國立中山大學,National Sun Yat-sen University,學位論文,thesis/dissertation,大鼠神經瘤N18細胞中經β–amyloid前驅蛋白所誘導產生之細胞凋亡為β–amyloid前驅結合蛋白I所調控 ,β–amyloid precursor protein induced apoptosis is regulated by β–amyloid precursor protein binding protein I in N18 cell

論文名稱 Title	大鼠神經瘤N18細胞中經β–amyloid前驅蛋白所誘導產生之細胞凋亡為β–amyloid前驅結合蛋白I所調控 β–amyloid precursor protein induced apoptosis is regulated by β–amyloid precursor protein binding protein I in N18 cell
系所名稱 Department	生物醫學研究所 Institute of Biomedical Sciences
畢業學年期 Year, semester	91 學年度第 2 學期 The spring semester of Academic Year 91	語文別 Language	中文 Chinese
學位類別 Degree	碩士 Master	頁數 Number of pages	90
研究生 Author	李秉澤 Pin-Tse Li
指導教授 Advisor	呂佩融 Pei-Jung Lu
召集委員 Convenor	洪義人 Yi-Ren Hong
口試委員 Advisory Committee	戴明泓 Ming-Hong Tai
口試日期 Date of Exam	2003-06-09	繳交日期 Date of Submission	2003-06-18
關鍵字 Keywords	阿滋海默症、細胞凋亡 APP, apoptosis, β–amyloid
統計 Statistics	本論文已被瀏覽 5676 次，被下載 13 次 The thesis/dissertation has been browsed 5676 times, has been downloaded 13 times.

中文摘要
阿茲海默症患者有三項重要的病理特徵，分別為neurofibrillary tangle、amyloid plaques與neuronal cell death， neurofibrillary tangle 主要由高度磷酸化的tau蛋白質於神經細胞內沉澱所造成，而amyloid plaques則是由
Abstract
The pathological hallmarks of Alzheimer’s disease (AD) include neurofibrillary tangle, amyloid plaques and neuronal cell death. Neurofibrillary tangle is composed of hyperphosphorylated tau whereas APP (

目次 Table of Contents
目錄中文摘要.......................................................i 英文摘要.....................................................iii 英文縮寫表.....................................................v 前言...........................................................1 材料與方法....................................................11 結果..........................................................36 討論..........................................................50 參考文獻......................................................55 圖與圖解......................................................61 表............................................................78 附錄..........................................................80

參考文獻 References
Barinaga, M. (1998). Is apoptosis key in Alzheimer’s disease? Science 281, 1303-1304. Borg, J. P., Ooi, J., Levy, E. and Margolis, B. (1996). The phosphotyrosine interaction domains of X11 and Fe65 bind to distinct sites on the YENPTY motif of amyloid precursor protein. Mol. Cell Biol. 16, 6229-6241 Chen, Y., L, D., Hirschberg, J. and Neve, R. L. (2000). The amyloid precursor protein-binding protein APP-BP1 drives the cell cycle through the S-M checkpoint and causes apoptosis in neurons. J. Biol. Chem. 275, 8929-8935. Chow, N., Korenberg, J. R., Chen, X. N. and Neve, R. L. (1996). APP-BP1, a novel protein that binds to the carboxyl-terminal region of the amyloid precursor protein. J. Biol. Chem. 271, 11339-11346. Citron, M., Westaway, D., Xia, W., Carlson, G., Diehl, T., Levesque, G. Johnson-Wood, K., Lee, M., Seubert, P., Davis A., D, K., Motter, R., Sherrington, R., Perry, B., Yao, H., Strome, R., Lieberburg, I., Rommens, J., Kim, S., Schenk, D., P, F., St George Hyslop, P. and Selkoe, D. (1997) Mutant presenilins of Alzheimer's disease increase production of 42-residue amyloid beta-protein in both transfected cells and transgenic mice. Nat Med 3, 67-72 Cook, D., Forman, M., Sung, J., Leight, S., Kolson, D., Iwatsubo, T., Lee, V. and Doms, R. (1997) Alzheimer's A beta(1-42) is generated in the endoplasmic reticulum/intermediate compartment of NT2N cells. Nat Med 3, 1021-3 Hartmann, T., Bieger, S., Bruhl, B., Tienari, P., Ida, N., Allsop, D., Roberts, G., Masters, C., Dotti, C., Unsicker, K.and Beyreuther, K. (1997) Distinct sites of intracellular production for Alzheimer's disease A beta40/42 amyloid peptides. Nat Med 3 1016-20 Hung, A. Y. and Selkoe, D. J. (1994). Selective ectodomain phosphorylation and regulated cleavage of beta-amyloid precursor protein. EMBO J. 13, 534-542. Kang. J., Lemaire, H. G., Underback, A., Salbaum, J. M., Masters, C, L., Grezeschik, K, H., Multhaup, G., Beyreuther, K. and Muller-Hill, B. (1987) The precursor of Alzheimer disease amyloid A4 protein resembles a cell-surface receptor. Nature 325, 733-736 Komano, H., Seeger, M., Gandy, S., Wang, G., Krafft, G. and Fuller, R. (1998) Involvement of cell surface glycosyl-phosphatidylinositol-linked aspartyl proteases in

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