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Abnormal phosphorylation of Ser409/410 of TDP‐43 in FTLD‐U and ALS
Author(s) -
Inukai Yuki,
aka Takashi,
Arai Tetsuaki,
Yoshida Mari,
Hashizume Yoshio,
Beach Thomas G.,
Buratti Emanuele,
Baralle Francisco E.,
Akiyama Haruhiko,
Hisanaga Shin-ichi,
Hasegawa Masato
Publication year - 2008
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2008.07.027
Subject(s) - frontotemporal lobar degeneration , amyotrophic lateral sclerosis , phosphorylation , pathology , monoclonal antibody , stain , microbiology and biotechnology , chemistry , biology , medicine , frontotemporal dementia , staining , antibody , biochemistry , immunology , disease , dementia
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.