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TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis.

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Affiliations

  • 1. Department of Psychogeriatrics, Tokyo Institute of Psychiatry, Setagaya-ku, Tokyo 156-8585, Japan.
      Authors
    • Arai T 1
    (1 author)

ORCIDs linked to this article

Biochemical and Biophysical Research Communications, 30 Oct 2006, 351(3):602-611
https://doi.org/10.1016/j.bbrc.2006.10.093 PMID: 17084815 

Abstract 

Ubiquitin-positive tau-negative neuronal cytoplasmic inclusions and dystrophic neurites are common pathological features in frontotemporal lobar degeneration (FTLD) with or without symptoms of motor neuron disease and in amyotrophic lateral sclerosis (ALS). Using biochemical and immunohistochemical analyses, we have identified a TAR DNA-binding protein of 43 kDa (TDP-43), a nuclear factor that functions in regulating transcription and alternative splicing, as a component of these structures in FTLD. Furthermore, skein-like inclusions, neuronal intranuclear inclusions, and glial inclusions in the spinal cord of ALS patients are also positive for TDP-43. Dephosphorylation treatment of the sarkosyl insoluble fraction has shown that abnormal phosphorylation takes place in accumulated TDP-43. The common occurrence of intracellular accumulations of TDP-43 supports the hypothesis that these disorders represent a clinicopathological entity of a single disease, and suggests that they can be newly classified as a proteinopathy of TDP-43.

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Read article at publisher's site: https://doi.org/10.1016/j.bbrc.2006.10.093

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