Na,K-ATPase activity in mouse muscle is regulated by AMPK and PGC-1a

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Standard

Na,K-ATPase activity in mouse muscle is regulated by AMPK and PGC-1a. / Ingwersen, Maria S; Kristensen, Michael; Pilegaard, Henriette; Wojtaszewski, Jørgen; Richter, Erik A.; Juel, Carsten.

I: Journal of Membrane Biology, Bind 242, Nr. 1, 2011, s. 1-10.

Publikation: Bidrag til tidsskriftTidsskriftartikelfagfællebedømt

Harvard

Ingwersen, MS, Kristensen, M, Pilegaard, H, Wojtaszewski, J, Richter, EA & Juel, C 2011, 'Na,K-ATPase activity in mouse muscle is regulated by AMPK and PGC-1a', Journal of Membrane Biology, bind 242, nr. 1, s. 1-10. https://doi.org/10.1007/s00232-011-9365-7

APA

Ingwersen, M. S., Kristensen, M., Pilegaard, H., Wojtaszewski, J., Richter, E. A., & Juel, C. (2011). Na,K-ATPase activity in mouse muscle is regulated by AMPK and PGC-1a. Journal of Membrane Biology, 242(1), 1-10. https://doi.org/10.1007/s00232-011-9365-7

Vancouver

Ingwersen MS, Kristensen M, Pilegaard H, Wojtaszewski J, Richter EA, Juel C. Na,K-ATPase activity in mouse muscle is regulated by AMPK and PGC-1a. Journal of Membrane Biology. 2011;242(1):1-10. https://doi.org/10.1007/s00232-011-9365-7

Author

Ingwersen, Maria S ; Kristensen, Michael ; Pilegaard, Henriette ; Wojtaszewski, Jørgen ; Richter, Erik A. ; Juel, Carsten. / Na,K-ATPase activity in mouse muscle is regulated by AMPK and PGC-1a. I: Journal of Membrane Biology. 2011 ; Bind 242, Nr. 1. s. 1-10.

Bibtex

@article{2926cfc7bf1b4d118cc24f89e3c66a32,
title = "Na,K-ATPase activity in mouse muscle is regulated by AMPK and PGC-1a",
abstract = "Na,K-ATPase activity, which is crucial for skeletal muscle function, undergoes acute and long-term regulation in response to muscle activity. The aim of the present study was to test the hypothesis that AMP kinase (AMPK) and the transcriptional coactivator PGC-1a are underlying factors in long-term regulation of Na,K-ATPase isoform (a,{\ss} and PLM) abundance and Na(+) affinity. Repeated treatment of mice with the AMPK activator AICAR decreased total PLM protein content but increased PLM phosphorylation, whereas the number of a- and {\ss}-subunits remained unchanged. The K (m) for Na(+) stimulation of Na,K-ATPase was reduced (higher affinity) after AICAR treatment. PLM abundance was increased in AMPK kinase-dead mice compared with control mice, but PLM phosphorylation and Na,K-ATPase Na(+) affinity remained unchanged. Na,K-ATPase activity and subunit distribution were also measured in mice with different degrees of PGC-1a expression. Protein abundances of a1 and a2 were reduced in PGC-1a +/- and -/- mice, and the {\ss}(1)/{\ss}(2) ratio was increased with PGC-1a overexpression (TG mice). PLM protein abundance was decreased in TG mice, but phosphorylation status was unchanged. Na,K-ATPase V (max) was decreased in PCG-1a TG and KO mice. Experimentally in vitro induced phosphorylation of PLM increased Na,K-ATPase Na(+) affinity, confirming that PLM phosphorylation is important for Na,K-ATPase function. In conclusion, both AMPK and PGC-1a regulate PLM abundance, AMPK regulates PLM phosphorylation and PGC-1a expression influences Na,K-ATPase a(1) and a(2) content and {\ss}(1)/{\ss}(2) isoform ratio. Phosphorylation of the Na,K-ATPase subunit PLM is an important regulatory mechanism.",
author = "Ingwersen, {Maria S} and Michael Kristensen and Henriette Pilegaard and J{\o}rgen Wojtaszewski and Richter, {Erik A.} and Carsten Juel",
note = "CURIS 2011 5200 066",
year = "2011",
doi = "10.1007/s00232-011-9365-7",
language = "English",
volume = "242",
pages = "1--10",
journal = "Journal of Membrane Biology",
issn = "0022-2631",
publisher = "Springer",
number = "1",

}

RIS

TY - JOUR

T1 - Na,K-ATPase activity in mouse muscle is regulated by AMPK and PGC-1a

AU - Ingwersen, Maria S

AU - Kristensen, Michael

AU - Pilegaard, Henriette

AU - Wojtaszewski, Jørgen

AU - Richter, Erik A.

AU - Juel, Carsten

N1 - CURIS 2011 5200 066

PY - 2011

Y1 - 2011

N2 - Na,K-ATPase activity, which is crucial for skeletal muscle function, undergoes acute and long-term regulation in response to muscle activity. The aim of the present study was to test the hypothesis that AMP kinase (AMPK) and the transcriptional coactivator PGC-1a are underlying factors in long-term regulation of Na,K-ATPase isoform (a,ß and PLM) abundance and Na(+) affinity. Repeated treatment of mice with the AMPK activator AICAR decreased total PLM protein content but increased PLM phosphorylation, whereas the number of a- and ß-subunits remained unchanged. The K (m) for Na(+) stimulation of Na,K-ATPase was reduced (higher affinity) after AICAR treatment. PLM abundance was increased in AMPK kinase-dead mice compared with control mice, but PLM phosphorylation and Na,K-ATPase Na(+) affinity remained unchanged. Na,K-ATPase activity and subunit distribution were also measured in mice with different degrees of PGC-1a expression. Protein abundances of a1 and a2 were reduced in PGC-1a +/- and -/- mice, and the ß(1)/ß(2) ratio was increased with PGC-1a overexpression (TG mice). PLM protein abundance was decreased in TG mice, but phosphorylation status was unchanged. Na,K-ATPase V (max) was decreased in PCG-1a TG and KO mice. Experimentally in vitro induced phosphorylation of PLM increased Na,K-ATPase Na(+) affinity, confirming that PLM phosphorylation is important for Na,K-ATPase function. In conclusion, both AMPK and PGC-1a regulate PLM abundance, AMPK regulates PLM phosphorylation and PGC-1a expression influences Na,K-ATPase a(1) and a(2) content and ß(1)/ß(2) isoform ratio. Phosphorylation of the Na,K-ATPase subunit PLM is an important regulatory mechanism.

AB - Na,K-ATPase activity, which is crucial for skeletal muscle function, undergoes acute and long-term regulation in response to muscle activity. The aim of the present study was to test the hypothesis that AMP kinase (AMPK) and the transcriptional coactivator PGC-1a are underlying factors in long-term regulation of Na,K-ATPase isoform (a,ß and PLM) abundance and Na(+) affinity. Repeated treatment of mice with the AMPK activator AICAR decreased total PLM protein content but increased PLM phosphorylation, whereas the number of a- and ß-subunits remained unchanged. The K (m) for Na(+) stimulation of Na,K-ATPase was reduced (higher affinity) after AICAR treatment. PLM abundance was increased in AMPK kinase-dead mice compared with control mice, but PLM phosphorylation and Na,K-ATPase Na(+) affinity remained unchanged. Na,K-ATPase activity and subunit distribution were also measured in mice with different degrees of PGC-1a expression. Protein abundances of a1 and a2 were reduced in PGC-1a +/- and -/- mice, and the ß(1)/ß(2) ratio was increased with PGC-1a overexpression (TG mice). PLM protein abundance was decreased in TG mice, but phosphorylation status was unchanged. Na,K-ATPase V (max) was decreased in PCG-1a TG and KO mice. Experimentally in vitro induced phosphorylation of PLM increased Na,K-ATPase Na(+) affinity, confirming that PLM phosphorylation is important for Na,K-ATPase function. In conclusion, both AMPK and PGC-1a regulate PLM abundance, AMPK regulates PLM phosphorylation and PGC-1a expression influences Na,K-ATPase a(1) and a(2) content and ß(1)/ß(2) isoform ratio. Phosphorylation of the Na,K-ATPase subunit PLM is an important regulatory mechanism.

U2 - 10.1007/s00232-011-9365-7

DO - 10.1007/s00232-011-9365-7

M3 - Journal article

C2 - 21687978

VL - 242

SP - 1

EP - 10

JO - Journal of Membrane Biology

JF - Journal of Membrane Biology

SN - 0022-2631

IS - 1

ER -

ID: 33716570