Abstract.
Protein synthesis is severely depressed in hibernating mammals. In the absence of significant protein synthesis, the continued turnover of proteins as a function of normal cellular activity would result in the net depletion of protein pools. We measured levels of ubiquitylated proteins in the gut of thirteen-lined ground squirrels (Spermophilus tridecemlineatus) and liver of golden-mantled ground squirrels (Spermophilus lateralis). In both tissues, ubiquitin conjugate concentrations increased during entrance into torpor and were elevated 2–3 fold by late torpor compared with levels in active animals. The data are consistent with a depression of proteolysis with a resultant high level of ubiquitylated proteins during the natural hypothermia of torpor. The periodic returns to euthermy during the hibernation season allow for degradation of these conjugated proteins and may serve to restore protein pools.
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van Breukelen, .F., Carey, .H. Ubiquitin conjugate dynamics in the gut and liver of hibernating ground squirrels. J Comp Physiol B 172, 269–273 (2002). https://doi.org/10.1007/s00360-002-0252-5
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DOI: https://doi.org/10.1007/s00360-002-0252-5