Akt2 influences glycogen synthase activity in human skeletal muscle through regulation of NH2-terminal (sites 2+2a) phosphorylation

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Akt2 influences glycogen synthase activity in human skeletal muscle through regulation of NH2-terminal (sites 2+2a) phosphorylation. / Friedrichsen, Martin; Birk, Jesper Bratz; Richter, Erik A.; Ribel-Madsen, Rasmus; Pehmøller, Christian; Hansen, Bo Falck; Beck-Nielsen, Henning; Hirshman, Michael F; Goodyear, Laurie J; Vaag, Allan; Poulsen, Pernille; Wojtaszewski, Jørgen.

I: American Journal of Physiology: Endocrinology and Metabolism, Bind 304, Nr. 6, 2013, s. E631-E639.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Friedrichsen, M, Birk, JB, Richter, EA, Ribel-Madsen, R, Pehmøller, C, Hansen, BF, Beck-Nielsen, H, Hirshman, MF, Goodyear, LJ, Vaag, A, Poulsen, P & Wojtaszewski, J 2013, 'Akt2 influences glycogen synthase activity in human skeletal muscle through regulation of NH2-terminal (sites 2+2a) phosphorylation', American Journal of Physiology: Endocrinology and Metabolism, bind 304, nr. 6, s. E631-E639. https://doi.org/10.1152/ajpendo.00494.2012

APA

Friedrichsen, M., Birk, J. B., Richter, E. A., Ribel-Madsen, R., Pehmøller, C., Hansen, B. F., ... Wojtaszewski, J. (2013). Akt2 influences glycogen synthase activity in human skeletal muscle through regulation of NH2-terminal (sites 2+2a) phosphorylation. American Journal of Physiology: Endocrinology and Metabolism, 304(6), E631-E639. https://doi.org/10.1152/ajpendo.00494.2012

Vancouver

Friedrichsen M, Birk JB, Richter EA, Ribel-Madsen R, Pehmøller C, Hansen BF o.a. Akt2 influences glycogen synthase activity in human skeletal muscle through regulation of NH2-terminal (sites 2+2a) phosphorylation. American Journal of Physiology: Endocrinology and Metabolism. 2013;304(6):E631-E639. https://doi.org/10.1152/ajpendo.00494.2012

Author

Friedrichsen, Martin ; Birk, Jesper Bratz ; Richter, Erik A. ; Ribel-Madsen, Rasmus ; Pehmøller, Christian ; Hansen, Bo Falck ; Beck-Nielsen, Henning ; Hirshman, Michael F ; Goodyear, Laurie J ; Vaag, Allan ; Poulsen, Pernille ; Wojtaszewski, Jørgen. / Akt2 influences glycogen synthase activity in human skeletal muscle through regulation of NH2-terminal (sites 2+2a) phosphorylation. I: American Journal of Physiology: Endocrinology and Metabolism. 2013 ; Bind 304, Nr. 6. s. E631-E639.

Bibtex

@article{f691d5cf7aee485bb16a68f78f6be9de,
title = "Akt2 influences glycogen synthase activity in human skeletal muscle through regulation of NH2-terminal (sites 2+2a) phosphorylation",
abstract = "Type 2 diabetes is characterized by reduced muscle glycogen synthesis. The key enzyme in this process, glycogen synthase (GS), is activated via proximal insulin signaling, but the exact molecular events remain unknown. We previously demonstrated that phosphorylation of Threonine-308 on Akt (pAkt-T308), Akt2 activity, and GS activity in muscle were positivity associated with insulin sensitivity. Now, in the same study population, we determined the influence of several upstream elements in the canonical PI3K signaling on muscle GS activation. 181 non-diabetic twins were examined with the euglycemic-hyperinsulinemic clamp combined with excision of muscle biopsies. Insulin signaling was evaluated at the levels of the insulin receptor, IRS-1-associated PI3K (IRS-1-PI3K), Akt, and GS employing kinase activity assays and phospho-specific western blotting. The insulin-stimulated GS activity was positively associated with pAkt-T308 (P=0.01) and Akt2 activity (P=0.04), but not pAkt-S473 or IRS-1-PI3K activity. Furthermore, pAkt-T308 and Akt2 activity were negatively associated with NH(2)-terminal GS phosphorylation (P=0.001 for both), which in turn was negatively associated with insulin-stimulated GS activity (P",
author = "Martin Friedrichsen and Birk, {Jesper Bratz} and Richter, {Erik A.} and Rasmus Ribel-Madsen and Christian Pehm{\o}ller and Hansen, {Bo Falck} and Henning Beck-Nielsen and Hirshman, {Michael F} and Goodyear, {Laurie J} and Allan Vaag and Pernille Poulsen and J{\o}rgen Wojtaszewski",
note = "CURIS 2013 NEXS 012",
year = "2013",
doi = "10.1152/ajpendo.00494.2012",
language = "English",
volume = "304",
pages = "E631--E639",
journal = "American Journal of Physiology: Endocrinology and Metabolism",
issn = "0193-1849",
publisher = "American Physiological Society",
number = "6",

}

RIS

TY - JOUR

T1 - Akt2 influences glycogen synthase activity in human skeletal muscle through regulation of NH2-terminal (sites 2+2a) phosphorylation

AU - Friedrichsen, Martin

AU - Birk, Jesper Bratz

AU - Richter, Erik A.

AU - Ribel-Madsen, Rasmus

AU - Pehmøller, Christian

AU - Hansen, Bo Falck

AU - Beck-Nielsen, Henning

AU - Hirshman, Michael F

AU - Goodyear, Laurie J

AU - Vaag, Allan

AU - Poulsen, Pernille

AU - Wojtaszewski, Jørgen

N1 - CURIS 2013 NEXS 012

PY - 2013

Y1 - 2013

N2 - Type 2 diabetes is characterized by reduced muscle glycogen synthesis. The key enzyme in this process, glycogen synthase (GS), is activated via proximal insulin signaling, but the exact molecular events remain unknown. We previously demonstrated that phosphorylation of Threonine-308 on Akt (pAkt-T308), Akt2 activity, and GS activity in muscle were positivity associated with insulin sensitivity. Now, in the same study population, we determined the influence of several upstream elements in the canonical PI3K signaling on muscle GS activation. 181 non-diabetic twins were examined with the euglycemic-hyperinsulinemic clamp combined with excision of muscle biopsies. Insulin signaling was evaluated at the levels of the insulin receptor, IRS-1-associated PI3K (IRS-1-PI3K), Akt, and GS employing kinase activity assays and phospho-specific western blotting. The insulin-stimulated GS activity was positively associated with pAkt-T308 (P=0.01) and Akt2 activity (P=0.04), but not pAkt-S473 or IRS-1-PI3K activity. Furthermore, pAkt-T308 and Akt2 activity were negatively associated with NH(2)-terminal GS phosphorylation (P=0.001 for both), which in turn was negatively associated with insulin-stimulated GS activity (P

AB - Type 2 diabetes is characterized by reduced muscle glycogen synthesis. The key enzyme in this process, glycogen synthase (GS), is activated via proximal insulin signaling, but the exact molecular events remain unknown. We previously demonstrated that phosphorylation of Threonine-308 on Akt (pAkt-T308), Akt2 activity, and GS activity in muscle were positivity associated with insulin sensitivity. Now, in the same study population, we determined the influence of several upstream elements in the canonical PI3K signaling on muscle GS activation. 181 non-diabetic twins were examined with the euglycemic-hyperinsulinemic clamp combined with excision of muscle biopsies. Insulin signaling was evaluated at the levels of the insulin receptor, IRS-1-associated PI3K (IRS-1-PI3K), Akt, and GS employing kinase activity assays and phospho-specific western blotting. The insulin-stimulated GS activity was positively associated with pAkt-T308 (P=0.01) and Akt2 activity (P=0.04), but not pAkt-S473 or IRS-1-PI3K activity. Furthermore, pAkt-T308 and Akt2 activity were negatively associated with NH(2)-terminal GS phosphorylation (P=0.001 for both), which in turn was negatively associated with insulin-stimulated GS activity (P

U2 - 10.1152/ajpendo.00494.2012

DO - 10.1152/ajpendo.00494.2012

M3 - Journal article

C2 - 23321478

VL - 304

SP - E631-E639

JO - American Journal of Physiology: Endocrinology and Metabolism

JF - American Journal of Physiology: Endocrinology and Metabolism

SN - 0193-1849

IS - 6

ER -

ID: 43894751