University of Hertfordshire

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By the same authors

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

Research output: Contribution to journalArticlepeer-review

  • H.J. Meadows
  • C.D. Benham
  • W. Cairns
  • I. Gloger
  • C. Jennings
  • A.D. Medhurst
  • P. Murdock
  • C.G. Chapman
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Original languageEnglish
Pages (from-to)714-722
JournalPflugers Archiv European Journal of Physiology
Publication statusPublished - 2000


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.


“The original publication is available at”. Copyright Springer. DOI: 10.1007/s004240050997 [Full text of this article is not available in the UHRA]

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