Amyotrophic lateral sclerosis-associated gene mutations and ALS animal models

doi:10.3969.j.issn.1671-7856.2017.10.018

Home > Archive>Volume 27, Issue 10, 2017 >89-95. DOI:10.3969.j.issn.1671-7856.2017.10.018

Amyotrophic lateral sclerosis-associated gene mutations and ALS animal models
DOI:
                        10.3969.j.issn.1671-7856.2017.10.018
                    
CSTR:
                        
                    
Author:
                        ZHANG LiZHANG Li
Institute of Laboratory Animal Sciences, Chinese Academy of Medical Sciences & Comparative Medical Center, Peking Union Medical College, Key Laboratory of Human Disease Comparative Medicine, National Health and Family Planning Commission of P. R. C, Beijing 100021, China
Find this author on All Journals
Find this author on BaiDu
Search for this author on this site
ZHANG Lian-fengZHANG Lian-feng
Institute of Laboratory Animal Sciences, Chinese Academy of Medical Sciences & Comparative Medical Center, Peking Union Medical College, Key Laboratory of Human Disease Comparative Medicine, National Health and Family Planning Commission of P. R. C, Beijing 100021, China;Neuroscience Center, Chinese Academy of Medical Sciences, Beijing 100730, China
Find this author on All Journals
Find this author on BaiDu
Search for this author on this site

                    
Affiliation:
Clc Number:
Fund Project:

Article

Figures

Metrics

Reference [32]

Cited by

Materials

Comments

Abstract:

Amyotrophic lateral sclerosis (ALS) is a progressive neurodegenerative disease characterized by a selective loss of upper and lower motor neurons that lead to paralysis and even death. Mutations in a large number of genes, including FUS/TLS, EPHA4, SS18 L1, ATXN2 and C9ORF72, are identified to the casual genes of ALS, which broadens our understanding of the role of RNA modulation in ALS pathogenesis. This review summarized ALS-associated genes and the related ALS rodent models.

Key words:Amyotrophic lateral sclerosis;Gene mutation;Animal model

Reference

[1] Andersen PM, Nilsson P, Ala-Hurula V, et al. Amyotrophic lateral sclerosis associated with homozygosity for an Asp90Ala mutation in CuZn-superoxide dismutase[J]. Nat Genet, 1995, 10(1):61-66.

[2] Ackerley S, James PA, Kalli A, et al. A mutation in the small heat-shock protein HSPB1 leading to distal hereditary motor neuronopathy disrupts neurofilament assembly and the axonal transport of specific cellular cargoes[J]. Hum Molec Genet, 2006, 15(2):347-354.

[3] Krishnan J, Lemmens R, Robberecht W, et al. Role of heat shock response and Hsp27 in mutant SOD1-dependent cell death[J]. Exp Neurol, 2006, 200(2):301-310.

[4] Hideyama T, Kwak S. When does ALS start? ADAR2-GluA2 hypothesis for the etiology of sporadic ALS[J]. Front Mol Neurosci, 2011, 4:33.

[5] Van Hoecke A, Schoonaert L, Lemmens R, et al. EPHA4 is a disease modifier of amyotrophic lateral sclerosis in animal models and in humans[J]. Nat Med, 2012, 18(9):1418-1422.

[6] Deng H, Gao K, Jankovic J. The role of FUS gene variants in neurodegenerative diseases[J]. Nat Rev Neurol, 2014, 10(6):337-348.

[7] Bennion Callister J, Pickering-Brown SM. Pathogenesis/genetics of frontotemporal dementia and how it relates to ALS[J]. Exp Neurol, 2014, 262 Pt B:84-90.

[8] Cañete-Soler R, Wu J, Zhai J, et al. p190RhoGEF binds to a destabilizing element in the 3'-untranslated region of light neurofilament subunit mRNA and alters the stability of the transcript.[J]. J Biol Chem, 2001, 276(34):32046-32050.

[9] Chen YZ, Bennett CL, Huynh HM, et al. DNA/RNA helicase gene mutations in a form of juvenile amyotrophic lateral sclerosis (ALS4)[J]. Am J Hum Genet, 2004, 74(6):1128-1135.

[10] Liu X, Lu M, Tang L, et al. ATXN2 CAG repeat expansions increase the risk for Chinese patients with amyotrophic lateral sclerosis[J]. Neurobiol Aging, 2013, 34(9):2236. e5-8.

[11] Elden AC, Kim HJ, Hart MP, at al. Ataxin-2 intermediate-length polyglutamine expansions are associated with increased risk for ALS[J]. Nature, 2010, 466(7310):1069-1075.

[12] Wu CH, Fallini C, Ticozzi N, et al. Mutations in the profilin 1 gene cause familial amyotrophic lateral sclerosis[J]. Nature. 2012, 488(7412):499-503.

[13] Teyssou E, Vandenberghe N, Moigneu C, et al. Genetic analysis of SS18L1 in French amyotrophic lateral sclerosis[J]. Neurobiol. Aging, 2014, 35(5):e9-e12.

[14] Renton AE, Traynor BJ. CRESTing the ALS mountain[J]. Nat Neurosci, 2013, 16(7):774-775.

[15] Haeusler AR, Donnelly CJ, Periz G, et al. C9 or f72 nucleotide repeat structures initiate molecular cascades of disease[J]. Nature. 2014, 507(7491):195-200.

[16] Maruyama H, Morino H, Ito H. Mutations of optineurin in amyotrophic lateral sclerosis[J]. Nature, 2010, 465(7295):223-226.

[17] Renton AE, Chiò A, Traynor BJ. State of play in amyotrophic lateral sclerosis genetics[J]. Nat Neurosci, 2014, 17(1):17-23.

[18] Gal J, Ström AL, Kwinter DM, et al. Sequestosome 1/p62 links familial ALS mutant SOD1 to LC3 via an ubiquitin-independent mechanism[J]. J Neurochem, 2009, 111(4):1062-1073.

[19] Zou ZY, Liu MS, Li XG, et al. Screening of VCP mutations in Chinese amyotrophic lateral sclerosis patients[J]. Neurobiol Aging, 2013, 34(5):1519.e3-4.

[20] Su XW, Broach JR, Connor JR, et al. Genetic heterogeneity of amyotrophic lateral sclerosis:implications for clinical practice and research[J]. Muscle Nerve, 2014, 49(6):786-803.

[21] Martinez FJ, Pratt GA, Van Nostrand EL, et al. Protein-RNA networks regulated by normal and ALS-associated mutant HNRNPA2B1 in the nervous system[J]. Neuron, 2016, 92(4):780-795.

[22] Kim HJ, Kim NC, Wang YD, et al. Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS[J]. Nature, 2013, 495(7442):467-473.

[23] Cox LE, Ferraiuolo L, Goodall EF, et al. Mutations in CHMP2B in lower motor neuron predominant amyotrophic lateral sclerosis (ALS)[J]. PLoS One, 2010, 5(3):e9872.

[24] Simpson CL, Lemmens R, Miskiewicz K, et al. Variants of the elongator protein 3(ELP3) gene are associated with motor neuron degeneration[J]. Hum Mol Genet, 2009, 18(3):472-481.

[25] Münch C, Sedlmeier R, Meyer T, et al. Point mutations of the p150 subunit of dynactin (DCTN1) gene in ALS[J]. Neurology, 2004, 63(4):724-726.

[26] Hirano M, Quinzii CM, Mitsumoto H, et al. Senataxin mutations and amyotrophic lateral sclerosis[J]. Amyotroph Lateral Scler, 2011, 12(3):223-227.

[27] 范昌发,岳秉飞,王军志. 转基因动物模型在ALS发病机制研究及药物疗效观察中的应用[J].实验动物科学, 2008, 25(4):45-48.

[28] McGoldrick P, Joyce PI, Fisher EM, et al. Rodent models of amyotrophic lateral sclerosis[J]. Biochim Biophys Acta, 2013, 1832(9):1421-1436.

[29] Lai C, Xie C, McCormack SG, et al. Amyotrophic lateral sclerosis 2-deficiency leads to neuronal degeneration in amyotrophic lateral sclerosis through altered AMPA receptor trafficking[J]. J Neurosci, 2006, 26(45):11798-11806.

[30] Moser JM, Bigini P, Schmitt-John T. The Wobbler mouse, an ALS animal model[J]. Mol Genet Genomics, 2013, 288(5-6):207-229.

[31] Mitchell JC, McGoldrick P, Vance C, et al. Overexpression of human wild-type FUS causes progressive motor neuron degeneration in an age- and dose-dependent fashion[J]. Acta Neuropathol, 2012, 125(2):273-288.

[32] Xu G, Ayers JI, Roberts BL, et al. Direct and indirect mechanisms for wild-type SOD1 to enhance the toxicity of mutant SOD1 in bigenic transgenic mice[J]. Hum Mol Genet, 2014, 24(4):1019-1035.

Get Citation

Copy

Article Metrics

Abstract:
PDF:
HTML:
Cited by:

History

Received:March 01,2017
Revised:
Adopted:
Online: October 23,2017
Published:

Home

About this journal

Editorial Board

Info for Author

Contact Us

中文版

Get Citation

Related Videos

Share

Article Metrics

History

Article QR Code