Advances with RNA interference in Alzheimer's disease research

被引:34
作者
Chen, Shun [1 ,2 ]
Ge, Xuemei [2 ]
Chen, Yinghui [3 ]
Lv, Nan [2 ]
Liu, Zhenguo [1 ]
Yuan, Weien [2 ]
机构
[1] Shanghai Jiao Tong Univ, Xinhua Hosp, Sch Med, Dept Neurol, Shanghai 200092, Peoples R China
[2] Shanghai Jiao Tong Univ, Sch Pharm, Shanghai 200092, Peoples R China
[3] Fudan Univ, Jinshan Hosp, Dept Neurol, Shanghai 200433, Peoples R China
基金
美国国家科学基金会;
关键词
RNAi; beta-amyloid; tau; amyloid precursor protein; AMYLOID PRECURSOR PROTEIN; BETA-SECRETASE CLEAVAGE; NEUROFIBRILLARY TANGLES; CURRENT PROGRESS; ALPHA-SECRETASE; TAU; PEPTIDE; LOCALIZATION; THERAPEUTICS; SIRNA;
D O I
10.2147/DDDT.S40229
中图分类号
R914 [药物化学];
学科分类号
100701 ;
摘要
Alzheimer's disease (AD) is a progressive neurodegenerative disorder characterized clinically by memory and cognitive dysfunction. Unfortunately, there is no effective therapeutic method for AD treatment or ways to halt disease progression. Many mechanisms are involved in the disease, including genes mutation and protein dysfunction. RNA interference (RNAi) technology may potentially be able to control AD. It can inhibit the protein expression of specific genes by activating a sequence-specific RNA degradation process. This is a powerful tool with which to study gene function, investigate the mechanism of the disease, and validate drug targets. In this review, we highlight the advances in RNAi technology in the investigation and treatment of AD.
引用
收藏
页码:117 / 125
页数:9
相关论文
共 98 条
[1]   ADAMs family members as amyloid precursor protein α-secretases [J].
Allinson, TMJ ;
Parkin, ET ;
Turner, AJ ;
Hooper, NM .
JOURNAL OF NEUROSCIENCE RESEARCH, 2003, 74 (03) :342-352
[2]   Hyperphosphorylation induces self-assembly of τ into tangles of paired helical filaments/straight filaments [J].
Alonso, AD ;
Zaidi, T ;
Novak, M ;
Grundke-Iqbal, I ;
Iqbal, K .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2001, 98 (12) :6923-6928
[3]   Delivery of siRNA to the mouse brain by systemic injection of targeted exosomes [J].
Alvarez-Erviti, Lydia ;
Seow, Yiqi ;
Yin, HaiFang ;
Betts, Corinne ;
Lakhal, Samira ;
Wood, Matthew J. A. .
NATURE BIOTECHNOLOGY, 2011, 29 (04) :341-U179
[4]  
Alzheimer A., 1907, Allg Zeitschrift Psychiatr, V64, P146, DOI DOI 10.1002/CA.980080612
[6]   High-content siRNA screening of the kinome identifies kinases involved in Alzheimer's disease-related tau hyperphosphorylation [J].
Azorsa, David O. ;
Robeson, RiLee H. ;
Frost, Danielle ;
Hoovet, Bessie Meec ;
Brautigam, Gillian R. ;
Dickey, Chad ;
Beaudry, Christian ;
Basu, Gargi D. ;
Holz, David R. ;
Hernandez, Joseph A. ;
Bisanz, Kristen M. ;
Gwinn, Leslie ;
Grover, Andrew ;
Rogers, Joseph ;
Reiman, Eric M. ;
Hutton, Michael ;
Stephan, Dietrich A. ;
Mousses, Spyro ;
Dunckley, Travis .
BMC GENOMICS, 2010, 11
[7]   Role of genes linked to sporadic Alzheimer's disease risk in the production of β-amyloid peptides [J].
Bali, Jitin ;
Gheinani, Ali Hashemi ;
Zurbriggen, Sebastian ;
Rajendran, Lawrence .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2012, 109 (38) :15307-15311
[8]   ABNORMAL ALZHEIMER-LIKE PHOSPHORYLATION OF TAU-PROTEIN BY CYCLIN-DEPENDENT KINASES CDK2 AND CDK5 [J].
BAUMANN, K ;
MANDELKOW, EM ;
BIERNAT, J ;
PIWNICAWORMS, H ;
MANDELKOW, E .
FEBS LETTERS, 1993, 336 (03) :417-424
[9]   A furin-like convertase mediates propeptide cleavage of BACE, the Alzheimer's β-secretase [J].
Bennett, BD ;
Denis, P ;
Haniu, M ;
Teplow, DB ;
Kahn, S ;
Louis, JC ;
Citron, M ;
Vassar, R .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (48) :37712-37717
[10]   Alzheimer's disease [J].
Scheltens, Philip ;
De Strooper, Bart ;
Kivipelto, Miia ;
Holstege, Henne ;
Chetelat, Gael ;
Teunissen, Charlotte E. ;
Cummings, Jeffrey ;
van der Flier, Wiesje M. .
LANCET, 2021, 397 (10284) :1577-1590