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Brief Reports

A novel mutation in the cleavage site N291 of TDP-43 protein in a familial case of amyotrophic lateral sclerosis

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Pages 463-466 | Received 22 Dec 2019, Accepted 30 Mar 2020, Published online: 17 Apr 2020

References

  • Guo L, Shorter J. Biology and pathobiology of TDP-43 and emergent therapeutic strategies. Cold Spring Harb Perspect Med. 2017;7:a024554.
  • Okamoto K, Hirai S, Shoji M, Senoh Y, Yamazaki T. Axonal swellings in the corticospinal tracts in amyotrophic lateral sclerosis. Acta Neuropathol. 1990;80:222–6.
  • Kwong LK, Neumann M, Sampathu DM, Lee VM-Y, Trojanowski JQ. TDP-43 proteinopathy: the neuropathology underlying major forms of sporadic and familial frontotemporal lobar degeneration and motor neuron disease. Acta Neuropathol. 2007;114:63–70.
  • Ling S-C, Polymenidou M, Cleveland Don W. Converging mechanisms in ALS and FTD: disrupted RNA and protein homeostasis. Neuron. 2013;79:416–38.
  • Brown RH Jr., Al-Chalabi A. Amyotrophic lateral sclerosis. N Engl J Med. 2017;377:162–72.
  • Kabashi E, Valdmanis PN, Dion P, Spiegelman D, McConkey BJ, Velde CV, et al. TARDBP mutations in individuals with sporadic and familial amyotrophic lateral sclerosis. Nat Genet. 2008;40:572–4.
  • Moreno F, Rabinovici GD, Karydas A, Miller Z, Hsu SC, Legati A, et al. A novel mutation P112H in the TARDBP gene associated with frontotemporal lobar degeneration without motor neuron disease and abundant neuritic amyloid plaques. Acta Neuropathol Commun. 2015;3:19.
  • Maurel C, Madji-Hounoum B, Thepault R-A, Marouillat S, Brulard C, Danel-Brunaud V, et al. Mutation in the RRM2 domain of TDP-43 in amyotrophic lateral sclerosis with rapid progression associated with ubiquitin positive aggregates in cultured motor neurons. Amyotroph Lateral Scler Frontotemporal Degener. 2018;19:149–51.
  • Zhang Y-J, Xu Y-F, Cook C, Gendron TF, Roettges P, Link CD, et al. Aberrant cleavage of TDP-43 enhances aggregation and cellular toxicity. Proc Natl Acad Sci USA. 2009;106:7607–12.
  • Herskowitz JH, Gozal YM, Duong DM, Dammer EB, Gearing M, Ye K, et al. Asparaginyl endopeptidase cleaves TDP-43 in brain. Proteomics. 2012;12:2455–63.
  • Kametani F, Obi T, Shishido T, Akatsu H, Murayama S, Saito Y, et al. Mass spectrometric analysis of accumulated TDP-43 in amyotrophic lateral sclerosis brains. Sci Rep. 2016;6:23281.
  • Zou Z-Y, Peng Y, Wang X-N, Liu M-S, Li X-G, Cui L-Y, et al. Screening of the TARDBP gene in familial and sporadic amyotrophic lateral sclerosis patients of Chinese origin. Neurobiol Aging. 2012;33:2229.e11–2229.e18.
  • Zhang YJ, Xu YF, Dickey CA, Buratti E, Baralle F, Bailey R, et al. Progranulin mediates caspase-dependent cleavage of TAR DNA binding protein-43. J Neurosci. 2007;27:10530–10534.
  • Suzuki H, Lee K, Matsuoka M. TDP-43-induced death is associated with altered regulation of BIM and Bcl-xL and attenuated by caspase-mediated TDP-43 cleavage. J Biol Chem. 2011;286:13171–83.
  • Zhang Z, Xie M, Ye K. Asparagine endopeptidase is an innovative therapeutic target for neurodegenerative diseases. Expert Opin Ther Targets. 2016;20:1237–45.
  • Nonaka T, Suzuki G, Tanaka Y, Kametani F, Hirai S, Okado H, et al. Phosphorylation of TAR DNA-binding protein of 43 kDa (TDP-43) by truncated casein kinase 1δ triggers mislocalization and accumulation of TDP-43. J Biol Chem. 2016;291:5473–83.
  • Xiong H-L, Wang J-Y, Sun Y-M, Wu J-J, Chen Y, Qiao K, et al. Association between novel TARDBP mutations and Chinese patients with amyotrophic lateral sclerosis. BMC Med Genet. 2010;11:8.

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