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Basic Science and Pathogenesis.

Geoffrey Canet1, Nicolas Sergeant2, Brendan P Lucey3

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Tau protein changes in phosphorylation, secretion, and splicing are linked to circadian rhythms, sleep, and body temperature (BT). This discovery offers new insights into Alzheimer's disease (AD) pathology development.

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Area of Science:

  • Neuroscience
  • Chronobiology
  • Molecular Biology

Background:

  • Hyperphosphorylated tau aggregates are key in Alzheimer's disease (AD) and tauopathies.
  • Sleep disturbances in AD are linked to altered tau phosphorylation and secretion, with poor sleep a potential AD risk factor.
  • Physiological regulation of tau phosphorylation, secretion, and splicing across the sleep-wake cycle is not well understood.

Purpose of the Study:

  • Investigate if tau phosphorylation, secretion, and splicing are governed by circadian rhythms linked to sleep and body temperature (BT).
  • Elucidate the underlying mechanisms by exposing neuronal cells to physiological temperatures during different sleep-wake states.

Main Methods:

  • In vitro, in vivo, and clinical methods were employed.
  • Neuronal cells were exposed to physiological temperatures mimicking sleep-wake cycles.
  • Circadian variations in tau phosphorylation, secretion, and splicing were analyzed in relation to sleep and body temperature.

Main Results:

  • Tau phosphorylation exhibits sleep-driven circadian variations, with hyperphosphorylation occurring during lower body temperature sleep.
  • Body temperature modulates tau secretion, with higher temperatures increasing extracellular and circulating tau.
  • Lower temperatures favored tau exon 10 exclusion, and human CSF tau levels correlated with BT increase post-wakefulness.

Conclusions:

  • Tau phosphorylation, secretion, and splicing follow a circadian pattern regulated by body temperature and sleep.
  • Findings provide novel insights into tau pathology development and spread, particularly relevant given sleep and thermoregulation deficits in AD.