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Glycoprotein glycans play important roles in biological processes including cell adhesion,molecular trafficking and clearance,receptor activation,signal transduction,and endocytosis.The study aimed to examine changes in glycoprotein glycans in skeletal muscles in hibernating Daurian ground squirrels (Spermophilus dauricus) .The animals were randomly assigned to five groups of eight animals: pre-hibernation (PRE) ,hibernation (HIB) ,arousal (ARO) and post-hibernation (POST) .Analysis of glycan profiles was performed using lectin microarrays,and altered glycan patterns in the skeletal muscles were validated by lectin histochemistry.Our results revealed that seven lectins (e.g.PTL-II and SBA) exhibited changes in relative fluorescence intensities in soleus muscles of HIB group compared to PRE group,and 11 lectins (e.g.WGA and RCA120) were changed in ARO group compared to HIB group; for extensor digitorum longus,15 lectins (e.g.DBA and PHA-E+L) showed changes in relative fluorescence intensities in HIB group,and 11 lectins (e.g.DSA and DBA) showed alterations in ARO groups.In conclusion,the precision alteration of protein glycosylation related to the hibernation of daurian ground squirrels may provide useful information to study their protective mechanism against skeletal muscle atrophy during hibernation.