Recombinant hTASK1 is an O2-sensitive K+ channel

Anthony Lewis; M. Hartness; C. Chapman; I. Fearon; H. Meadows; C. Peers; P. Kemp

doi:10.1006/bbrc.2001.5310

Recombinant hTASK1 is an O2-sensitive K+ channel

Anthony Lewis, M. Hartness, C. Chapman, I. Fearon, H. Meadows, C. Peers, P. Kemp

Research output: Contribution to journal › Article › peer-review

Abstract

Hypoxic inhibition of background K+ channels is crucial to O2 sensing by chemoreceptor tissues, but direct demonstration of O2 sensitivity by any member of this K+ channel family is lacking. HEK293 cells were transfected with a pcDNA3.1-hTASK1 construct; expression of hTASK1 was verified using RT-PCR and immunocytochemistry. Whole-cell K+ currents of cells stably expressing hTASK-1 were, as anticipated, extremely sensitive to extracellular pH, within the physiological range (IC50 ≈ 7.0). All cells expressing this signature pH sensitivity were acutely modulated by pO2; reduction of pO2 from 150 to

Original language	English
Pages (from-to)	1290-1294
Number of pages	5
Journal	Biochemical and Biophysical Research Communications
Volume	285
Issue number	5
DOIs	https://doi.org/10.1006/bbrc.2001.5310
Publication status	Published - 2001

Access to Document

10.1006/bbrc.2001.5310

Cite this

@article{424ef39e9d764dccb624e792e6496e45,

title = "Recombinant hTASK1 is an O2-sensitive K+ channel",

abstract = "Hypoxic inhibition of background K+ channels is crucial to O2 sensing by chemoreceptor tissues, but direct demonstration of O2 sensitivity by any member of this K+ channel family is lacking. HEK293 cells were transfected with a pcDNA3.1-hTASK1 construct; expression of hTASK1 was verified using RT-PCR and immunocytochemistry. Whole-cell K+ currents of cells stably expressing hTASK-1 were, as anticipated, extremely sensitive to extracellular pH, within the physiological range (IC50 ≈ 7.0). All cells expressing this signature pH sensitivity were acutely modulated by pO2; reduction of pO2 from 150 to ",

author = "Anthony Lewis and M. Hartness and C. Chapman and I. Fearon and H. Meadows and C. Peers and P. Kemp",

year = "2001",

doi = "10.1006/bbrc.2001.5310",

language = "English",

volume = "285",

pages = "1290--1294",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

publisher = "Elsevier BV",

number = "5",

}

TY - JOUR

T1 - Recombinant hTASK1 is an O2-sensitive K+ channel

AU - Lewis, Anthony

AU - Hartness, M.

AU - Chapman, C.

AU - Fearon, I.

AU - Meadows, H.

AU - Peers, C.

AU - Kemp, P.

PY - 2001

Y1 - 2001

N2 - Hypoxic inhibition of background K+ channels is crucial to O2 sensing by chemoreceptor tissues, but direct demonstration of O2 sensitivity by any member of this K+ channel family is lacking. HEK293 cells were transfected with a pcDNA3.1-hTASK1 construct; expression of hTASK1 was verified using RT-PCR and immunocytochemistry. Whole-cell K+ currents of cells stably expressing hTASK-1 were, as anticipated, extremely sensitive to extracellular pH, within the physiological range (IC50 ≈ 7.0). All cells expressing this signature pH sensitivity were acutely modulated by pO2; reduction of pO2 from 150 to

AB - Hypoxic inhibition of background K+ channels is crucial to O2 sensing by chemoreceptor tissues, but direct demonstration of O2 sensitivity by any member of this K+ channel family is lacking. HEK293 cells were transfected with a pcDNA3.1-hTASK1 construct; expression of hTASK1 was verified using RT-PCR and immunocytochemistry. Whole-cell K+ currents of cells stably expressing hTASK-1 were, as anticipated, extremely sensitive to extracellular pH, within the physiological range (IC50 ≈ 7.0). All cells expressing this signature pH sensitivity were acutely modulated by pO2; reduction of pO2 from 150 to

U2 - 10.1006/bbrc.2001.5310

DO - 10.1006/bbrc.2001.5310

M3 - Article

SN - 0006-291X

VL - 285

SP - 1290

EP - 1294

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 5

ER -

Recombinant hTASK1 is an O2-sensitive K+ channel

Abstract

Access to Document

Fingerprint

Cite this