Cloning, localisation and functional expression of the human ortholgue of the TREK-1 potassium channel
Meadows, H.J.; Benham, C.D.; Cairns, W.; Gloger, I.; Jennings, C.; Medhurst, A.D.; Murdock, P.; Chapman, C.G.
Citation: Meadows , H J , Benham , C D , Cairns , W , Gloger , I , Jennings , C , Medhurst , A D , Murdock , P & Chapman , C G 2000 , ' Cloning, localisation and functional expression of the human ortholgue of the TREK-1 potassium channel ' Pflugers Archiv European Journal of Physiology , vol 439 , pp. 714-722 .
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 www.springerlink.com”. Copyright Springer. DOI: 10.1007/s004240050997 [Full text of this article is not available in the UHRA]