Trafficking of Alzheimer's disease-related membrane proteins and its participation in disease pathogenesis

被引:46
作者
Suzuki, Toshiharu [1 ]
Araki, Yoichi [1 ]
Yamamoto, Tohru [1 ]
Nakaya, Tadashi [1 ]
机构
[1] Hokkaido Univ, Grad Sch Pharmaceut Sci, Kita Ku, Sapporo, Hokkaido 0600812, Japan
关键词
Alzheimer's disease; amyloid beta-protein precursor; cargo-receptor; kinesin; membrane trafficking; neurodegeneration;
D O I
10.1093/jb/mvj121
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Alzheimer's disease (AD) is a common neurodegenerative disorder that causes senile dementia. The pathological characteristics are the appearance of neurofibrillary tangles comprising abnormally phosphorylated tau and senile plaques composed of amyloid P-protein depositions. Amyloid P-protein precursor (APP) and presenilin (PS) are known to be causative genes of familial AD. Recent analyses have documented that APP functions in the axonal transport of vesicles and PS regulates intracellular protein trafficking. Dystrophic neurites, in which APP and Alcadein accumulate in swollen axons, are also observed in AD brain. These pathological characteristics and the features of AD-related proteins suggest that AD is a disease of the vesicular transport system. Here we review recent progress of research on AD pathogenesis from the viewpoint of membrane trafficking.
引用
收藏
页码:949 / 955
页数:7
相关论文
共 51 条
[1]   Phosphorylation-dependent regulation of the interaction of amyloid precursor protein with Fe65 affects the production of β-amyloid [J].
Ando, K ;
Iijima, K ;
Elliott, JI ;
Kirino, Y ;
Suzuki, T .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (43) :40353-40361
[2]   Coordinated metabolism of alcadein and amyloid β-protein precursor regulates FE65-dependent gene transactivation [J].
Araki, Y ;
Miyagi, N ;
Kato, N ;
Yoshida, T ;
Wada, S ;
Nishimura, M ;
Komano, H ;
Yamamoto, T ;
De Strooper, B ;
Yamamoto, K ;
Suzuki, T .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (23) :24343-24354
[3]   Novel cadherin-related membrane proteins, alcadeins, enhance the X11-like protein-mediated stabilization of amyloid β-protein precursor metabolism [J].
Araki, Y ;
Tomita, S ;
Yamaguchi, H ;
Miyagi, N ;
Sumioka, A ;
Kirino, Y ;
Suzuki, T .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (49) :49448-49458
[4]   The X11α protein slows cellular amyloid precursor protein processing and reduces Aβ40 and Aβ42 secretion [J].
Borg, JP ;
Yang, YN ;
De Taddéo-Borg, M ;
Margolis, B ;
Turner, RS .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (24) :14761-14766
[5]   A transcriptively active complex of APP with Fe65 and histone acetyltransferase Tip60 [J].
Cao, XW ;
Südhof, TC .
SCIENCE, 2001, 293 (5527) :115-120
[6]   Maturation and pro-peptide cleavage of β-secretase [J].
Capell, A ;
Steiner, H ;
Willem, M ;
Kaiser, H ;
Meyer, C ;
Walter, J ;
Lammich, S ;
Multhaup, G ;
Haass, C .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (40) :30849-30854
[7]   APL-1, A CAENORHABDITIS-ELEGANS GENE ENCODING A PROTEIN RELATED TO THE HUMAN BETA-AMYLOID PROTEIN-PRECURSOR [J].
DAIGLE, I ;
LI, C .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1993, 90 (24) :12045-12049
[8]   Phenotypic and biochemical analyses of BACE1- and BACE2-deficient mice [J].
Dominguez, D ;
Tournoy, J ;
Hartmann, D ;
Huth, T ;
Cryns, K ;
Deforce, S ;
Serneels, L ;
Camacho, IE ;
Marjaux, E ;
Craessaerts, K ;
Roebroek, AJM ;
Schwake, M ;
D'Hooge, R ;
Bach, P ;
Kalinke, U ;
Moechars, D ;
Alzheimer, C ;
Reiss, K ;
Saftig, P ;
De Strooper, B .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2005, 280 (35) :30797-30806
[9]   Presenilin 1 mediates the turnover of telencephalin in hippocampal neurons via an autophagic degradative pathway [J].
Esselens, C ;
Oorschot, V ;
Baert, V ;
Raemaekers, T ;
Spittaels, K ;
Serneels, L ;
Zheng, H ;
Saftig, P ;
De Strooper, B ;
Klumperman, J ;
Annaert, W .
JOURNAL OF CELL BIOLOGY, 2004, 166 (07) :1041-1054
[10]   The cell surface metalloprotease disintegrin Kuzbanian is required for axonal extension in Drosophila [J].
Fambrough, D ;
Pan, DJ ;
Rubin, GM ;
Goodman, CS .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1996, 93 (23) :13233-13238