Abnormal phosphorylation of Ser409/410 of TDP-43 in FTLD-U and ALS

A monoclonal antibody specific for phosphoserines 409 and 410 of TDP-43 (mAb pS409/410) has been produced. It strongly stained TDP-43-positive inclusions in brain of patients with frontotemporal lobar degeneration and amyotrophic lateral sclerosis, but did not stain nuclei, in which normal TDP-43 is...

Full description

Saved in:
Bibliographic Details
Published in:FEBS letters 2008-08, Vol.582 (19), p.2899-2904
Main Authors: Inukai, Yuki, Nonaka, Takashi, Arai, Tetsuaki, Yoshida, Mari, Hashizume, Yoshio, Beach, Thomas G., Buratti, Emanuele, Baralle, Francisco E., Akiyama, Haruhiko, Hisanaga, Shin-ichi, Hasegawa, Masato
Format: Article
Language:English
Subjects:
Aggregation
Amyotrophic Lateral Sclerosis - metabolism
Animals
Antibodies, Monoclonal - immunology
Brain - metabolism
Degradation
Dementia - metabolism
DNA-Binding Proteins - immunology
DNA-Binding Proteins - metabolism
Humans
Inclusions
Phosphorylation
Phosphoserine - analysis
Phosphoserine - immunology
Rats
Rats, Wistar
Serine - metabolism
Tau
Ubiquitin
α-synuclein
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:A monoclonal antibody specific for phosphoserines 409 and 410 of TDP-43 (mAb pS409/410) has been produced. It strongly stained TDP-43-positive inclusions in brain of patients with frontotemporal lobar degeneration and amyotrophic lateral sclerosis, but did not stain nuclei, in which normal TDP-43 is localized. It did not recognize TDP-43 rapidly extracted from brains of rats at various developmental stages, strongly suggesting that phosphorylation of Ser409/410 is an abnormal event. Analysis of postmortem changes of TDP-43 revealed that the amounts of Sarkosyl-insoluble, urea-soluble full-length TDP-43 and a 35 kDa N-terminal fragment increased time-dependently.
ISSN:0014-5793
1873-3468
DOI:10.1016/j.febslet.2008.07.027