Open AccessTDP‐43 as structure‐based biomarker in amyotrophic lateral sclerosis
Author(s) -
Beyer Léon,
Günther René,
Koch Jan Christoph,
Klebe Stephan,
Hagenacker Tim,
Lingor Paul,
Biesalski AnneSophie,
Hermann Andreas,
Nabers Andreas,
Gold Ralf,
Tönges Lars,
Gerwert Klaus
Publication year - 2021
Publication title -
annals of clinical and translational neurology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.824
H-Index - 42
ISSN - 2328-9503
DOI - 10.1002/acn3.51256
Subject(s) - amyotrophic lateral sclerosis , medicine , biomarker , transactivation , cerebrospinal fluid , pathology , oncology , disease , gene , gene expression , biochemistry , biology
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.