文摘
Previously, eEF-2 phosphorylation has been identified as a reversible mechanism involved inthe inhibition of the elongation phase of translation. In this study, an increased level of phosphorylationof eukaryotic elongation factor-2 (eEF-2) was observed in the brains and livers of hibernating groundsquirrels. In brain and liver from hibernators, eEF-2 kinase activity was increased relative to that of activeanimals. The activity of protein phosphatase 2A (PP2A), a phosphatase that dephosphorylates eEF-2, wasalso decreased in brain and liver from hibernators. This was associated with an increase in the level ofinhibitor 2 of PP2A (I2PP2A), although there was an increase in the level of the catalytic subunit of PP2A(PP2A/C) in hibernating brains and livers. These results indicate that eEF-2 phosphorylation representsa specific and previously uncharacterized mechanism for inhibition of the elongation phase of proteinsynthesis during hibernation. Increased levels of eEF-2 phosphorylation in hibernators appear to be acomponent of the regulated shutdown of cellular functions that permits hibernating animals to toleratesevere reductions in cerebral blood flow and oxygen delivery capacity.