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

Research output: Contribution to journalArticlepeer-review

20 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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