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Sleep deprivation induces the unfolded protein response in mouse cerebral cortex
Open accessAbstract
Little is known about the molecular mechanisms underlying sleep. We show the induction of key regulatory proteins in a cellular protective pathway, the unfolded protein response (UPR), following 6 h of induced wakefulness. Using C57/B6 male mice maintained on a 12:12 light/dark cycle, we examined, in cerebral cortex, the effect of different durations of prolonged wakefulness (0, 3, 6, 9 and 12 h) from the beginning of the lights‐on inactivity period, on the protein expression of BiP/GRP78, a chaperone and classical UPR marker. BiP/GRP78 expression is increased with increasing durations of sleep deprivation (6, 9 and 12 h). There is no change in BiP/GRP78 levels in handling control experiments carried out during the lights‐off period. PERK, the transmembrane kinase responsible for attenuating protein synthesis, which is negatively regulated by binding to BiP/GRP78, is activated by dissociation from BiP/GRP78 and by autophosphorylation. There is phosphorylation of the elongation initiation factor 2α and alteration in ribosomal function. These changes are first observed after 6 h of induced wakefulness. Thus, prolonging wakefulness beyond a certain duration induces the UPR indicating a physiological limit to wakefulness.
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The eIF2α-P/UPR pathway is also induced during sleep deprivation of wild type mice, providing an additional mechanistic explanation through which improving disturbances in sleep may be neuroprotective.
“the eIF2 𝛂 -P/UPR pathway is also induced during sleep deprivation of wild type mice, providing an additional mechanistic explanation through which improving disturbances in sleep may be neuroprotective [45]”
From Long-Term Trazodone Use and Cognition: A Potential Therapeutic Role for Slow-Wave Sleep Enhancers (2019) · cites this paper as [45]
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“Furthermore, a PET study has shown that there is a decrease in glucose uptake in the frontal and parietal cortex following sleep deprivation (Thomas et al. 2000).”
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Metadata
- Authors
- Naidoo, N., Giang, W., Galante, R. J., & Pack, A. I.
- Affiliations
- University of Pennsylvania (US)
- Venue
- Journal of Neurochemistry
- Publisher
- Wiley
- Published
- 2005-02-04
- Volume
- 92
- Issue
- 5
- Pages
- 1150-1157
- ISSN
- 0022-3042 (ISSN-L)
- 1471-4159
- OpenAlex
- W1491392377
- Cited by
- 219
- References
- 4
- Citations by year
- 2026: 11 · 2025: 8 · 2024: 15 · 2023: 14 · 2022: 13 · 2021: 8 · 2020: 10 · 2019: 14 · 2018: 10 · 2017: 11 · 2016: 12 · 2015: 6 · 2014: 13 · 2013: 12 · 2012: 9
- FWCI
- 4.20
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Neurochemistry (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute on Aging (P01AG017628)
- National Heart, Lung, and Blood Institute (P50HL060287, U01HL066588)
- Topics
- Life Sciences › Neuroscience › Cognitive Neuroscience › Sleep and Wakefulness Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
- Social Sciences › Psychology › Experimental and Cognitive Psychology › Sleep and Work-Related Fatigue
- Keywords
- sleep deprivation, unfolded protein response, cerebral cortex, BiP/GRP78, PERK, eIF2α phosphorylation, prolonged wakefulness, endoplasmic reticulum stress, ribosomal function, autophosphorylation, molecular chaperones
- MeSH terms
- Endoplasmic Reticulum Chaperone BiP, Animals, Cerebral Cortex, DNA-Binding Proteins, Gene Expression Regulation, Heat-Shock Proteins, Male, Mice, Inbred C57BL, Phosphorylation, Polyribosomes, Protein Denaturation, Sleep Deprivation, Time Factors, Transcription Factors, Blotting, Western, Molecular Chaperones, eIF-2 Kinase, Immunoprecipitation, Mice
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