Dual regulation of muscle glycogen synthase during exercise by activation and compartmentalization

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Standard

Dual regulation of muscle glycogen synthase during exercise by activation and compartmentalization. / Prats, Clara; Helge, Jørn W; Nordby, Pernille; Qvortrup, Klaus; Ploug, Thorkil; Dela, Flemming; Wojtaszewski, Jørgen.

I: Journal of Biological Chemistry, Bind 284, Nr. 23, 2009, s. 15692-15700.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Prats, C, Helge, JW, Nordby, P, Qvortrup, K, Ploug, T, Dela, F & Wojtaszewski, J 2009, 'Dual regulation of muscle glycogen synthase during exercise by activation and compartmentalization', Journal of Biological Chemistry, bind 284, nr. 23, s. 15692-15700. https://doi.org/10.1074/jbc.M900845200

APA

Prats, C., Helge, J. W., Nordby, P., Qvortrup, K., Ploug, T., Dela, F., & Wojtaszewski, J. (2009). Dual regulation of muscle glycogen synthase during exercise by activation and compartmentalization. Journal of Biological Chemistry, 284(23), 15692-15700. https://doi.org/10.1074/jbc.M900845200

Vancouver

Prats C, Helge JW, Nordby P, Qvortrup K, Ploug T, Dela F o.a. Dual regulation of muscle glycogen synthase during exercise by activation and compartmentalization. Journal of Biological Chemistry. 2009;284(23):15692-15700. https://doi.org/10.1074/jbc.M900845200

Author

Prats, Clara ; Helge, Jørn W ; Nordby, Pernille ; Qvortrup, Klaus ; Ploug, Thorkil ; Dela, Flemming ; Wojtaszewski, Jørgen. / Dual regulation of muscle glycogen synthase during exercise by activation and compartmentalization. I: Journal of Biological Chemistry. 2009 ; Bind 284, Nr. 23. s. 15692-15700.

Bibtex

@article{bd8054305f2b11dea8de000ea68e967b,
title = "Dual regulation of muscle glycogen synthase during exercise by activation and compartmentalization",
abstract = "Glycogen synthase (GS) is considered the rate-limiting enzyme in glycogenesis but still today there is a lack of understanding on its regulation. We have previously shown phosphorylation-dependent GS intracellular redistribution at the start of glycogen re-synthesis in rabbit skeletal muscle (Prats, C., Cadefau, J. A., Cuss{\'o}, R., Qvortrup, K., Nielsen, J. N., Wojtaszewki, J. F., Wojtaszewki, J. F., Hardie, D. G., Stewart, G., Hansen, B. F., and Ploug, T. (2005) J. Biol. Chem. 280, 23165-23172). In the present study we investigate the regulation of human muscle GS activity by glycogen, exercise, and insulin. Using immunocytochemistry we investigate the existence and relevance of GS intracellular compartmentalization during exercise and during glycogen re-synthesis. The results show that GS intrinsic activity is strongly dependent on glycogen levels and that such regulation involves associated dephosphorylation at sites 2+2a, 3a, and 3a + 3b. Furthermore, we report the existence of several glycogen metabolism regulatory mechanisms based on GS intracellular compartmentalization. After exhausting exercise, epinephrine-induced protein kinase A activation leads to GS site 1b phosphorylation targeting the enzyme to intramyofibrillar glycogen particles, which are preferentially used during muscle contraction. On the other hand, when phosphorylated at sites 2+2a, GS is preferentially associated with subsarcolemmal and intermyofibrillar glycogen particles. Finally, we verify the existence in human vastus lateralis muscle of the previously reported mechanism of glycogen metabolism regulation in rabbit tibialis anterior muscle. After overnight low muscle glycogen level and/or in response to exhausting exercise-induced glycogenolysis, GS is associated with spherical structures at the I-band of sarcomeres.",
author = "Clara Prats and Helge, {J{\o}rn W} and Pernille Nordby and Klaus Qvortrup and Thorkil Ploug and Flemming Dela and J{\o}rgen Wojtaszewski",
note = "CURIS 2009 5200 096",
year = "2009",
doi = "10.1074/jbc.M900845200",
language = "English",
volume = "284",
pages = "15692--15700",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",
number = "23",

}

RIS

TY - JOUR

T1 - Dual regulation of muscle glycogen synthase during exercise by activation and compartmentalization

AU - Prats, Clara

AU - Helge, Jørn W

AU - Nordby, Pernille

AU - Qvortrup, Klaus

AU - Ploug, Thorkil

AU - Dela, Flemming

AU - Wojtaszewski, Jørgen

N1 - CURIS 2009 5200 096

PY - 2009

Y1 - 2009

N2 - Glycogen synthase (GS) is considered the rate-limiting enzyme in glycogenesis but still today there is a lack of understanding on its regulation. We have previously shown phosphorylation-dependent GS intracellular redistribution at the start of glycogen re-synthesis in rabbit skeletal muscle (Prats, C., Cadefau, J. A., Cussó, R., Qvortrup, K., Nielsen, J. N., Wojtaszewki, J. F., Wojtaszewki, J. F., Hardie, D. G., Stewart, G., Hansen, B. F., and Ploug, T. (2005) J. Biol. Chem. 280, 23165-23172). In the present study we investigate the regulation of human muscle GS activity by glycogen, exercise, and insulin. Using immunocytochemistry we investigate the existence and relevance of GS intracellular compartmentalization during exercise and during glycogen re-synthesis. The results show that GS intrinsic activity is strongly dependent on glycogen levels and that such regulation involves associated dephosphorylation at sites 2+2a, 3a, and 3a + 3b. Furthermore, we report the existence of several glycogen metabolism regulatory mechanisms based on GS intracellular compartmentalization. After exhausting exercise, epinephrine-induced protein kinase A activation leads to GS site 1b phosphorylation targeting the enzyme to intramyofibrillar glycogen particles, which are preferentially used during muscle contraction. On the other hand, when phosphorylated at sites 2+2a, GS is preferentially associated with subsarcolemmal and intermyofibrillar glycogen particles. Finally, we verify the existence in human vastus lateralis muscle of the previously reported mechanism of glycogen metabolism regulation in rabbit tibialis anterior muscle. After overnight low muscle glycogen level and/or in response to exhausting exercise-induced glycogenolysis, GS is associated with spherical structures at the I-band of sarcomeres.

AB - Glycogen synthase (GS) is considered the rate-limiting enzyme in glycogenesis but still today there is a lack of understanding on its regulation. We have previously shown phosphorylation-dependent GS intracellular redistribution at the start of glycogen re-synthesis in rabbit skeletal muscle (Prats, C., Cadefau, J. A., Cussó, R., Qvortrup, K., Nielsen, J. N., Wojtaszewki, J. F., Wojtaszewki, J. F., Hardie, D. G., Stewart, G., Hansen, B. F., and Ploug, T. (2005) J. Biol. Chem. 280, 23165-23172). In the present study we investigate the regulation of human muscle GS activity by glycogen, exercise, and insulin. Using immunocytochemistry we investigate the existence and relevance of GS intracellular compartmentalization during exercise and during glycogen re-synthesis. The results show that GS intrinsic activity is strongly dependent on glycogen levels and that such regulation involves associated dephosphorylation at sites 2+2a, 3a, and 3a + 3b. Furthermore, we report the existence of several glycogen metabolism regulatory mechanisms based on GS intracellular compartmentalization. After exhausting exercise, epinephrine-induced protein kinase A activation leads to GS site 1b phosphorylation targeting the enzyme to intramyofibrillar glycogen particles, which are preferentially used during muscle contraction. On the other hand, when phosphorylated at sites 2+2a, GS is preferentially associated with subsarcolemmal and intermyofibrillar glycogen particles. Finally, we verify the existence in human vastus lateralis muscle of the previously reported mechanism of glycogen metabolism regulation in rabbit tibialis anterior muscle. After overnight low muscle glycogen level and/or in response to exhausting exercise-induced glycogenolysis, GS is associated with spherical structures at the I-band of sarcomeres.

U2 - 10.1074/jbc.M900845200

DO - 10.1074/jbc.M900845200

M3 - Journal article

VL - 284

SP - 15692

EP - 15700

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 23

ER -

ID: 12771785