Molecular Dissection of TDP-43 Proteinopathies View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2011-11

AUTHORS

Masato Hasegawa, Takashi Nonaka, Hiroshi Tsuji, Akira Tamaoka, Makiko Yamashita, Fuyuki Kametani, Mari Yoshida, Tetsuaki Arai, Haruhiko Akiyama

ABSTRACT

TDP-43 has been identified as a major component of ubiquitin-positive tau-negative cytoplasmic inclusions in frontotemporal lobar degeneration with ubiquitin-positive inclusions (FTLD-U) and in amyotrophic lateral sclerosis (ALS). We raised antibodies to phosphopeptides representing 36 out of 64 candidate phosphorylation sites of human TDP-43 and showed that the antibodies to pS379, pS403/404, pS409, pS410 and pS409/410 labeled the inclusions, but not the nuclei. Immunoblot analyses demonstrated that the antibodies recognized TDP-43 at ~45 kDa, smearing substances and 18-26 kDa C-terminal fragments. Furthermore, the band patterns of the C-terminal fragments differed between neuropathological subtypes, but were indistinguishable between brain regions and spinal cord in each individual patient. Protease treatment of Sarkosyl-insoluble TDP-43 suggests that the different band patterns of the C-terminal fragments reflect different conformations of abnormal TDP-43 molecules between the diseases. These results suggest that molecular species of abnormal TDP-43 are different between the diseases and that they propagate from affected cells to other cells during disease progression and determine the clinicopathological phenotypes of the diseases. More... »

PAGES

480-485

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s12031-011-9571-x

DOI

http://dx.doi.org/10.1007/s12031-011-9571-x

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1028842281

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/21678031


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