β-淀粉样蛋白前体蛋白胞内结构域(AICD)研究进展

被引:5
作者
张弦
许华曦
张云武
机构
[1] 厦门大学生物医学研究院厦门大学生命科学学院分子细胞神经科学实验室
关键词
老年性痴呆症; β-淀粉样蛋白前体蛋白; APP胞内结构域;
D O I
暂无
中图分类号
R749.1 [脑器质性精神障碍];
学科分类号
100204 [神经病学];
摘要
老年性痴呆症(Alzheimer's disease,AD)一个重要的病理学特征,是在神经细胞外形成由β-淀粉样蛋白(β-amyloid,Aβ)组成的淀粉样斑(amyloid plaques)。β-淀粉样蛋白前体蛋白(β-amyloid procursor protein,APP)经β-分泌酶和γ-分泌酶依次水解后产生Aβ和APP胞内结构域(APP intracellular domain,AICD)。现在已经知道Aβ在AD的发病机制中起着关键作用,但是关于AICD的生理及病理功能还不清楚。近年来研究发现AICD可以与细胞内多种蛋白相互作用,而且AICD在基因转录、细胞凋亡以及APP的加工和运输过程中均有调节功能。本文针对这一领域的研究进展,对AICD的生理及病理功能进行探讨。
引用
收藏
页码:159 / 164
页数:6
相关论文
共 13 条
[1]
Fe65 does not stabilize AICD during activation of transcription in a luciferase assay [J].
Huysseune, Sandra ;
Kienlen-Campard, Pascal ;
Octave, Jean-Noel .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2007, 361 (02) :317-322
[2]
The intracellular domain of the amyloid precursor protein (AICD) enhances the p53-mediated apoptosis [J].
Ozaki, Toshinori ;
Li, Yuanyuan ;
Kikuchi, Hironobu ;
Tomita, Taisuke ;
Iwatsubo, Takeshi ;
Nakagawara, Akira .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2006, 351 (01) :57-63
[3]
Presenilin-dependent transcriptional control of the Aβ-degrading enzyme neprilysin by intracellular domains of βAPP and APLP [J].
Pardossi-Piquard, R ;
Petit, A ;
Kawarai, T ;
Sunyach, C ;
da Costa, CA ;
Vincent, B ;
Ring, S ;
D'Adamio, L ;
Shen, J ;
Müller, U ;
Hyslop, PS ;
Checler, F .
NEURON, 2005, 46 (04) :541-554
[4]
X11α modulates secretory and endocytic trafficking and metabolism of amyloid precursor protein:: Mutational analysis of the yenpty sequence [J].
King, GD ;
Perez, RG ;
Steinhilb, ML ;
Gaut, JR ;
Turner, RS .
NEUROSCIENCE, 2003, 120 (01) :143-154
[5]
Aph-1, Pen-2, and nicastrin with presenilin generate an active γ-secretase complex [J].
De Strooper, B .
NEURON, 2003, 38 (01) :9-12
[6]
Exchange of N-CoR corepressor and Tip60 coactivator complexes links gene expression by NF-κB and β-amyloid precursor protein [J].
Baek, SH ;
Ohgi, KA ;
Rose, DW ;
Koo, EH ;
Glass, CK ;
Rosenfeld, MG .
CELL, 2002, 110 (01) :55-67
[7]
A presenilin-1/γ-secretase cleavage releases the E-cadherin intracellular domain and regulates disassembly of adherens junctions [J].
Marambaud, P ;
Shioi, J ;
Serban, G ;
Georgakopoulos, A ;
Sarner, S ;
Nagy, V ;
Baki, L ;
Wen, P ;
Efthimiopoulos, S ;
Shao, ZP ;
Wisniewski, T ;
Robakis, NK .
EMBO JOURNAL, 2002, 21 (08) :1948-1956
[8]
Neuron-specific phosphorylation of Alzheimer's β-amyloid precursor protein by cyclin-dependent kinase 5 [J].
Iijima, K ;
Ando, K ;
Takeda, S ;
Satoh, Y ;
Seki, T ;
Itohara, S ;
Greengard, P ;
Kirino, Y ;
Nairn, AC ;
Suzuki, T .
JOURNAL OF NEUROCHEMISTRY, 2000, 75 (03) :1085-1091
[9]
Requirements for presenilin-dependent cleavage of notch and other transmembrane proteins [J].
Struhl, G ;
Adachi, A .
MOLECULAR CELL, 2000, 6 (03) :625-636
[10]
X11α and x11β interact with presenilin-1 via their PDZ domains [J].
Lau, KF ;
McLoughlin, DM ;
Standen, C ;
Miller, CCJ .
MOLECULAR AND CELLULAR NEUROSCIENCE, 2000, 16 (05) :557-565