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Basic Science and Pathogenesis.

Leonard Petrucelli1

  • 1Mayo Clinic, Jacksonville, FL, USA.

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TAR DNA binding protein of 43 kDa (TDP-43) co-pathology worsens Alzheimer's disease (AD) progression. Researchers identified a novel biomarker for TDP-43 dysfunction and linked it to endolysosomal pathway disruption in AD.

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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Pathology

Background:

  • Alzheimer's disease (AD) is characterized by tau tangles and Aβ plaques, but TDP-43 inclusions are present in many cases, correlating with more severe disease.
  • Understanding the role of TDP-43 proteinopathy in AD pathogenesis is crucial for developing precision medicine approaches.

Purpose of the Study:

  • To investigate the contribution of TAR DNA binding protein of 43 kDa (TDP-43) proteinopathy to Alzheimer's disease (AD) pathogenesis.
  • To develop sensitive biomarkers for tracking TDP-43 dysfunction in living patients.

Main Methods:

  • Exploiting mRNA misprocessing events, such as cryptic exon inclusion, caused by TDP-43 nuclear clearance to create biomarkers.
  • Analyzing aberrant transcripts and their impact on molecular pathways in the brain.
  • Investigating the link between TDP-43 dysfunction and endolysosomal pathway activity.

Main Results:

  • Developed and verified a novel biomarker for TDP-43 dysfunction, a cryptic form of HDGFL2, detectable in post-mortem AD brain tissue with mixed pathology.
  • Uncovered a connection between TDP-43 dysfunction and impaired endolysosomal activity.
  • Demonstrated that disrupting the endolysosomal pathway can induce TDP-43 pathology and neurodegeneration in vivo.

Conclusions:

  • TDP-43 co-pathology significantly impacts AD pathogenesis, potentially through disruption of the neuronal endolysosomal pathway.
  • Further exploration of TDP-43 dysfunction consequences may lead to new AD biomarker and therapeutic strategies.