フルテキストファイル
著者
Hashimoto Yuki Department of Biological Regulation,School of Health Science,Tottori University Faculty of Medicine
Taniguchi Miyako Department of Biological Regulation,School of Health Science,Tottori University Faculty of Medicine 研究者総覧 KAKEN
Kitaura Miki Department of Biological Regulation,School of Health Science,Tottori University Faculty of Medicine
Nakamura Yuka Department of Biological Regulation,School of Health Science,Tottori University Faculty of Medicine
Jinbo Daiki Department of Biological Regulation,School of Health Science,Tottori University Faculty of Medicine
Urakami Katsuya Department of Biological Regulation,School of Health Science,Tottori University Faculty of Medicine 研究者総覧 KAKEN
キーワード
Alzheimer’s disease
concanavalin A
glycoprotein
glycosylation
抄録
Alzheimer’s disease (AD) is the most common cause of dementia in the elderly. It is characterized pathologically by the formation of senile plaques and neurofibrilly tangles in the brain. Diagnostic markers for detecting earlier stages of AD are needed. We measured the intensity of concanavalin A (Con A) binding activities of glycoproteins of the cerebrospinal fluid (CSF) and serum of subjects to clarify the modification of core mannose since we expected that aberrant glycosylation of glycoproteins might be useful as a new biomarker for detecting AD. CSF samples were collected from 15 patients with probable AD (AD group), 5 patients with probable dementia with Lewy bodies (DLB) (DLB group) and 8 controls without dementia (control group), whereas serum samples from 20 patients with probable AD and 20 controls without dementia were also collected. Glycoproteins in the CSF and serum were detected by lectin blotting using Con A. In the CSF of the AD group, 2 Con A binding glycoproteins were significantly higher compared with the control group. Furthermore, using analysis of variance, 3 Con A binding glycoproteins detected from the CSF of the AD group showed significant differences among the 3 groups. The levels of 3 Con A binding glycoproteins were significantly lower than in non-dementia controls in the serum. These changes in Con A binding activities did not depend on the amount of proteins. Therefore, the data indicate that the aberrance of protein glycosylation relates to the pathology of AD, and has some promise as a new biomarker for the diagnosis of AD.
出版者
Tottori University Faculty of Medicine
資料タイプ
学術雑誌論文
ISSN・ISBN
1346-8049
書誌ID
AA00892882
掲載誌名
Yonago Acta medica
最新掲載誌名
Yonago Acta medica
51
1
開始ページ
1
終了ページ
9
発行日
2008-03
著者版フラグ
出版社版
著作権表記
Yonago Acta medica 編集委員会
掲載情報
Yonago Acta medica. 2008, 51(1), 1-9
部局名
医学部・医学系研究科・医学部附属病院
言語
英語