The stress protein/chaperone Grp94 counteracts muscle disuse atrophy by stabilizing subsarcolemmal neuronal nitric oxide synthase.

ABSTRACT:

Aims

Redox and growth-factor imbalance fosters muscle disuse atrophy. Since the endoplasmic-reticulum chaperone Grp94 is required for folding insulin-like growth factors (IGFs) and for antioxidant cytoprotection, we investigated its involvement in muscle mass loss due to inactivity.

Results

Rat soleus muscles were transfected in vivo and analyzed after 7 days of hindlimb unloading, an experimental model of muscle disuse atrophy, or standard caging. Increased muscle protein carbonylation and decreased Grp94 protein levels (p<0.05) characterized atrophic unloaded solei. Recombinant Grp94 expression significantly reduced atrophy of transfected myofibers, compared with untransfected and empty-vector transfected ones (p<0.01), and decreased the percentage of carbonylated myofiber

SUBMITTER: Vitadello M 

PROVIDER: S-EPMC4025603 | biostudies-literature | 2014 Jun

REPOSITORIES: biostudies-literature