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HuD regulates coding and noncoding RNA to induce APP→Aβ processing.

Min-Ju Kang1, Kotb Abdelmohsen1, Emmette R Hutchison2

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Summary
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The neuronal protein HuD enhances Alzheimer's disease (AD) pathology by increasing amyloid precursor protein (APP) and BACE1 levels. Elevated HuD in AD brains suggests a key role in disease progression.

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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Genetics

Background:

  • The RNA-binding protein HuD is crucial for neuronal function, particularly in learning and memory.
  • Alzheimer's disease (AD) is characterized by the accumulation of amyloid-beta (Aβ) peptides, derived from amyloid precursor protein (APP).

Purpose of the Study:

  • To investigate the role of HuD in Alzheimer's disease pathogenesis.
  • To identify HuD target transcripts involved in AD.

Main Methods:

  • Investigated HuD interactions with APP and BACE1 mRNA using 3' UTR analysis.
  • Assessed the impact of HuD on mRNA and long noncoding RNA (lncRNA) stability.
  • Analyzed protein and RNA levels in HuD-overexpressing mouse models and human AD cortical tissue.

Main Results:

  • HuD directly binds to APP and BACE1 mRNAs, increasing their stability.
  • HuD stabilizes the lncRNA BACE1AS, which enhances BACE1 expression.
  • Overexpression of HuD in mice led to increased levels of APP, BACE1, BACE1AS, and Aβ.
  • Human AD brains showed significantly higher levels of HuD, APP, BACE1, BACE1AS, and Aβ compared to controls.

Conclusions:

  • HuD promotes the production of APP and the activity of BACE1, a key enzyme in Aβ generation.
  • HuD plays a significant role in Alzheimer's disease pathogenesis by coordinating the expression of critical AD-related genes.
  • Targeting HuD may offer a novel therapeutic strategy for Alzheimer's disease.