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Cisplatin inhibits MEK1/2.

Tetsu Yamamoto1, Igor F Tsigelny1,2,3, Andreas W Götz3

  • 1Moores Cancer Center and Department of Medicine, University of California, San Diego, La Jolla, CA 92093, USA.

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|July 10, 2015
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Summary

Cisplatin (cDDP) binds to and inhibits the activity of copper-dependent MEK1/2 enzymes. This interaction, influenced by copper levels, suggests potential therapeutic strategies involving MAPK pathway signaling inhibitors.

Keywords:
ERKMEK1RAScisplatincopper

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Pharmacology

Background:

  • Cisplatin (cDDP) typically targets proteins with CXXC motifs.
  • MEK1/2 is a copper-dependent enzyme lacking the CXXC motif.
  • Understanding cDDP interactions with non-CXXC copper-binding proteins is limited.

Purpose of the Study:

  • To investigate the interaction between cisplatin and the copper-dependent enzyme MEK1/2.
  • To determine if cisplatin inhibits MEK1/2 activity.
  • To explore the role of copper in this interaction.

Main Methods:

  • Enzyme activity assays using recombinant MEK1 and MEK1/2 in whole cells.
  • Copper titration experiments to assess inhibition reversal.
  • Cellular copper level analysis and molecular modeling.
  • Quantum chemistry calculations.

Main Results:

  • Cisplatin inhibited recombinant MEK1 (IC50 = 0.28 μM) and MEK1/2 in cells (IC50 = 37.4 μM).
  • Inhibition was reversed by Cu+1 and Cu+2 in a dose-dependent manner.
  • Cisplatin bound to MEK1/2, with binding affected by copper availability.
  • Molecular modeling predicted copper and cDDP binding sites.

Conclusions:

  • Cisplatin binds to and inhibits copper-dependent MEK1/2 at clinically relevant concentrations.
  • The binding and inhibition are linked to cisplatin's interaction with copper bound to MEK1/2.
  • This finding may inform the development of combination therapies targeting the MAPK pathway.