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Inflammation Induces TDP-43 Mislocalization and Aggregation.

Ana Sofia Correia1, Priyanka Patel2, Kallol Dutta2

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Inflammation, triggered by lipopolysaccharide (LPS), promotes the mislocalization and aggregation of TAR DNA-binding protein 43 (TDP-43). This exacerbates TDP-43 proteinopathies, suggesting a link between inflammation and neurodegenerative diseases.

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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Immunology

Background:

  • TAR DNA-binding protein 43 (TDP-43) is a key protein implicated in neurodegenerative diseases like amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD).
  • Protein aggregation and mislocalization are hallmarks of these debilitating conditions.

Purpose of the Study:

  • To investigate the role of inflammation in the pathological processes involving TDP-43.
  • To determine if inflammatory stimuli can induce or worsen TDP-43 mislocalization and aggregation.

Main Methods:

  • Exposure of cultured microglia, astrocytes, and NSC-34 motoneuron cells to lipopolysaccharide (LPS) or TNF-alpha (TNF-α).
  • Administration of chronic LPS injections to TDP-43(A315T) transgenic mice.
  • Analysis of TDP-43 localization and aggregation levels in cellular and animal models.

Main Results:

  • LPS exposure induced TDP-43 mislocalization in microglia and astrocytes.
  • TNF-α treatment increased cytoplasmic TDP-43 levels in NSC-34 cells.
  • Chronic LPS administration in TDP-43(A315T) mice exacerbated TDP-43 aggregation in spinal motor neurons.

Conclusions:

  • Inflammation, particularly LPS-induced, can promote TDP-43 mislocalization and aggregation.
  • These findings suggest that inflammation may be a contributing factor to the development or worsening of TDP-43 proteinopathies.
  • Targeting inflammatory pathways could be a potential therapeutic strategy for neurodegenerative disorders involving TDP-43.