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Am J Physiol Regul Integr Comp Physiol 276: R308-R316, 1999;
0363-6119/99 $5.00
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Vol. 276, Issue 2, R308-R316, February 1999

Upregulation of M-creatine kinase and glyceraldehyde3-phosphate dehydrogenase: two markers of muscle disuse

Nathalie Cros1, Jacky Muller1, Sophie Bouju1, Geneviève Piétu2, Chantal Jacquet1, Jean J. Léger1, Jean-François Marini3, and Claude A. Dechesne1

1 Institut National de la Santé et de la Recherche Médicale U 300, Faculté Pharmacie, 34060 Montpellier cedex 01; 3 Université de Nice, Centre National de la Recherche Scientifique (CNRS) Unité Mixte de Recherche 6548, 06108 Nice cedex 02; and 2 CNRS Unité Propre de Recherche 420, 94800 Villejuif, France

Muscle disuse induces substantial alterations in the highly plastic skeletal muscle tissues, which occur especially in antigravity slow muscles. We differentially screened a muscle cDNA array to identify modifications in gene profile expression induced in slow rat soleus muscle mechanically unloaded by hindlimb suspension as a model for muscle disuse. This study focused on muscle creatine kinase mRNA and protein and glyceraldehyde-3-phosphate dehydrogenase mRNA, which were found to be upregulated in unweighted muscles. These upregulations were analyzed over a 4-wk time course of hindlimb suspension and compared with variations in myosin heavy chain (MHC) isoforms while specifically focusing on type IIx MHC mRNA and protein. The two metabolic marker upregulations clearly preceded IIx MHC contractile protein upregulation. Muscle creatine kinase upregulation was shown to be an excellent, and the earliest, marker of muscle disuse at mRNA and protein levels.

gene regulation; muscle atrophy


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