Protein kinase C {alpha} activity is important for contraction-induced FXYD1 phosphorylation in skeletal muscle

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Standard

Protein kinase C {alpha} activity is important for contraction-induced FXYD1 phosphorylation in skeletal muscle. / Thomassen, Martin; Rose, Adam John; Jensen, Thomas Elbenhardt; Maarbjerg, Stine Just; Bune, Laurids Touborg; Leitges, Michael; Richter, Erik A.; Bangsbo, Jens; Nordsborg, Nikolai Baastrup.

I: American Journal of Physiology: Regulatory, Integrative and Comparative Physiology, Bind 301, Nr. 6, 2011, s. R1808-R1814.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Thomassen, M, Rose, AJ, Jensen, TE, Maarbjerg, SJ, Bune, LT, Leitges, M, Richter, EA, Bangsbo, J & Nordsborg, NB 2011, 'Protein kinase C {alpha} activity is important for contraction-induced FXYD1 phosphorylation in skeletal muscle', American Journal of Physiology: Regulatory, Integrative and Comparative Physiology, bind 301, nr. 6, s. R1808-R1814. https://doi.org/10.1152/ajpregu.00066.2011

APA

Thomassen, M., Rose, A. J., Jensen, T. E., Maarbjerg, S. J., Bune, L. T., Leitges, M., Richter, E. A., Bangsbo, J., & Nordsborg, N. B. (2011). Protein kinase C {alpha} activity is important for contraction-induced FXYD1 phosphorylation in skeletal muscle. American Journal of Physiology: Regulatory, Integrative and Comparative Physiology, 301(6), R1808-R1814. https://doi.org/10.1152/ajpregu.00066.2011

Vancouver

Thomassen M, Rose AJ, Jensen TE, Maarbjerg SJ, Bune LT, Leitges M o.a. Protein kinase C {alpha} activity is important for contraction-induced FXYD1 phosphorylation in skeletal muscle. American Journal of Physiology: Regulatory, Integrative and Comparative Physiology. 2011;301(6):R1808-R1814. https://doi.org/10.1152/ajpregu.00066.2011

Author

Thomassen, Martin ; Rose, Adam John ; Jensen, Thomas Elbenhardt ; Maarbjerg, Stine Just ; Bune, Laurids Touborg ; Leitges, Michael ; Richter, Erik A. ; Bangsbo, Jens ; Nordsborg, Nikolai Baastrup. / Protein kinase C {alpha} activity is important for contraction-induced FXYD1 phosphorylation in skeletal muscle. I: American Journal of Physiology: Regulatory, Integrative and Comparative Physiology. 2011 ; Bind 301, Nr. 6. s. R1808-R1814.

Bibtex

@article{ce0c809fa740444f96e22530d15ece4e,
title = "Protein kinase C {alpha} activity is important for contraction-induced FXYD1 phosphorylation in skeletal muscle",
abstract = "Exercise induced phosphorylation of FXYD1 is a potential important regulator of Na(+), K(+) pump activity. It was investigated if skeletal muscle contractions induce phosphorylation of FXYD1 and if Protein Kinase C a (PKCa) activity is a prerequisite for this possible mechanism. In part 1, human muscle biopsies were obtained at rest, after 30 s of high intensity exercise (166±31% of VO(2max)) and after a subsequent 20 min of moderate intensity exercise (79±8% of VO(2max)). In general, FXYD1 phosphorylation was increased compared to rest both after 30 s (P",
author = "Martin Thomassen and Rose, {Adam John} and Jensen, {Thomas Elbenhardt} and Maarbjerg, {Stine Just} and Bune, {Laurids Touborg} and Michael Leitges and Richter, {Erik A.} and Jens Bangsbo and Nordsborg, {Nikolai Baastrup}",
note = "CURIS 2011 5200 118",
year = "2011",
doi = "10.1152/ajpregu.00066.2011",
language = "English",
volume = "301",
pages = "R1808--R1814",
journal = "American Journal of Physiology: Regulatory, Integrative and Comparative Physiology",
issn = "0363-6119",
publisher = "American Physiological Society",
number = "6",

}

RIS

TY - JOUR

T1 - Protein kinase C {alpha} activity is important for contraction-induced FXYD1 phosphorylation in skeletal muscle

AU - Thomassen, Martin

AU - Rose, Adam John

AU - Jensen, Thomas Elbenhardt

AU - Maarbjerg, Stine Just

AU - Bune, Laurids Touborg

AU - Leitges, Michael

AU - Richter, Erik A.

AU - Bangsbo, Jens

AU - Nordsborg, Nikolai Baastrup

N1 - CURIS 2011 5200 118

PY - 2011

Y1 - 2011

N2 - Exercise induced phosphorylation of FXYD1 is a potential important regulator of Na(+), K(+) pump activity. It was investigated if skeletal muscle contractions induce phosphorylation of FXYD1 and if Protein Kinase C a (PKCa) activity is a prerequisite for this possible mechanism. In part 1, human muscle biopsies were obtained at rest, after 30 s of high intensity exercise (166±31% of VO(2max)) and after a subsequent 20 min of moderate intensity exercise (79±8% of VO(2max)). In general, FXYD1 phosphorylation was increased compared to rest both after 30 s (P

AB - Exercise induced phosphorylation of FXYD1 is a potential important regulator of Na(+), K(+) pump activity. It was investigated if skeletal muscle contractions induce phosphorylation of FXYD1 and if Protein Kinase C a (PKCa) activity is a prerequisite for this possible mechanism. In part 1, human muscle biopsies were obtained at rest, after 30 s of high intensity exercise (166±31% of VO(2max)) and after a subsequent 20 min of moderate intensity exercise (79±8% of VO(2max)). In general, FXYD1 phosphorylation was increased compared to rest both after 30 s (P

U2 - 10.1152/ajpregu.00066.2011

DO - 10.1152/ajpregu.00066.2011

M3 - Journal article

C2 - 21957166

VL - 301

SP - R1808-R1814

JO - American Journal of Physiology: Regulatory, Integrative and Comparative Physiology

JF - American Journal of Physiology: Regulatory, Integrative and Comparative Physiology

SN - 0363-6119

IS - 6

ER -

ID: 35089836