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TDP-43 as structure-based biomarker in amyotrophic lateral sclerosis

  • Léon Beyer
  • , René Günther
  • , Jan Christoph Koch
  • , Stephan Klebe
  • , Tim Hagenacker
  • , Paul Lingor
  • , Anne Sophie Biesalski
  • , Andreas Hermann
  • , Andreas Nabers
  • , Ralf Gold
  • , Lars Tönges
  • , Klaus Gerwert
  • Max-Planck-lnstitut für Kohlenforschung
  • Technische Universität Dresden
  • German Center for Neurodegenerative Diseases (DZNE)
  • University Medical Center
  • University Hospital of Essen
  • Huntington-Zentrum (NRW) Bochum im St. Josef Hospital
  • University of Rostock

Research output: Contribution to journalArticlepeer-review

24 Scopus citations

Abstract

Pathologic alterations of Transactivation response DNA-binding protein 43 kilo Dalton (TDP-43) are a major hallmark of amyotrophic lateral sclerosis (ALS). In this pilot study, we analyzed the secondary structure distribution of TDP-43 in cerebrospinal fluid of ALS patients (n = 36) compared to Parkinson´s disease patients (PD; n = 30) and further controls (Ctrl; n = 24) using the immuno-infrared sensor technology. ALS patients could be discriminated from PD and Ctrl with a sensitivity/specificity of 89 %/77 % and 89 %/83 %, respectively. Our findings demonstrate that TDP-43 misfolding measured by the immuno-infrared sensor technology has the potential to serve as a biomarker candidate for ALS.

Original languageEnglish
Pages (from-to)271-277
Number of pages7
JournalAnnals of Clinical and Translational Neurology
Volume8
Issue number1
DOIs
StatePublished - Jan 2021

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