Elderly mice manage protein misfolding less efficiently than young mice, report Naidoo et al. this week. Because protein misfolding can lead to protein aggregation and neurodegeneration, cells initiate the "unfolded protein response" when unfolded proteins begin to accumulate in the endoplasmic reticulum (ER).
If ER stress continues, an ER-induced apoptosis pathway is activated. Naidoo et al. previously showed that sleep deprivation activates the unfolded protein response in young mice: the chaperone BiP (which helps ensure proper folding) is upregulated, and the translation initiation factor eIF2α is inactivated by phosphorylation.
The authors now show that baseline levels of BiP and phosphorylated eIF2α were lower in aged mice than in young, and the levels were not altered by sleep deprivation.
Furthermore, baseline levels of pro-apoptotic proteins were higher in aged mice and were further elevated by sleep deprivation in aged mice, but not young mice, suggesting that a deficient unfolded protein response increases apoptosis.-Society for Neuroscience
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