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Pflügers Archiv

, Volume 439, Issue 6, pp 714–722 | Cite as

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

  • H.J. Meadows
  • C.D. Benham
  • W. Cairns
  • I. Gloger
  • C. Jennings
  • A.D. Medhurst
  • P. Murdock
  • C.G. Chapman
Original Article

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.

Arachidonic acid Human Membrane potential Potassium channel 

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Copyright information

© Springer-Verlag 2000

Authors and Affiliations

  • H.J. Meadows
    • 1
  • C.D. Benham
    • 1
  • W. Cairns
    • 2
  • I. Gloger
    • 2
  • C. Jennings
    • 1
  • A.D. Medhurst
    • 1
  • P. Murdock
    • 2
  • C.G. Chapman
    • 2
  1. 1.Neuroscience Research, SmithKline Beecham Pharmaceuticals, New Frontiers Science Park, Harlow, Essex, CM19 5AWUK
  2. 2.Biotechnology and Genetics, SmithKline Beecham Pharmaceuticals, New Frontiers Science Park, Harlow, Essex, CM19 5AWUK

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