Association of phosphorylation site of tau protein with neuronal apoptosis in Alzheimer's disease

フォーマット:

論文

責任表示:

Kobayashi, Katsuji ; Nakano, Hiroyuki ; Hayashi, Masahiro ; Shimazaki, Masao ; Fukutani, Yuken ; Sasaki, Kazuo ; Sugimori, Kaoru ; Koshino, Yoshifumi

言語:

英語

出版情報:

Elsevier, 2003-04-01

著者名:

Kobayashi, Katsuji

Nakano, Hiroyuki

Hayashi, Masahiro

Shimazaki, Masao

Fukutani, Yuken

Sasaki, Kazuo

Sugimori, Kaoru

Koshino, Yoshifumi

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掲載情報:

Journal of the Neurological Sciences

ISSN:

0022-510x      

巻:

208

開始ページ:

17

終了ページ:

24

バージョン:

author

概要:

金沢大学大学院医学系研究科<br />In addition to neuritic changes and amyloid deposits, neuronal and glial cell apoptosis is an important pathological feature of Alzheimer's disease (AD). Several factors have been postulated as causes or trigge … rs of cellular apoptotic change. This study focused on a quantifiable relationship between phosphorylation sites of tau protein in the neurofibrillary tangles (NFT) and neuronal apoptosis. Five monoclonal anti-tau antibodies (AT180, AT8, HT7, Tau2 and Tau5) for NFT labeling and TdT-mediated UTP nick-end labeling (TUNEL) for localizing apoptotic change were employed. TUNEL-stained neuronal nuclei showed significantly high density in the entorhinal cortex, cornu ammonis (CA) and the parietal cortex. In all regions, density of TUNEL-stained neuronal nuclei showed significantly direct correlation with that of AT8-, AT180- and Tau2-positive neurons. Correlation of TUNEL-stained neuronal nuclei with tau-positive neurons differed depending on the cerebral regions. Density of TUNEL-stained neuronal nuclei showed inverse correlation with that of both AT8-positive and Gallyas-stained NFT in the CA and showed significantly direct correlation with AT8- and HT7-positive neurons in the frontal cortex. Density of tau-positive and Gallyas-stained NFT was higher than that of TUNEL-stained nuclei. We conclude that phosphorylation sites of tau, 159-163 and 202-205, are probably associated with neuronal apoptosis and apoptotic change follows abnormal phosphorylation of tau. 続きを見る

URL:

http://hdl.handle.net/2297/1795