Abnormal phosphorylation of ser409/410 of TDP-43 in FTLD-U and ALS

作者：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^*

来源：FEBS Letters, 2008, 582(19): 2899-2904.

DOI：10.1016/j.febslet.2008.07.027

• ubiquitin
• inclusions
• tau
• alpha-synuclein
• degradation
• aggregation

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.

• 出版日期2008-8-20
• 单位河北医科大学