Am J Physiol Cell Physiol Fuel your research with LabChart
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Am J Physiol Cell Physiol 287: C200-C208, 2004. First published March 10, 2004; doi:10.1152/ajpcell.00415.2003
0363-6143/04 $5.00
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
287/1/C200    most recent
00415.2003v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via ISI Web of Science (16)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Fujii, N.
Right arrow Articles by Goodyear, L. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Fujii, N.
Right arrow Articles by Goodyear, L. J.

CELLULAR METABOLISM

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

Nobuharu Fujii,1 Marni D. Boppart,1 Scott D. Dufresne,1 Patricia F. Crowley,1 Alison C. Jozsi,1 Kei Sakamoto,1 Haiyan Yu,1 Williams G. Aschenbach,1 Shokei Kim,2 Hitoshi Miyazaki,3 Liangyou Rui,1,4 Morris F. White,1,4 Michael F. Hirshman,1 and Laurie J. Goodyear1

1Research Division, Joslin Diabetes Center, and Department of Medicine, Brigham and Women's Hospital and Harvard Medical School, Boston, Massachusetts 02215; 2Department of Pharmacology, Osaka City University Medical School, Osaka 545-8585; 3Gene Experiment Center, Institute of Applied Biochemistry, University of Tsukuba, Tsukuba-City 305-8572, Japan; and 4Howard Hughes Medical Institute, Chevy Chase, Maryland 20815

Submitted 29 September 2003 ; accepted in final form 6 March 2004

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.

electroporation; gene delivery; muscle contraction; exercise


Address for reprint requests and other correspondence: L. J. Goodyear, Joslin Diabetes Center, One Joslin Place, Boston, MA 02215 (E-mail: laurie.goodyear{at}joslin.harvard.edu).




This article has been cited by other articles:


Home page
 Am. J. Physiol. Cell Physiol.Home page
T. Akimoto, P. Li, and Z. Yan
Functional interaction of regulatory factors with the Pgc-1{alpha} promoter in response to exercise by in vivo imaging
Am J Physiol Cell Physiol, July 1, 2008; 295(1): C288 - C292.
[Abstract] [Full Text] [PDF]

Home page
 DiabetesHome page
H. P.M.M. Lauritzen, H. Galbo, J. Brandauer, L. J. Goodyear, and T. Ploug
Large GLUT4 Vesicles Are Stationary While Locally and Reversibly Depleted During Transient Insulin Stimulation of Skeletal Muscle of Living Mice: Imaging Analysis of GLUT4-Enhanced Green Fluorescent Protein Vesicle Dynamics
Diabetes, February 1, 2008; 57(2): 315 - 324.
[Abstract] [Full Text] [PDF]

Home page
 DiabetesHome page
H. F. Kramer, E. B. Taylor, C. A. Witczak, N. Fujii, M. F. Hirshman, and L. J. Goodyear
Calmodulin-Binding Domain of AS160 Regulates Contraction- but Not Insulin-Stimulated Glucose Uptake in Skeletal Muscle
Diabetes, December 1, 2007; 56(12): 2854 - 2862.
[Abstract] [Full Text] [PDF]

Home page
 J. Appl. Physiol.Home page
H. F. Kramer and L. J. Goodyear
Exercise, MAPK, and NF-{kappa}B signaling in skeletal muscle
J Appl Physiol, July 1, 2007; 103(1): 388 - 395.
[Abstract] [Full Text] [PDF]

Home page
 DiabetesHome page
C. A. Witczak, N. Fujii, M. F. Hirshman, and L. J. Goodyear
Ca2+/Calmodulin-Dependent Protein Kinase Kinase-{alpha} Regulates Skeletal Muscle Glucose Uptake Independent of AMP-Activated Protein Kinase and Akt Activation
Diabetes, May 1, 2007; 56(5): 1403 - 1409.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Endocrinol. Metab.Home page
C. R. Bruce, C. Brolin, N. Turner, M. E. Cleasby, F. R. van der Leij, G. J. Cooney, and E. W. Kraegen
Overexpression of carnitine palmitoyltransferase I in skeletal muscle in vivo increases fatty acid oxidation and reduces triacylglycerol esterification
Am J Physiol Endocrinol Metab, April 1, 2007; 292(4): E1231 - E1237.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
H.-J. Koh, D. E. Arnolds, N. Fujii, T. T. Tran, M. J. Rogers, N. Jessen, Y. Li, C. W. Liew, R. C. Ho, M. F. Hirshman, et al.
Skeletal Muscle-Selective Knockout of LKB1 Increases Insulin Sensitivity, Improves Glucose Homeostasis, and Decreases TRB3
Mol. Cell. Biol., November 15, 2006; 26(22): 8217 - 8227.
[Abstract] [Full Text] [PDF]

Home page
 J. Virol.Home page
H. Pan, J. Xie, F. Ye, and S.-J. Gao
Modulation of Kaposi's Sarcoma-Associated Herpesvirus Infection and Replication by MEK/ERK, JNK, and p38 Multiple Mitogen-Activated Protein Kinase Pathways during Primary Infection.
J. Virol., June 1, 2006; 80(11): 5371 - 5382.
[Abstract] [Full Text] [PDF]

Home page
 DiabetesHome page
M. E. Cleasby, J. R. Davey, T. A. Reinten, M. W. Graham, D. E. James, E. W. Kraegen, and G. J. Cooney
Acute Bidirectional Manipulation of Muscle Glucose Uptake by In Vivo Electrotransfer of Constructs Targeting Glucose Transporter Genes
Diabetes, September 1, 2005; 54(9): 2702 - 2711.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Visit Other APS Journals Online
Copyright © 2004 by the American Physiological Society.