Regular alteration of protein glycosylation in skeletal muscles of hibernating Daurian ground squirrels (Spermophilus dauricus).

Abstract

Glycosylation is one of the most common post-translational protein modifications and is closely associated with muscle atrophy. This study aims to investigate the changes in glycan profiles in the fast-twitch extensor digitorum longus (EDL) muscles of Daurian ground squirrels (Spermophilus dauricus) during hibernation as well as the correlation between protein glycosylation and muscle atrophy prevention in hibernating animals. The results showed that there was no significant change in the muscle-to-body mass ratio, muscle fiber cross-sectional area (CSA), fiber distribution and ultrastructures in the EDL muscles of ground squirrels during hibernation. Alterations of six glycans comprising sialic acid α2-3 galactose (Sia2-3Gal) and Fucα1-2Galβ1-4Glc(NAc) in the EDL muscles were observed. In addition, the observed downregulation of sialyltransferase (ST3Gals) mRNA levels and upregulation of fucosyltransferase (FUT1 and FUT2) mRNA levels during hibernation and the subsequent restoration to normal levels during periodic interbout arousal were consistent with the changes in sialic acid and fucose modifications. Our results indicate that changes in ST3Gals and FUTs in the EDL muscles of Daurian ground squirrels during hibernation can alter sialylation and fucosylation of muscle glycoproteins, which may protect the skeletal muscles of hibernating Daurian ground squirrels from disuse atrophy.