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Alzheimer Disease ll: Pathophysiology01:23

Alzheimer Disease ll: Pathophysiology

Alzheimer disease involves structural changes in the brain that begin long before symptoms appear. The most distinctive features are extracellular neuritic plaques and intracellular neurofibrillary tangles.Neuritic plaques form in the cerebral cortex and around blood vessels. These plaques contain a dense core of beta-amyloid (Aβ)—a toxic protein fragment that clumps outside neurons. The core is surrounded by damaged neuronal extensions, as well as reactive astrocytes and microglia. Abnormal...
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Alzheimer's Disease (AD) is a continually advancing neurodegenerative disorder, distinguished by escalating memory loss, cognitive dysfunction, and dementia. The disease unfolds in three stages: preclinical, mild cognitive impairment (MCI), and dementia. Its onset is insidious, and the progression gradual, with the cause not well explained by other disorders.
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Related Experiment Video

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In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein
09:22

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Published on: January 2, 2015

Endogenous Aβ causes cell death via early tau hyperphosphorylation.

G Amadoro1, V Corsetti, M T Ciotti

  • 1Institute of Neurobiology and Molecular Medicine, CNR, Via del Fosso di Fiorano 64-65, 00143 Rome, Italy. g.amadoro@inmm.cnr.it

Neurobiology of Aging
|July 25, 2009
PubMed
Summary

Early Alzheimer's disease (AD) tau changes link to amyloid pathway activation. This interaction causes neuronal dysfunction, offering new therapeutic targets for AD.

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Area of Science:

  • Neuroscience
  • Cell Biology
  • Biochemistry

Background:

  • Alzheimer's disease (AD) involves amyloid-beta (Aβ) overproduction and tau hyperphosphorylation.
  • Previous work identified amyloidogenic pathway activation in hippocampal neurons upon NGF withdrawal.

Purpose of the Study:

  • To investigate the relationship between early tau hyperphosphorylation and the amyloidogenic pathway in neuronal cell death.
  • To elucidate the mechanisms and consequences of site-specific tau modifications in an AD-like model.

Main Methods:

  • Utilized NGF withdrawal in hippocampal neurons to induce AD-like conditions.
  • Employed Aβ antibodies (4G8, 6E10) and secretase inhibitors to block pathological processes.
  • Analyzed tau cleavage, caspase-3 and calpain-I activation, and Akt-GSK3β signaling.
  • Assessed tau detachment from microtubules and mitochondrial trafficking.

Main Results:

  • Observed early, transient, site-specific tau hyperphosphorylation (Ser262, Thr231) preceding apoptotic death.
  • Demonstrated that Aβ antibodies or secretase inhibitors blocked tau hyperphosphorylation and cell death.
  • Confirmed that tau hyperphosphorylation precedes caspase-3 and calpain-I activation.
  • Showed Akt-GSK3β signaling controls tau phosphorylation.
  • Found that site-specific tau hyperphosphorylation detaches tau from microtubules and impairs mitochondrial transport.

Conclusions:

  • Established a direct temporal and causal link between early tau hyperphosphorylation and amyloidogenic pathway activation.
  • Revealed a coordinated interplay between endogenous Aβ and tau post-translational modifications impacting neuronal function.
  • Highlighted a novel mechanism contributing to neuronal compromise in AD pathogenesis.