhibitors*
  • STAT3 Transcription Factor / metabolism
  • src Homology Domains / drug effects*
  • src-Family Kinases / metabolism*

Substances

  • Antineoplastic Agents
  • STAT3 Transcription Factor
  • src-Family Kinases