Stress Proteins in Mammalian Hibernation

Many organisms whose body temperatures (T_b) vary when they areexposed to a wide range of environmental temperatures exhibitdifferential expression of stress (heat shock) proteins, presumablyto minimize protein damage during thermal stress. In contrast,we know relatively little about natural variation in stressproteins in homeotherms (i.e., birds and mammals), perhaps dueto the relatively constant T_b that is the hallmark of this vertebrategroup. The significant changes in T_b and metabolism characteristicof mammalian hibernators suggest they could provide insightinto the ecological relevance of stress proteins in mammals.Here we examined differential expression of stress proteinsin several tissues of active and torpid 13-lined ground squirrels.There were few significant differences in expression of inducibleHsp70 protein in liver, kidney, heart, intestine, and skeletalmuscle between active and torpid squirrels, and neither fastingin active squirrels nor torpor bout length in hibernators significantlyaltered Hsp70 abundance in these tissues. However, Hsp70 proteinwas lower in brown adipose tissue (BAT) of torpid compared withactive squirrels. In contrast, abundance of GRP75, the mitochondria]form of Hsp70, was greater in liver, skeletal muscle and intestineof torpid compared with active squirrels, with the greatestchange in intestine. Because GRP75 has been shown to be inducedby non-thermal stressors including glucose deprivation and oxidativestress, these results suggest that the ecological significanceof stress proteins for hibernators may be more closely associatedwith the metabolic demands of heterothermy rather than thermalstress per se.