RGD Reference Report - Expression of endoplasmic reticulum stress proteins during skeletal muscle disuse atrophy. - Rat Genome Database
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Expression of endoplasmic reticulum stress proteins during skeletal muscle disuse atrophy.

Authors: Hunter, RB  Mitchell-Felton, H  Essig, DA  Kandarian, SC 
Citation: Hunter RB, etal., Am J Physiol Cell Physiol. 2001 Oct;281(4):C1285-90.
RGD ID: 2313240
Pubmed: (View Article at PubMed) PMID:11546666

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 2 alpha 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.


Gene Ontology Annotations    

Biological Process

Objects Annotated

Genes (Rattus norvegicus)
Casq1  (calsequestrin 1)

Additional Information