Overexpression or ablation of JNK in skeletal muscle has no effect on glycogen synthase activity

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Overexpression or ablation of JNK in skeletal muscle has no effect on glycogen synthase activity. / Fujii, Nobuharu; Boppart, Marni D.; Dufresne, Scott D.; Crowley, Patricia F.; Jozsi, Alison C.; Sakamoto, Kei; Yu, Haiyan; Aschenbach, Williams G.; Kim, Shokei; Miyazaki, Hitoshi; Rui, Liangyou; White, Morris F.; Hirshman, Michael F.; Goodyear, Laurie J.

In: American Journal of Physiology - Cell Physiology, Vol. 287, No. 1 56-1, 01.07.2004, p. C200-C208.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Fujii, N, Boppart, MD, Dufresne, SD, Crowley, PF, Jozsi, AC, Sakamoto, K, Yu, H, Aschenbach, WG, Kim, S, Miyazaki, H, Rui, L, White, MF, Hirshman, MF & Goodyear, LJ 2004, 'Overexpression or ablation of JNK in skeletal muscle has no effect on glycogen synthase activity', American Journal of Physiology - Cell Physiology, vol. 287, no. 1 56-1, pp. C200-C208. https://doi.org/10.1152/ajpcell.00415.2003

APA

Fujii, N., Boppart, M. D., Dufresne, S. D., Crowley, P. F., Jozsi, A. C., Sakamoto, K., Yu, H., Aschenbach, W. G., Kim, S., Miyazaki, H., Rui, L., White, M. F., Hirshman, M. F., & Goodyear, L. J. (2004). Overexpression or ablation of JNK in skeletal muscle has no effect on glycogen synthase activity. American Journal of Physiology - Cell Physiology, 287(1 56-1), C200-C208. https://doi.org/10.1152/ajpcell.00415.2003

Vancouver

Fujii N, Boppart MD, Dufresne SD, Crowley PF, Jozsi AC, Sakamoto K et al. Overexpression or ablation of JNK in skeletal muscle has no effect on glycogen synthase activity. American Journal of Physiology - Cell Physiology. 2004 Jul 1;287(1 56-1):C200-C208. https://doi.org/10.1152/ajpcell.00415.2003

Author

Fujii, Nobuharu ; Boppart, Marni D. ; Dufresne, Scott D. ; Crowley, Patricia F. ; Jozsi, Alison C. ; Sakamoto, Kei ; Yu, Haiyan ; Aschenbach, Williams G. ; Kim, Shokei ; Miyazaki, Hitoshi ; Rui, Liangyou ; White, Morris F. ; Hirshman, Michael F. ; Goodyear, Laurie J. / Overexpression or ablation of JNK in skeletal muscle has no effect on glycogen synthase activity. In: American Journal of Physiology - Cell Physiology. 2004 ; Vol. 287, No. 1 56-1. pp. C200-C208.

Bibtex

@article{58ad7451d5f54d43af0d69c018af0aa3,
title = "Overexpression or ablation of JNK in skeletal muscle has no effect on glycogen synthase activity",
abstract = "c-Jun NH2-terminal kinase (JNK) is highly expressed in skeletal muscle and is robustly activated in response to muscle contraction. Little is known about the biological functions of JNK signaling in terminally differentiated muscle cells, although this protein has been proposed to regulate insulin-stimulated glycogen synthase activity in mouse skeletal muscle. To determine whether JNK signaling regulates contraction-stimulated glycogen synthase activation, we applied an electroporation technique to induce JNK overexpression (O/E) in mouse skeletal muscle. Ten days after electroporation, in situ muscle contraction increased JNK activity 2.6-fold in control muscles and 15-fold in the JNK O/E muscles. Despite the enormous activation of JNK activity in JNK O/E muscles, contraction resulted in similar increases in glycogen synthase activity in control and JNK O/E muscles. Consistent with these findings, basal and contraction-induced glycogen synthase activity was normal in muscles of both JNK1- and JNK2-deficient mice. JNK overexpression in muscle resulted in significant alterations in the basal phosphorylation state of several signaling proteins, such as extracellular signal-regulated kinase 1/2, p90 S6 kinase, glycogen synthase kinase 3, protein kinase B/Akt, and p70 S6 kinase, in the absence of changes in the expression of these proteins. These data suggest that JNK signaling regulates the phosphorylation state of several kinases in skeletal muscle. JNK activation is unlikely to be the major mechanism by which contractile activity increases glycogen synthase activity in skeletal muscle.",
keywords = "Electroporation, Exercise, Gene delivery, Muscle contraction",
author = "Nobuharu Fujii and Boppart, {Marni D.} and Dufresne, {Scott D.} and Crowley, {Patricia F.} and Jozsi, {Alison C.} and Kei Sakamoto and Haiyan Yu and Aschenbach, {Williams G.} and Shokei Kim and Hitoshi Miyazaki and Liangyou Rui and White, {Morris F.} and Hirshman, {Michael F.} and Goodyear, {Laurie J.}",
year = "2004",
month = jul,
day = "1",
doi = "10.1152/ajpcell.00415.2003",
language = "English",
volume = "287",
pages = "C200--C208",
journal = "American Journal of Physiology: Cell Physiology",
issn = "0363-6143",
publisher = "American Physiological Society",
number = "1 56-1",

}

RIS

TY - JOUR

T1 - Overexpression or ablation of JNK in skeletal muscle has no effect on glycogen synthase activity

AU - Fujii, Nobuharu

AU - Boppart, Marni D.

AU - Dufresne, Scott D.

AU - Crowley, Patricia F.

AU - Jozsi, Alison C.

AU - Sakamoto, Kei

AU - Yu, Haiyan

AU - Aschenbach, Williams G.

AU - Kim, Shokei

AU - Miyazaki, Hitoshi

AU - Rui, Liangyou

AU - White, Morris F.

AU - Hirshman, Michael F.

AU - Goodyear, Laurie J.

PY - 2004/7/1

Y1 - 2004/7/1

N2 - c-Jun NH2-terminal kinase (JNK) is highly expressed in skeletal muscle and is robustly activated in response to muscle contraction. Little is known about the biological functions of JNK signaling in terminally differentiated muscle cells, although this protein has been proposed to regulate insulin-stimulated glycogen synthase activity in mouse skeletal muscle. To determine whether JNK signaling regulates contraction-stimulated glycogen synthase activation, we applied an electroporation technique to induce JNK overexpression (O/E) in mouse skeletal muscle. Ten days after electroporation, in situ muscle contraction increased JNK activity 2.6-fold in control muscles and 15-fold in the JNK O/E muscles. Despite the enormous activation of JNK activity in JNK O/E muscles, contraction resulted in similar increases in glycogen synthase activity in control and JNK O/E muscles. Consistent with these findings, basal and contraction-induced glycogen synthase activity was normal in muscles of both JNK1- and JNK2-deficient mice. JNK overexpression in muscle resulted in significant alterations in the basal phosphorylation state of several signaling proteins, such as extracellular signal-regulated kinase 1/2, p90 S6 kinase, glycogen synthase kinase 3, protein kinase B/Akt, and p70 S6 kinase, in the absence of changes in the expression of these proteins. These data suggest that JNK signaling regulates the phosphorylation state of several kinases in skeletal muscle. JNK activation is unlikely to be the major mechanism by which contractile activity increases glycogen synthase activity in skeletal muscle.

AB - c-Jun NH2-terminal kinase (JNK) is highly expressed in skeletal muscle and is robustly activated in response to muscle contraction. Little is known about the biological functions of JNK signaling in terminally differentiated muscle cells, although this protein has been proposed to regulate insulin-stimulated glycogen synthase activity in mouse skeletal muscle. To determine whether JNK signaling regulates contraction-stimulated glycogen synthase activation, we applied an electroporation technique to induce JNK overexpression (O/E) in mouse skeletal muscle. Ten days after electroporation, in situ muscle contraction increased JNK activity 2.6-fold in control muscles and 15-fold in the JNK O/E muscles. Despite the enormous activation of JNK activity in JNK O/E muscles, contraction resulted in similar increases in glycogen synthase activity in control and JNK O/E muscles. Consistent with these findings, basal and contraction-induced glycogen synthase activity was normal in muscles of both JNK1- and JNK2-deficient mice. JNK overexpression in muscle resulted in significant alterations in the basal phosphorylation state of several signaling proteins, such as extracellular signal-regulated kinase 1/2, p90 S6 kinase, glycogen synthase kinase 3, protein kinase B/Akt, and p70 S6 kinase, in the absence of changes in the expression of these proteins. These data suggest that JNK signaling regulates the phosphorylation state of several kinases in skeletal muscle. JNK activation is unlikely to be the major mechanism by which contractile activity increases glycogen synthase activity in skeletal muscle.

KW - Electroporation

KW - Exercise

KW - Gene delivery

KW - Muscle contraction

UR - http://www.scopus.com/inward/record.url?scp=2942692413&partnerID=8YFLogxK

U2 - 10.1152/ajpcell.00415.2003

DO - 10.1152/ajpcell.00415.2003

M3 - Journal article

C2 - 15013949

AN - SCOPUS:2942692413

VL - 287

SP - C200-C208

JO - American Journal of Physiology: Cell Physiology

JF - American Journal of Physiology: Cell Physiology

SN - 0363-6143

IS - 1 56-1

ER -

ID: 239777369