期刊
FEBS LETTERS
卷 582, 期 19, 页码 2899-2904出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2008.07.027
关键词
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. (C) 2008 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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