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Am J Physiol Cell Physiol 287: C200-C208, 2004. First published March 10, 2004; doi:10.1152/ajpcell.00415.2003
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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).




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