Cloning, localisation and functional expression of the human orthologue of the TREK-1 potassium channel

Pflugers Arch. 2000 Apr;439(6):714-22. doi: 10.1007/s004249900235.

Abstract

We have cloned human TREK-1, one of the newly emerging mammalian family of 2-P domain potassium channels. The channel has 411 amino acids with a 41-amino-acid extension at the C-terminus when compared with the cloned mouse TREK-1 channel. Expression of hTREK-1 produced a substantial hyperpolarising shift in resting membrane potential accompanied by the induction of large, outwardly rectifying, non-inactivating currents which were potassium selective. Pharmacologically, hTREK-1-mediated currents were only blocked to a limited extent by classic potassium channel blockers or open channel pore blockers known to potently inhibit other channels. The channel was reversibly potentiated by arachidonic acid. CNS distribution of hTREK-1 is widespread with higher levels being observed in caudate, putamen, amygdala, thalamus and spinal cord. Only low levels of expression were seen in the majority of peripheral regions. Thus, hTREK-1, although functionally and pharmacologically similar to mouse TREK-1, appears to have a more CNS-specific distribution.

MeSH terms

  • Amino Acid Sequence / genetics
  • Animals
  • Base Sequence / genetics
  • Cell Line
  • Cloning, Molecular*
  • Humans
  • Mice
  • Molecular Sequence Data
  • Oocytes / metabolism
  • Peptide Fragments / metabolism
  • Peptide Fragments / physiology
  • Potassium Channels / genetics*
  • Potassium Channels / metabolism*
  • Potassium Channels, Tandem Pore Domain*
  • Tissue Distribution
  • Xenopus laevis / metabolism

Substances

  • Peptide Fragments
  • Potassium Channels
  • Potassium Channels, Tandem Pore Domain
  • potassium channel protein TREK-1

Associated data

  • GENBANK/AF171068