Characterizations of a loss-of-function mutation in the Kir3.4 channel subunit.

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Characterizations of a loss-of-function mutation in the Kir3.4 channel subunit. / Calloe, Kirstine; Ravn, Lasse Steen; Schmitt, Nicole; Sui, Jin Liang; Duno, Morten; Haunso, Stig; Grunnet, Morten; Svendsen, Jesper Hastrup; Olesen, Søren-Peter.

In: Biochemical and Biophysical Research Communications, Vol. 364, No. 4, 2007, p. 889-95.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Calloe, K, Ravn, LS, Schmitt, N, Sui, JL, Duno, M, Haunso, S, Grunnet, M, Svendsen, JH & Olesen, S-P 2007, 'Characterizations of a loss-of-function mutation in the Kir3.4 channel subunit.', Biochemical and Biophysical Research Communications, vol. 364, no. 4, pp. 889-95. https://doi.org/10.1016/j.bbrc.2007.10.106

APA

Calloe, K., Ravn, L. S., Schmitt, N., Sui, J. L., Duno, M., Haunso, S., Grunnet, M., Svendsen, J. H., & Olesen, S-P. (2007). Characterizations of a loss-of-function mutation in the Kir3.4 channel subunit. Biochemical and Biophysical Research Communications, 364(4), 889-95. https://doi.org/10.1016/j.bbrc.2007.10.106

Vancouver

Calloe K, Ravn LS, Schmitt N, Sui JL, Duno M, Haunso S et al. Characterizations of a loss-of-function mutation in the Kir3.4 channel subunit. Biochemical and Biophysical Research Communications. 2007;364(4):889-95. https://doi.org/10.1016/j.bbrc.2007.10.106

Author

Calloe, Kirstine ; Ravn, Lasse Steen ; Schmitt, Nicole ; Sui, Jin Liang ; Duno, Morten ; Haunso, Stig ; Grunnet, Morten ; Svendsen, Jesper Hastrup ; Olesen, Søren-Peter. / Characterizations of a loss-of-function mutation in the Kir3.4 channel subunit. In: Biochemical and Biophysical Research Communications. 2007 ; Vol. 364, No. 4. pp. 889-95.

Bibtex

@article{a94d5650e92211dcbee902004c4f4f50,
title = "Characterizations of a loss-of-function mutation in the Kir3.4 channel subunit.",
abstract = "Kir3.4 and Kir3.1 potassium channel subunits mediate the acetylcholine induced inwardly rectifying current I(KACh) in the heart. We found a glycine to arginine substitution in codon 247 of Kir3.4 in a patient with a single episode of atrial fibrillation (AF). Expression in Xenopus laevis oocytes and two-electrode voltage-clamp revealed that Kir3.4-G247R basal current was reduced compared to wild-type Kir3.4 and co-expression with the muscarinic acetylcholine receptor type 2 showed that also the acetylcholine induced current was severely reduced in Kir3.4-G247R, indicating that the mutation interfered with activation by the stimulatory G betagamma-subunits. Co-expression of Kir3.4-G247R with wild-type Kir3.4 or Kir3.1 had a compensating effect on both basal current levels and the response to muscarinic stimulation suggesting the function of Kir3.4-G247R is compensated in vivo. This may explain the lack of clear clinical manifestations and further studies are necessary to elucidate if mutations in Kir3.4 are predisposing AF. Udgivelsesdato: 2007-Dec-28",
author = "Kirstine Calloe and Ravn, {Lasse Steen} and Nicole Schmitt and Sui, {Jin Liang} and Morten Duno and Stig Haunso and Morten Grunnet and Svendsen, {Jesper Hastrup} and S{\o}ren-Peter Olesen",
note = "Keywords: Animals; Atrial Fibrillation; G Protein-Coupled Inwardly-Rectifying Potassium Channels; Humans; Ion Channel Gating; Mutagenesis, Site-Directed; Mutation; Oocytes; Potassium; Structure-Activity Relationship; Xenopus laevis",
year = "2007",
doi = "10.1016/j.bbrc.2007.10.106",
language = "English",
volume = "364",
pages = "889--95",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Elsevier",
number = "4",

}

RIS

TY - JOUR

T1 - Characterizations of a loss-of-function mutation in the Kir3.4 channel subunit.

AU - Calloe, Kirstine

AU - Ravn, Lasse Steen

AU - Schmitt, Nicole

AU - Sui, Jin Liang

AU - Duno, Morten

AU - Haunso, Stig

AU - Grunnet, Morten

AU - Svendsen, Jesper Hastrup

AU - Olesen, Søren-Peter

N1 - Keywords: Animals; Atrial Fibrillation; G Protein-Coupled Inwardly-Rectifying Potassium Channels; Humans; Ion Channel Gating; Mutagenesis, Site-Directed; Mutation; Oocytes; Potassium; Structure-Activity Relationship; Xenopus laevis

PY - 2007

Y1 - 2007

N2 - Kir3.4 and Kir3.1 potassium channel subunits mediate the acetylcholine induced inwardly rectifying current I(KACh) in the heart. We found a glycine to arginine substitution in codon 247 of Kir3.4 in a patient with a single episode of atrial fibrillation (AF). Expression in Xenopus laevis oocytes and two-electrode voltage-clamp revealed that Kir3.4-G247R basal current was reduced compared to wild-type Kir3.4 and co-expression with the muscarinic acetylcholine receptor type 2 showed that also the acetylcholine induced current was severely reduced in Kir3.4-G247R, indicating that the mutation interfered with activation by the stimulatory G betagamma-subunits. Co-expression of Kir3.4-G247R with wild-type Kir3.4 or Kir3.1 had a compensating effect on both basal current levels and the response to muscarinic stimulation suggesting the function of Kir3.4-G247R is compensated in vivo. This may explain the lack of clear clinical manifestations and further studies are necessary to elucidate if mutations in Kir3.4 are predisposing AF. Udgivelsesdato: 2007-Dec-28

AB - Kir3.4 and Kir3.1 potassium channel subunits mediate the acetylcholine induced inwardly rectifying current I(KACh) in the heart. We found a glycine to arginine substitution in codon 247 of Kir3.4 in a patient with a single episode of atrial fibrillation (AF). Expression in Xenopus laevis oocytes and two-electrode voltage-clamp revealed that Kir3.4-G247R basal current was reduced compared to wild-type Kir3.4 and co-expression with the muscarinic acetylcholine receptor type 2 showed that also the acetylcholine induced current was severely reduced in Kir3.4-G247R, indicating that the mutation interfered with activation by the stimulatory G betagamma-subunits. Co-expression of Kir3.4-G247R with wild-type Kir3.4 or Kir3.1 had a compensating effect on both basal current levels and the response to muscarinic stimulation suggesting the function of Kir3.4-G247R is compensated in vivo. This may explain the lack of clear clinical manifestations and further studies are necessary to elucidate if mutations in Kir3.4 are predisposing AF. Udgivelsesdato: 2007-Dec-28

U2 - 10.1016/j.bbrc.2007.10.106

DO - 10.1016/j.bbrc.2007.10.106

M3 - Journal article

C2 - 17967416

VL - 364

SP - 889

EP - 895

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 4

ER -

ID: 2983063