A cell biological perspective on Alzheimer's disease

被引：189

作者：

Annaert, W

De Strooper, B

机构：

[1] Flanders Interuniv Inst Biotechnol VIB, Neuronal Cell Biol Lab, B-3000 Louvain, Belgium

[2] Catholic Univ Louvain, Ctr Human Genet, B-3000 Louvain, Belgium

来源：

ANNUAL REVIEW OF CELL AND DEVELOPMENTAL BIOLOGY | 2002年 / 18卷

关键词：

regulated intramembrane proteolysis; presenilin; APP; secretase; nicastrin;

D O I：

10.1146/annurev.cellbio.18.020402.142302

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

The amyloid precursor protein and the proteases cleaving this protein are important players in the pathogenesis of Alzheimer's disease via the generation of the amyloid peptide. Physiologically, the amyloid precursor protein is implied in axonal vesicular trafficking and the proteases are implicated in developmentally important signaling pathways, most significantly those involving regulated intramembrane proteolysis or RIP. We discuss the cell biology behind the amyloid and tangle hypothesis for Alzheimer's disease, drawing on the many links to the fields of cell biology and developmental biology that have been established in the recent years.

引用

收藏

页码：25 / 51

页数：31

相关论文

共 156 条

[41] BACE2, a β-secretase homolog, cleaves at the β site and within the amyloid-β region of the amyloid-β precursor protein [J].

Farzan, M ;

Schnitzler, CE ;

Vasilieva, N ;

Leung, D ;

Choe, H .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2000, 97 (17) :9712-9717

[42] Simvastatin strongly reduces levels of Alzheimer's disease β-amyloid peptides Aβ42 and Aβ40 in vitro and in vivo [J].

Fassbender, K ;

Simons, M ;

Bergmann, C ;

Stroick, M ;

Lütjohann, D ;

Keller, P ;

Runz, H ;

Kühl, S ;

Bertsch, T ;

von Bergmannn, K ;

Hennerici, M ;

Beyreuther, K ;

Hartmann, T .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2001, 98 (10) :5856-5861

[43] Deficient neurogenesis in forebrain-specific presenilin-1 knockout mice is associated with reduced clearance of hippocampal memory traces [J].

Feng, RB ;

Rampon, C ;

Tang, YP ;

Shrom, D ;

Jin, J ;

Kim, M ;

Sopher, B ;

Martin, GM ;

Kim, SH ;

Langdon, RB ;

Sisodia, SS ;

Tsien, JZ .

NEURON, 2001, 32 (05) :911-926

[44] The γ-secretase-cleaved C-terminal fragment of amyloid precursor protein mediates signaling to the nucleus [J].

Gao, YH ;

Pimplikar, SW .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2001, 98 (26) :14979-14984

[45] Kinesin molecular motors: Transport pathways, receptors, and human disease [J].

Goldstein, LSB .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2001, 98 (13) :6999-7003

[46] Formation of neurofibrillary tangles in P301L tau transgenic mice induced by Aβ42 fibrils [J].

Götz, J ;

Chen, F ;

van Dorpe, J ;

Nitsch, RM .

SCIENCE, 2001, 293 (5534) :1491-1495

[47] APH-1 is a multipass membrane protein essential for the Notch signaling pathway in Caenorhabditis elegans embryos [J].

Goutte, C ;

Tsunozaki, M ;

Hale, VA ;

Priess, JR .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2002, 99 (02) :775-779

[48]

Goutte C, 2000, DEVELOPMENT, V127, P2481

[49] Disruption of axonal transport and neuronal viability by amyloid precursor protein mutations in Drosophila [J].

Gunawardena, S ;

Goldstein, LSB .

NEURON, 2001, 32 (03) :389-401

[50] AMYLOID BETA-PEPTIDE IS PRODUCED BY CULTURED-CELLS DURING NORMAL METABOLISM [J].

HAASS, C ;

SCHLOSSMACHER, MG ;

HUNG, AY ;

VIGOPELFREY, C ;

MELLON, A ;

OSTASZEWSKI, BL ;

LIEBERBURG, I ;

KOO, EH ;

SCHENK, D ;

TEPLOW, DB ;

SELKOE, DJ .

NATURE, 1992, 359 (6393) :322-325

← 1 2 3 4 5 6 7 8 9 10 →