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

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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.

In: Pflugers Archiv European Journal of Physiology, Vol. 439, 2000, p. 714-722.

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Meadows, H.J. ; Benham, C.D. ; Cairns, W. ; Gloger, I. ; Jennings, C. ; Medhurst, A.D. ; Murdock, P. ; Chapman, C.G. / Cloning, localisation and functional expression of the human ortholgue of the TREK-1 potassium channel. In: Pflugers Archiv European Journal of Physiology. 2000 ; Vol. 439. pp. 714-722.

Bibtex

@article{ce9777e06d2b49b2aaf193ef347d6d47,
title = "Cloning, localisation and functional expression of the human ortholgue of the TREK-1 potassium channel",
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.",
author = "H.J. Meadows and C.D. Benham and W. Cairns and I. Gloger and C. Jennings and A.D. Medhurst and P. Murdock and C.G. Chapman",
note = "“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]",
year = "2000",
doi = "10.1007/s004240050997",
language = "English",
volume = "439",
pages = "714--722",
journal = "Pflugers Archiv European Journal of Physiology",
issn = "0031-6768",
publisher = "Springer Verlag",

}

RIS

TY - JOUR

T1 - Cloning, localisation and functional expression of the human ortholgue of the TREK-1 potassium channel

AU - Meadows, H.J.

AU - Benham, C.D.

AU - Cairns, W.

AU - Gloger, I.

AU - Jennings, C.

AU - Medhurst, A.D.

AU - Murdock, P.

AU - Chapman, C.G.

N1 - “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]

PY - 2000

Y1 - 2000

N2 - 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.

AB - 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.

U2 - 10.1007/s004240050997

DO - 10.1007/s004240050997

M3 - Article

VL - 439

SP - 714

EP - 722

JO - Pflugers Archiv European Journal of Physiology

JF - Pflugers Archiv European Journal of Physiology

SN - 0031-6768

ER -