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Am J Physiol Cell Physiol 281: C1285-C1290, 2001;
0363-6143/01 $5.00
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Vol. 281, Issue 4, C1285-C1290, October 2001

Expression of endoplasmic reticulum stress proteins during skeletal muscle disuse atrophy

R. Bridge Hunter1, Heather Mitchell-Felton1, David A. Essig2, and Susan C. Kandarian1

1 Department of Health Sciences, Boston University, Boston, Massachusetts 02215; and 2 Department of Biology, Geneva College, Beaver Falls, Pennsylvania 15010

Disuse atrophy of skeletal muscle leads to an upregulation of genes encoding sarcoplasmic reticulum (SR) calcium-handling proteins. Because many of the proteins that are induced with endoplasmic reticulum (ER) stress are ER calcium-handling proteins, we sought to determine whether soleus muscle atrophy was associated with a prototypical ER stress response. Seven days of rat hindlimb unloading did not alter expression of ubiquitous ER stress proteins such as Grp78, calreticulin, and CHOP/GADD-153, nor other proteins that have been shown to be activated by ER stressors such as vinculin, the type I D-myo-inositol 1,4,5-trisphosphate receptor, or protein kinase R, a eukaryotic initiation factor 2alpha kinase. On the other hand, expression of heme oxygenase-1 (HO-1), an antioxidant ER stress protein, was significantly increased 2.2-fold. In addition, unloading led to an increase in calsequestrin, the muscle-specific SR calcium-binding protein, at both the mRNA (68%) and protein (24%) levels. Although disuse atrophy is associated with a significant remodeling of muscle-specific proteins controlling SR calcium flux, it is not characterized by a prototypical ER stress response. However, the upregulation of HO-1 may indicate ER adaptation to oxidative stress during muscle unloading.

unloading; sarcoplasmic reticulum; heme oxygenase; CHOP/GADD-153; vinculin; 78-kDa glucose-regulated protein; calreticulin; calsequestrin; calcium; inositol trisphosphate receptor; protein kinase R


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