Acknowledgement
This work was supported by the National Research Foundation of Korea (NRF) grant funded by the Korea government (MSIT) (2020R1A2C3006875, 2020R1A2C3006734). This research was also supported by a grant of the Korea Health Technology R&D Project through the Korea Health Industry Development Institute (KHIDI), funded by the Ministry of Health & Welfare and MSIT, Republic of Korea (HU20C0345).
References
- Rowland LP and Shneider NA (2001) Amyotrophic lateral sclerosis. New Engl J Med 344, 1688-1700 https://doi.org/10.1056/NEJM200105313442207
- Chio A, Logroscino G, Hardiman O et al (2009) Prognostic factors in ALS: a critical review. Amyotroph Lateral Scler 10, 310-323 https://doi.org/10.3109/17482960802566824
- Hardiman O, Al-Chalabi A, Chio A et al (2017) Amyotrophic lateral sclerosis. Nat Rev Dis Primers 3, 17071
- Zou ZY, Zhou ZR, Che CH, Liu CY, He RL and Huang HP (2017) Genetic epidemiology of amyotrophic lateral sclerosis: a systematic review and meta-analysis. J Neurol Neurosurg Psychiatr 88, 540-549 https://doi.org/10.1136/jnnp-2016-315018
- Boylan K (2015) Familial ALS. Neurol Clin 33, 807-830 https://doi.org/10.1016/j.ncl.2015.07.001
- Mejzini R, Flynn LL, Pitout IL, Fletcher S, Wilton SD and Akkari PA (2019) ALS genetics, mechanisms, and therapeutics: where are we now? Front Neurosci 13, 1310
- Kim G, Gautier O, Tassoni-Tsuchida E, Ma XR and Gitler AD (2020) ALS genetics: gains, losses, and implications for future therapies. Neuron 108, 822-842 https://doi.org/10.1016/j.neuron.2020.08.022
- Vance C, Rogelj B, Hortobagyi T et al (2009) Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosis type 6. Science 323, 1208-1211 https://doi.org/10.1126/science.1165942
- Rosen DR, Siddique T, Patterson D et al (1993) Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature 362, 59
- Oakes JA, Davies MC and Collins MO (2017) TBK1: a new player in ALS linking autophagy and neuroinflammation. Mol Brain 10, 5
- Sreedharan J, Blair IP, Tripathi VB et al (2008) TDP-43 mutations in familial and sporadic amyotrophic lateral sclerosis. Science 319, 1668-1672 https://doi.org/10.1126/science.1154584
- Renton AE, Majounie E, Waite A et al (2011) A hexanucleotide repeat expansion in C9ORF72 is the cause of chromosome 9p21-linked ALS-FTD. Neuron 72, 257-268 https://doi.org/10.1016/j.neuron.2011.09.010
- Schissel SL, Schuchman EH, Williams KJ and Tabas I (1996) Zn2+-stimulatedZn2+-stimulated sphingomyelinase is secreted by many cell types and is a product of the acid sphingomyelinase gene. J Biol Chem 271, 18431-18436 https://doi.org/10.1074/jbc.271.31.18431
- Kornhuber J, Rhein C, Muller CP and Muhle C (2015) Secretory sphingomyelinase in health and disease. Biol Chem 396, 707-736
- Lee JK, Jin HK, Park MH et al (2014) Acid sphingomyelinase modulates the autophagic process by controlling lysosomal biogenesis in Alzheimer's disease. J Exp Med 211, 1551-1570 https://doi.org/10.1084/jem.20132451
- Ong WY, Herr DR, Farooqui T, Ling EA and Farooqui AA (2015) Role of sphingomyelinases in neurological disorders. Expert Opin Ther Targets 19, 1725-1742 https://doi.org/10.1517/14728222.2015.1071794
- Park MH, Jin HK and Bae JS (2020) Potential therapeutic target for aging and age-related neurodegenerative diseases: the role of acid sphingomyelinase. Exp Mol Med 52, 380-389 https://doi.org/10.1038/s12276-020-0399-8
- Jenkins RW, Canals D and Hannun YA (2009) Roles and regulation of secretory and lysosomal acid sphingomyelinase. Cell Signal 21, 836-846 https://doi.org/10.1016/j.cellsig.2009.01.026
- Xiang Li, Erich Gulbins and Yang Zhang (2012) Oxidative stress triggers Ca-dependent lysosome trafficking and activation of acid sphingomyelinase. Cell Physiol Biochem 30, 815-826
- Smith EL and Schuchman EH (2008) The unexpected role of acid sphingomyelinase in cell death and the pathophysiology of common diseases. FASEB J 22, 3419-3431 https://doi.org/10.1096/fj.08-108043
- Park MH, Lee JY, Park KH et al (2018) Vascular and neurogenic rejuvenation in aging mice by modulation of ASM. Neuron 100, 167-182 https://doi.org/10.1016/j.neuron.2018.09.010
- Qiu H, Lee S, Shang Y et al (2014) ALS-associated mutation FUS-R521C causes DNA damage and RNA splicing defects. J Clin Invest 124, 981-999 https://doi.org/10.1172/JCI72723
- Mitchell JC, McGoldrick P, Vance C et al (2013) Overexpression of human wild-type FUS causes progressive motor neuron degeneration in an age- and dose-dependent fashion. Acta Neuropathol 125, 273-288 https://doi.org/10.1007/s00401-012-1043-z
- Sharma A, Lyashchenko AK, Lu L et al (2016) ALS-associated mutant FUS induces selective motor neuron degeneration through toxic gain of function. Nat Commun 7, 10465
- Hewitt C, Kirby J, Highley JR et al (2010) Novel FUS/TLS mutations and pathology in familial and sporadic amyotrophic lateral sclerosis. Arch Neurol 67, 455-461 https://doi.org/10.1001/archneurol.2010.52
- Cutler RG, Pedersen WA, Camandola S, Rothstein JD and Mattson MP (2002) Evidence that accumulation of ceramides and cholesterol esters mediates oxidative stress-induced death of motor neurons in amyotrophic lateral sclerosis. Ann Neurol 52, 448-457 https://doi.org/10.1002/ana.10312
- Arenas A, Kuang L, Zhang J, Kingren MS and Zhu H (2021) FUS regulates autophagy by mediating the transcription of genes critical to the autophagosome formation. J Neurochem 157, 752-763 https://doi.org/10.1111/jnc.15281
- Baskoylu SN, Chapkis N, Unsal B et al (2022) Disrupted autophagy and neuronal dysfunction in C. elegans knockin models of FUS amyotrophic lateral sclerosis. Cell Rep 38, 110195
- Petrov D, Mansfield C, Moussy A and Hermine O (2017) ALS clinical trials review: 20 years of failure. Are we any closer to registering a new treatment? Front Aging Neurosci 9, 68
- Kornhuber J, Tripal P, Reichel M et al (2010) Functional Inhibitors of Acid Sphingomyelinase (FIASMAs): a novel pharmacological group of drugs with broad clinical applications. Cell Physiol Biochem 26, 9-20 https://doi.org/10.1159/000315101
- Park MH, Park KH, Choi BJ et al (2022) Discovery of a dual-action small molecule that improves neuropathological features of Alzheimer's disease mice. Proc Natl Acad Sci U S A 119, e2115082119
- Horinouchi K, Erlich S, Perl DP et al (1995) Acid sphingomyelinase deficient mice: a model of types A and B Niemann-Pick disease. Nat Genet 10, 288-293 https://doi.org/10.1038/ng0795-288
- Shiihashi G, Ito D, Yagi T, Nihei Y, Ebine T and Suzuki N (2016) Mislocated FUS is sufficient for gain-of-toxic-function amyotrophic lateral sclerosis phenotypes in mice. Brain 139, 2380-2394 https://doi.org/10.1093/brain/aww161