PKC and AMPK regulation of Kv1.5 potassium channels

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

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PKC and AMPK regulation of Kv1.5 potassium channels. / Andersen, Martin Nybo; Skibsbye, Lasse; Tang, Chuyi; Petersen, Frederic; MacAulay, Nanna; Rasmussen, Hanne Borger; Jespersen, Thomas.

In: Channels (Austin), Vol. 9, No. 3, 2015, p. 121-8.

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

Harvard

Andersen, MN, Skibsbye, L, Tang, C, Petersen, F, MacAulay, N, Rasmussen, HB & Jespersen, T 2015, 'PKC and AMPK regulation of Kv1.5 potassium channels', Channels (Austin), vol. 9, no. 3, pp. 121-8. https://doi.org/10.1080/19336950.2015.1036205

APA

Andersen, M. N., Skibsbye, L., Tang, C., Petersen, F., MacAulay, N., Rasmussen, H. B., & Jespersen, T. (2015). PKC and AMPK regulation of Kv1.5 potassium channels. Channels (Austin), 9(3), 121-8. https://doi.org/10.1080/19336950.2015.1036205

Vancouver

Andersen MN, Skibsbye L, Tang C, Petersen F, MacAulay N, Rasmussen HB et al. PKC and AMPK regulation of Kv1.5 potassium channels. Channels (Austin). 2015;9(3):121-8. https://doi.org/10.1080/19336950.2015.1036205

Author

Andersen, Martin Nybo ; Skibsbye, Lasse ; Tang, Chuyi ; Petersen, Frederic ; MacAulay, Nanna ; Rasmussen, Hanne Borger ; Jespersen, Thomas. / PKC and AMPK regulation of Kv1.5 potassium channels. In: Channels (Austin). 2015 ; Vol. 9, No. 3. pp. 121-8.

Bibtex

@article{9811ac9aad9449caa0cbbd1cec488e10,
title = "PKC and AMPK regulation of Kv1.5 potassium channels",
abstract = "The voltage-gated Kv1.5 potassium channel, conducting the ultra-rapid rectifier K(+) current (IKur), is regulated through several pathways. Here we investigate if Kv1.5 surface expression is controlled by the 2 kinases PKC and AMPK, using Xenopus oocytes, MDCK cells and atrial derived HL-1 cells. By confocal microscopy combined with electrophysiology we demonstrate that PKC activation reduces Kv1.5 current, through a decrease in membrane expressed channels. AMPK activation was found to decrease the membrane expression in MDCK cells, but not in HL-1 cells and was furthermore shown to be dependent on co-expression of Nedd4-2 in Xenopus oocytes. These results indicate that Kv1.5 channels are regulated by both kinases, although through different molecular mechanisms in different cell systems.",
author = "Andersen, {Martin Nybo} and Lasse Skibsbye and Chuyi Tang and Frederic Petersen and Nanna MacAulay and Rasmussen, {Hanne Borger} and Thomas Jespersen",
year = "2015",
doi = "10.1080/19336950.2015.1036205",
language = "English",
volume = "9",
pages = "121--8",
journal = "Channels",
issn = "1933-6950",
publisher = "Taylor & Francis",
number = "3",

}

RIS

TY - JOUR

T1 - PKC and AMPK regulation of Kv1.5 potassium channels

AU - Andersen, Martin Nybo

AU - Skibsbye, Lasse

AU - Tang, Chuyi

AU - Petersen, Frederic

AU - MacAulay, Nanna

AU - Rasmussen, Hanne Borger

AU - Jespersen, Thomas

PY - 2015

Y1 - 2015

N2 - The voltage-gated Kv1.5 potassium channel, conducting the ultra-rapid rectifier K(+) current (IKur), is regulated through several pathways. Here we investigate if Kv1.5 surface expression is controlled by the 2 kinases PKC and AMPK, using Xenopus oocytes, MDCK cells and atrial derived HL-1 cells. By confocal microscopy combined with electrophysiology we demonstrate that PKC activation reduces Kv1.5 current, through a decrease in membrane expressed channels. AMPK activation was found to decrease the membrane expression in MDCK cells, but not in HL-1 cells and was furthermore shown to be dependent on co-expression of Nedd4-2 in Xenopus oocytes. These results indicate that Kv1.5 channels are regulated by both kinases, although through different molecular mechanisms in different cell systems.

AB - The voltage-gated Kv1.5 potassium channel, conducting the ultra-rapid rectifier K(+) current (IKur), is regulated through several pathways. Here we investigate if Kv1.5 surface expression is controlled by the 2 kinases PKC and AMPK, using Xenopus oocytes, MDCK cells and atrial derived HL-1 cells. By confocal microscopy combined with electrophysiology we demonstrate that PKC activation reduces Kv1.5 current, through a decrease in membrane expressed channels. AMPK activation was found to decrease the membrane expression in MDCK cells, but not in HL-1 cells and was furthermore shown to be dependent on co-expression of Nedd4-2 in Xenopus oocytes. These results indicate that Kv1.5 channels are regulated by both kinases, although through different molecular mechanisms in different cell systems.

U2 - 10.1080/19336950.2015.1036205

DO - 10.1080/19336950.2015.1036205

M3 - Letter

C2 - 26043299

VL - 9

SP - 121

EP - 128

JO - Channels

JF - Channels

SN - 1933-6950

IS - 3

ER -

ID: 143670198