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Cited by 71Amyotrophic Lateral Sclerosis ResearchNeuroinflammation and Neurodegeneration MechanismsAlzheimer's disease research and treatments

TDP-43 and Inflammation: Implications for Amyotrophic Lateral Sclerosis and Frontotemporal Dementia

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Bright, Fiona, Chan, Gabriella, van Hummel, Annika, Ittner, Lars M., Ke, Yazi D.·2021·International Journal of Molecular Sciences
DOI 10.3390/ijms22157781PMC PMC8346169
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Abstract

The abnormal mislocalisation and ubiquitinated protein aggregation of the TAR DNA binding protein 43 (TDP-43) within the cytoplasm of neurons and glia in the central nervous system (CNS) is a pathological hallmark of early-onset neurodegenerative disorders amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD). The pathomechanisms underlying abnormal mislocalisation and aggregation of TDP-43 remain unknown. However, there is a growing body of evidence implicating neuroinflammation and immune-mediated mechanisms in the pathogenesis of neurodegeneration. Importantly, most of the evidence for an active role of immunity and inflammation in the pathogenesis of ALS and FTD relates specifically to TDP-43, posing the question as to whether immune-mediated mechanisms could hold the key to understanding TDP-43’s underlying role in neurodegeneration in both diseases. Therefore, this review aims to piece together key lines of evidence for the specific association of TDP-43 with key immune and inflammatory pathways to explore the nature of this relationship and the implications for potential pathomechanisms underlying neurodegeneration in ALS and FTD.

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  • Protein aggregates released into extracellular space together with DAMPs from damaged neurons induce microglia activation and proinflammatory cytokine releasing.

    “Protein aggregates released into the extracellular space together with DAMPs released from damaged neurons induce microglia activation and proinflammatory cytokines releasing.20,83,84”

    From Role of neuroinflammation in neurodegeneration development (2023) · cites this paper as [20]

    Section 6.3 says DAMPs signal and activate microglia, and that TDP-43 inclusions activate a microglial inflammatory pathway that increases IL-1β production. Section 6.1 also reports microglial activation and proinflammatory cytokine production in response to TDP-43. These passages do not establish the claim’s more specific account that protein aggregates and DAMPs are released from damaged neurons into extracellular space and act together. (LLM, conf=0.86)

    Experimental — accuracy not yet measured

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  1. [1]Wyss-Coray T. Mucke L. Inflammation in neurodegenerative disease—A double-edged sword Neuron 2002 35 419 432 10.1016/S0896-6273(02)00794-8 12165466 · DOI · Paper page
  2. [2]Sochocka M. Diniz B.S. Leszek J. Inflammatory Response in the CNS: Friend or Foe? Mol. Neurobiol. 2017 54 8071 8089 10.1007/s12035-016-0297-1 27889895 PMC5684251 · DOI · Paper page
  3. [3]Zuo L. Prather E.R. Stetskiv M. Garrison D.E. Meade J.R. Peace T.I. Zhou T. Inflammaging and Oxidative Stress in Human Diseases: From Molecular Mechanisms to Novel Treatments Int. J. Mol. Sci. 2019 20 4472 10.3390/ijms20184472 31510091 PMC6769561 · DOI
  4. [5]Heneka M.T. Golenbock D.T. Latz E. Innate immunity in Alzheimer’s disease Nat. Immunol. 2015 16 229 236 10.1038/ni.3102 25689443 · DOI · Paper page
  5. [6]McCauley M.E. Baloh R.H. Inflammation in ALS/FTD pathogenesis Acta. Neuropathol. 2019 137 715 730 10.1007/s00401-018-1933-9 30465257 PMC6482122 · DOI · Paper page
  6. [7]Bright F. Werry E.L. Dobson-Stone C. Piguet O. Ittner L.M. Halliday G.M. Hodges J.R. Kiernan M.C. Loy C.T. Kassiou M. Neuroinflammation in frontotemporal dementia Nat. Rev. Neurol. 2019 15 540 555 10.1038/s41582-019-0231-z 31324897 · DOI · Paper page
  7. [8]Calabrese V. Santoro A. Monti D. Crupi R. Di Paola R. Latteri S. Cuzzocrea S. Zappia M. Giordano J. Calabrese E.J. Aging and Parkinson’s Disease: Inflammaging, neuroinflammation and biological remodeling as key factors in pathogenesis Free Radic Biol. Med. 2018 115 80 91 10.1016/j.freeradbiomed.2017.10.379 29080843 · DOI · Paper page
  8. [9]Ou S.H. Wu F. Harrich D. Garcia-Martinez L.F. Gaynor R.B. Cloning and characterization of a novel cellular protein, TDP-43, that binds to human immunodeficiency virus type 1 TAR DNA sequence motifs J. Virol. 1995 69 3584 3596 10.1128/jvi.69.6.3584-3596.1995 7745706 PMC189073 · DOI
  9. [10]Wang A. Conicella A.E. Schmidt H.B. Martin E.W. Rhoads S.N. Reeb A.N. Nourse A. Ramirez Montero D. Ryan V.H. Rohatgi R. A single N-terminal phosphomimic disrupts TDP-43 polymerization, phase separation, and RNA splicing EMBO J. 2018 37 e97452 10.15252/embj.201797452 29438978 PMC5830921 · DOI
  10. [11]Mompean M. Romano V. Pantoja-Uceda D. Stuani C. Baralle F.E. Buratti E. Laurents D.V. Point mutations in the N-terminal domain of transactive response DNA-binding protein 43 kDa (TDP-43) compromise its stability, dimerization, and functions J. Biol. Chem. 2017 292 11992 12006 10.1074/jbc.M117.775965 28566288 PMC5512090 · DOI
  11. [12]Buratti E. Baralle F.E. Multiple roles of TDP-43 in gene expression, splicing regulation, and human disease Front. Biosci. 2008 13 867 878 10.2741/2727 17981595 · DOI
  12. [13]Buratti E. Baralle F.E. TDP-43: Gumming up neurons through protein-protein and protein-RNA interactions Trends Biochem. Sci. 2012 37 237 247 10.1016/j.tibs.2012.03.003 22534659 · DOI
  13. [14]Mercado P.A. Ayala Y.M. Romano M. Buratti E. Baralle F.E. Depletion of TDP 43 overrides the need for exonic and intronic splicing enhancers in the human apoA-II gene Nucleic Acids Res. 2005 33 6000 6010 10.1093/nar/gki897 16254078 PMC1270946 · DOI
  14. [15]Hefferon T.W. Groman J.D. Yurk C.E. Cutting G.R. A variable dinucleotide repeat in the CFTR gene contributes to phenotype diversity by forming RNA secondary structures that alter splicing Proc. Natl. Acad. Sci. USA 2004 101 3504 3509 10.1073/pnas.0400182101 14993601 PMC373492 · DOI
  15. [16]Ederle H. Funk C. Abou-Ajram C. Hutten S. Funk E.B.E. Kehlenbach R.H. Bailer S.M. Dormann D. Nuclear egress of TDP-43 and FUS occurs independently of Exportin-1/CRM1 Sci. Rep. 2018 8 7084 10.1038/s41598-018-25007-5 29728564 PMC5935713 · DOI
  16. [17]Pinarbasi E.S. Cagatay T. Fung H.Y.J. Li Y.C. Chook Y.M. Thomas P.J. Active nuclear import and passive nuclear export are the primary determinants of TDP-43 localization Sci. Rep. 2018 8 7083 10.1038/s41598-018-25008-4 29728608 PMC5935693 · DOI
  17. [18]Archbold H.C. Jackson K.L. Arora A. Weskamp K. Tank E.M. Li X. Miguez R. Dayton R.D. Tamir S. Klein R.L. TDP43 nuclear export and neurodegeneration in models of amyotrophic lateral sclerosis and frontotemporal dementia Sci. Rep. 2018 8 4606 10.1038/s41598-018-22858-w 29545601 PMC5854632 · DOI
  18. [20]Chu J.F. Majumder P. Chatterjee B. Huang S.L. Shen C.J. TDP-43 Regulates Coupled Dendritic mRNA Transport-Translation Processes in Co-operation with FMRP and Staufen1 Cell Rep. 2019 29 3118 3133 10.1016/j.celrep.2019.10.061 31801077 · DOI
  19. [21]Ayala Y.M. De Conti L. Avendano-Vazquez S.E. Dhir A. Romano M. D’Ambrogio A. Tollervey J. Ule J. Baralle M. Buratti E. TDP-43 regulates its mRNA levels through a negative feedback loop EMBO J. 2011 30 277 288 10.1038/emboj.2010.310 21131904 PMC3025456 · DOI
  20. [22]Johnson B.S. McCaffery J.M. Lindquist S. Gitler A.D. A yeast TDP-43 proteinopathy model: Exploring the molecular determinants of TDP-43 aggregation and cellular toxicity Proc. Natl. Acad. Sci. USA 2008 105 6439 6444 10.1073/pnas.0802082105 18434538 PMC2359814 · DOI
  21. [24]Voigt A. Herholz D. Fiesel F.C. Kaur K. Muller D. Karsten P. Weber S.S. Kahle P.J. Marquardt T. Schulz J.B. TDP-43-mediated neuron loss in vivo requires RNA-binding activity PLoS ONE 2010 5 e12247 10.1371/journal.pone.0012247 20806063 PMC2923622 · DOI
  22. [25]Leibiger C. Deisel J. Aufschnaiter A. Ambros S. Tereshchenko M. Verheijen B.M. Buttner S. Braun R.J. TDP-43 controls lysosomal pathways thereby determining its own clearance and cytotoxicity Hum. Mol. Genet. 2018 27 1593 1607 10.1093/hmg/ddy066 29474575 · DOI · Paper page
  23. [26]Chang C.K. Chiang M.H. Toh E.K. Chang C.F. Huang T.H. Molecular mechanism of oxidation-induced TDP-43 RRM1 aggregation and loss of function FEBS Lett. 2013 587 575 582 10.1016/j.febslet.2013.01.038 23384725 · DOI
  24. [27]Shodai A. Morimura T. Ido A. Uchida T. Ayaki T. Takahashi R. Kitazawa S. Suzuki S. Shirouzu M. Kigawa T. Aberrant assembly of RNA recognition motif 1 links to pathogenic conversion of TAR DNA-binding protein of 43 kDa (TDP-43) J. Biol. Chem. 2013 288 14886 14905 10.1074/jbc.M113.451849 23558684 PMC3663511 · DOI
  25. [28]Garnier C. Devred F. Byrne D. Puppo R. Roman A.Y. Malesinski S. Golovin A.V. Lebrun R. Ninkina N.N. Tsvetkov P.O. Zinc binding to RNA recognition motif of TDP-43 induces the formation of amyloid-like aggregates Sci. Rep. 2017 7 6812 10.1038/s41598-017-07215-7 28754988 PMC5533730 · DOI
  26. [29]Zacco E. Grana-Montes R. Martin S.R. de Groot N.S. Alfano C. Tartaglia G.G. Pastore A. RNA as a key factor in driving or preventing self-assembly of the TAR DNA-binding protein 43 J. Mol. Biol. 2019 431 1671 1688 10.1016/j.jmb.2019.01.028 30742796 PMC6461199 · DOI
  27. [30]Buratti E. TDP-43 post-translational modifications in health and disease Expert Opin. Ther. Targets 2018 22 279 293 10.1080/14728222.2018.1439923 29431050 · DOI
  28. [31]Francois-Moutal L. Perez-Miller S. Scott D.D. Miranda V.G. Mollasalehi N. Khanna M. Structural Insights Into TDP-43 and Effects of Post-translational Modifications Front. Mol. Neurosci. 2019 12 301 10.3389/fnmol.2019.00301 31920533 PMC6934062 · DOI
  29. [32]Zhang Y.J. Xu Y.F. Cook C. Gendron T.F. Roettges P. Link C.D. Lin W.L. Tong J. Castanedes-Casey M. Ash P. Aberrant cleavage of TDP-43 enhances aggregation and cellular toxicity Proc. Natl. Acad. Sci. USA 2009 106 7607 7612 10.1073/pnas.0900688106 19383787 PMC2671323 · DOI
  30. [33]Berning B.A. Walker A.K. The Pathobiology of TDP-43 C-Terminal Fragments in ALS and FTLD Front. Neurosci. 2019 13 335 10.3389/fnins.2019.00335 31031584 PMC6470282 · DOI
  31. [34]Neumann M. Sampathu D.M. Kwong L.K. Truax A.C. Micsenyi M.C. Chou T.T. Bruce J. Schuck T. Grossman M. Clark C.M. Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis Science 2006 314 130 133 10.1126/science.1134108 17023659 · DOI · Paper page
  32. [35]Arai T. Hasegawa M. Akiyama H. Ikeda K. Nonaka T. Mori H. Mann D. Tsuchiya K. Yoshida M. Hashizume Y. TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis Biochem. Biophys Res. Commun. 2006 351 602 611 10.1016/j.bbrc.2006.10.093 17084815 · DOI · Paper page
  33. [36]Tan R.H. Kril J.J. Fatima M. McGeachie A. McCann H. Shepherd C. Forrest S.L. Affleck A. Kwok J.B. Hodges J.R. TDP-43 proteinopathies: Pathological identification of brain regions differentiating clinical phenotypes Brain 2015 138 3110 3122 10.1093/brain/awv220 26231953 · DOI
  34. [37]Steinacker P. Hendrich C. Sperfeld A.D. Jesse S. von Arnim C.A. Lehnert S. Pabst A. Uttner I. Tumani H. Lee V.M. TDP-43 in cerebrospinal fluid of patients with frontotemporal lobar degeneration and amyotrophic lateral sclerosis Arch. Neurol. 2008 65 1481 1487 10.1001/archneur.65.11.1481 19001167 PMC2690860 · DOI · Paper page
  35. [39]Kasai T. Tokuda T. Ishigami N. Sasayama H. Foulds P. Mitchell D.J. Mann D.M. Allsop D. Nakagawa M. Increased TDP-43 protein in cerebrospinal fluid of patients with amyotrophic lateral sclerosis Acta. Neuropathol. 2009 117 55 62 10.1007/s00401-008-0456-1 18989684 · DOI · Paper page
  36. [40]Rohn T.T. Caspase-cleaved TAR DNA-binding protein-43 is a major pathological finding in Alzheimer’s disease Brain Res. 2008 1228 189 198 10.1016/j.brainres.2008.06.094 18634762 PMC2565865 · DOI
  37. [41]Nakashima-Yasuda H. Uryu K. Robinson J. Xie S.X. Hurtig H. Duda J.E. Arnold S.E. Siderowf A. Grossman M. Leverenz J.B. Co-morbidity of TDP-43 proteinopathy in Lewy body related diseases Acta. Neuropathol. 2007 114 221 229 10.1007/s00401-007-0261-2 17653732 · DOI · Paper page
  38. [42]Schwab C. Arai T. Hasegawa M. Yu S. McGeer P.L. Colocalization of transactivation-responsive DNA-binding protein 43 and huntingtin in inclusions of Huntington disease J. Neuropathol. Exp. Neurol. 2008 67 1159 1165 10.1097/NEN.0b013e31818e8951 19018245 · DOI
  39. [44]Walker A.K. Daniels C.M. Goldman J.E. Trojanowski J.Q. Lee V.M. Messing A. Astrocytic TDP-43 pathology in Alexander disease J. Neurosci. 2014 34 6448 6458 10.1523/JNEUROSCI.0248-14.2014 24806671 PMC4012304 · DOI
  40. [45]Liu E.A. Mori E. Hamasaki F. Lieberman A.P. TDP-43 proteinopathy occurs independently of autophagic substrate accumulation and underlies nuclear defects in Niemann-Pick C disease Neuropathol. Appl. Neurobiol. 2021 10.1111/nan.12738 PMC8608685 34048071 · DOI
  41. [46]Pottier C. Ren Y. Perkerson R.B. 3rd Baker M. Jenkins G.D. van Blitterswijk M. DeJesus-Hernandez M. van Rooij J.G.J. Murray M.E. Christopher E. Genome-wide analyses as part of the international FTLD-TDP whole-genome sequencing consortium reveals novel disease risk factors and increases support for immune dysfunction in FTLD Acta Neuropathol. 2019 137 879 899 10.1007/s00401-019-01962-9 30739198 PMC6533145 · DOI
  42. [47]Broce I. Karch C.M. Wen N. Fan C.C. Wang Y. Tan C.H. Kouri N. Ross O.A. Hoglinger G.U. Muller U. Immune-related genetic enrichment in frontotemporal dementia: An analysis of genome-wide association studies PLoS Med. 2018 15 e1002487 10.1371/journal.pmed.1002487 29315334 PMC5760014 · DOI
  43. [48]Wils H. Kleinberger G. Janssens J. Pereson S. Joris G. Cuijt I. Smits V. Ceuterick-de Groote C. Van Broeckhoven C. Kumar-Singh S. TDP-43 transgenic mice develop spastic paralysis and neuronal inclusions characteristic of ALS and frontotemporal lobar degeneration Proc. Natl. Acad. Sci. USA 2010 107 3858 3863 10.1073/pnas.0912417107 20133711 PMC2840518 · DOI
  44. [49]Paolicelli R.C. Jawaid A. Henstridge C.M. Valeri A. Merlini M. Robinson J.L. Lee E.B. Rose J. Appel S. Lee V.M. TDP-43 Depletion in Microglia Promotes Amyloid Clearance but Also Induces Synapse Loss Neuron 2017 95 297 308 10.1016/j.neuron.2017.05.037 28669544 PMC5519492 · DOI · Paper page
  45. [50]Sudria-Lopez E. Koppers M. de Wit M. van der Meer C. Westeneng H.J. Zundel C.A. Youssef S.A. Harkema L. de Bruin A. Veldink J.H. Full ablation of C9orf72 in mice causes immune system-related pathology and neoplastic events but no motor neuron defects Acta. Neuropathol. 2016 132 145 147 10.1007/s00401-016-1581-x 27206760 PMC4911370 · DOI · Paper page
  46. [51]Burberry A. Suzuki N. Wang J.Y. Moccia R. Mordes D.A. Stewart M.H. Suzuki-Uematsu S. Ghosh S. Singh A. Merkle F.T. Loss-of-function mutations in the C9ORF72 mouse ortholog cause fatal autoimmune disease Sci. Transl. Med. 2016 8 347ra393 10.1126/scitranslmed.aaf6038 PMC5024536 27412785 · DOI · Paper page
  47. [52]Atanasio A. Decman V. White D. Ramos M. Ikiz B. Lee H.C. Siao C.J. Brydges S. LaRosa E. Bai Y. C9orf72 ablation causes immune dysregulation characterized by leukocyte expansion, autoantibody production, and glomerulonephropathy in mice Sci. Rep. 2016 6 23204 10.1038/srep23204 26979938 PMC4793236 · DOI · Paper page
  48. [53]Thurner L. Preuss K.D. Fadle N. Regitz E. Klemm P. Zaks M. Kemele M. Hasenfus A. Csernok E. Gross W.L. Progranulin antibodies in autoimmune diseases J. Autoimmun. 2013 42 29 38 10.1016/j.jaut.2012.10.003 23149338 · DOI
  49. [54]Thurner L. Fadle N. Regitz E. Kemele M. Klemm P. Zaks M. Stoger E. Bette B. Carbon G. Zimmer V. The molecular basis for development of proinflammatory autoantibodies to progranulin J. Autoimmun. 2015 61 17 28 10.1016/j.jaut.2015.05.002 26005049 · DOI
  50. [55]Ahmad L. Zhang S.Y. Casanova J.L. Sancho-Shimizu V. Human TBK1: A Gatekeeper of Neuroinflammation Trends Mol. Med. 2016 22 511 527 10.1016/j.molmed.2016.04.006 27211305 PMC4890605 · DOI · Paper page
  51. [56]Fitzgerald K.A. McWhirter S.M. Faia K.L. Rowe D.C. Latz E. Golenbock D.T. Coyle A.J. Liao S.M. Maniatis T. IKKepsilon and TBK1 are essential components of the IRF3 signaling pathway Nat. Immunol. 2003 4 491 496 10.1038/ni921 12692549 · DOI
  52. [57]Picher-Martel V. Dutta K. Phaneuf D. Sobue G. Julien J.P. Ubiquilin-2 drives NF-kappaB activity and cytosolic TDP-43 aggregation in neuronal cells Mol. Brain 2015 8 71 10.1186/s13041-015-0162-6 26521126 PMC4628361 · DOI · Paper page
  53. [58]Hjerpe R. Bett J.S. Keuss M.J. Solovyova A. McWilliams T.G. Johnson C. Sahu I. Varghese J. Wood N. Wightman M. UBQLN2 Mediates Autophagy-Independent Protein Aggregate Clearance by the Proteasome Cell 2016 166 935 949 10.1016/j.cell.2016.07.001 27477512 PMC5003816 · DOI
  54. [59]Dao T.P. Kolaitis R.M. Kim H.J. O’Donovan K. Martyniak B. Colicino E. Hehnly H. Taylor J.P. Castaneda C.A. Ubiquitin Modulates Liquid-Liquid Phase Separation of UBQLN2 via Disruption of Multivalent Interactions Mol. Cell 2018 69 965 978 10.1016/j.molcel.2018.02.004 29526694 PMC6181577 · DOI
  55. [60]Watanabe R. Higashi S. Nonaka T. Kawakami I. Oshima K. Niizato K. Akiyama H. Yoshida M. Hasegawa M. Arai T. Intracellular dynamics of Ataxin-2 in the human brains with normal and frontotemporal lobar degeneration with TDP-43 inclusions Acta. Neuropathol. Commun. 2020 8 176 10.1186/s40478-020-01055-9 33115537 PMC7594343 · DOI
  56. [61]Scoles D.R. Dansithong W. Pflieger L.T. Paul S. Gandelman M. Figueroa K.P. Rigo F. Bennett C.F. Pulst S.M. ALS-associated genes in SCA2 mouse spinal cord transcriptomes Hum. Mol. Genet. 2020 29 1658 1672 10.1093/hmg/ddaa072 32307524 PMC7322574 · DOI
  57. [62]Sieber M.W. Jaenisch N. Brehm M. Guenther M. Linnartz-Gerlach B. Neumann H. Witte O.W. Frahm C. Attenuated inflammatory response in triggering receptor expressed on myeloid cells 2 (TREM2) knock-out mice following stroke PLoS ONE 2013 8 e52982 10.1371/journal.pone.0052982 23301011 PMC3536811 · DOI
  58. [63]Kawabori M. Kacimi R. Kauppinen T. Calosing C. Kim J.Y. Hsieh C.L. Nakamura M.C. Yenari M.A. Triggering receptor expressed on myeloid cells 2 (TREM2) deficiency attenuates phagocytic activities of microglia and exacerbates ischemic damage in experimental stroke J. Neurosci. 2015 35 3384 3396 10.1523/JNEUROSCI.2620-14.2015 25716838 PMC4339351 · DOI · Paper page
  59. [64]Saber M. Kokiko-Cochran O. Puntambekar S.S. Lathia J.D. Lamb B.T. Triggering Receptor Expressed on Myeloid Cells 2 Deficiency Alters Acute Macrophage Distribution and Improves Recovery after Traumatic Brain Injury J. Neurotrauma 2017 34 423 435 10.1089/neu.2016.4401 26976047 · DOI
  60. [65]Yu L. De Jager P.L. Yang J. Trojanowski J.Q. Bennett D.A. Schneider J.A. The TMEM106B locus and TDP-43 pathology in older persons without FTLD Neurology 2015 84 927 934 10.1212/WNL.0000000000001313 25653292 PMC4351662 · DOI
  61. [66]Rhinn H. Abeliovich A. Differential Aging Analysis in Human Cerebral Cortex Identifies Variants in TMEM106B and GRN that Regulate Aging Phenotypes Cell Syst. 2017 4 404 415 10.1016/j.cels.2017.02.009 28330615 · DOI · Paper page
  62. [67]Osawa T. Mizuno Y. Fujita Y. Takatama M. Nakazato Y. Okamoto K. Optineurin in neurodegenerative diseases Neuropathology 2011 31 569 574 10.1111/j.1440-1789.2011.01199.x 21284751 · DOI
  63. [68]Slowicka K. van Loo G. Optineurin Functions for Optimal Immunity Front. Immunol. 2018 9 769 10.3389/fimmu.2018.00769 29692786 PMC5902560 · DOI
  64. [69]Meena N.P. Zhu G. Mittelstadt P.R. Giardino Torchia M.L. Pourcelot M. Arnoult D. Ashwell J.D. Munitic I. The TBK1-binding domain of optineurin promotes type I interferon responses FEBS Lett. 2016 590 1498 1508 10.1002/1873-3468.12176 27086836 PMC4879041 · DOI
  65. [70]Chew T.S. O’Shea N.R. Sewell G.W. Oehlers S.H. Mulvey C.M. Crosier P.S. Godovac-Zimmermann J. Bloom S.L. Smith A.M. Segal A.W. Optineurin deficiency in mice contributes to impaired cytokine secretion and neutrophil recruitment in bacteria-driven colitis Dis. Model. Mech. 2015 8 817 829 10.1242/dmm.020362 26044960 PMC4527293 · DOI
  66. [71]Gal J. Strom A.L. Kwinter D.M. Kilty R. Zhang J. Shi P. Fu W. Wooten M.W. Zhu H. Sequestosome 1/p62 links familial ALS mutant SOD1 to LC3 via an ubiquitin-independent mechanism J. Neurochem. 2009 111 1062 1073 10.1111/j.1471-4159.2009.06388.x 19765191 PMC2766427 · DOI · Paper page
  67. [72]Sanz L. Sanchez P. Lallena M.J. Diaz-Meco M.T. Moscat J. The interaction of p62 with RIP links the atypical PKCs to NF-kappaB activation EMBO J. 1999 18 3044 3053 10.1093/emboj/18.11.3044 10356400 PMC1171386 · DOI
  68. [73]Kratz M. Coats B.R. Hisert K.B. Hagman D. Mutskov V. Peris E. Schoenfelt K.Q. Kuzma J.N. Larson I. Billing P.S. Metabolic dysfunction drives a mechanistically distinct proinflammatory phenotype in adipose tissue macrophages Cell Metab. 2014 20 614 625 10.1016/j.cmet.2014.08.010 25242226 PMC4192131 · DOI
  69. [74]Gitcho M.A. Strider J. Carter D. Taylor-Reinwald L. Forman M.S. Goate A.M. Cairns N.J. VCP mutations causing frontotemporal lobar degeneration disrupt localization of TDP-43 and induce cell death J. Biol. Chem. 2009 284 12384 12398 10.1074/jbc.M900992200 19237541 PMC2673306 · DOI
  70. [75]Dec E. Rana P. Katheria V. Dec R. Khare M. Nalbandian A. Leu S.Y. Radom-Aizik S. Llewellyn K. BenMohamed L. Cytokine profiling in patients with VCP-associated disease Clin. Transl. Sci. 2014 7 29 32 10.1111/cts.12117 24119107 PMC4057603 · DOI
  71. [76]Nalbandian A. Khan A.A. Srivastava R. Llewellyn K.J. Tan B. Shukr N. Fazli Y. Kimonis V.E. BenMohamed L. Activation of the NLRP3 Inflammasome Is Associated with Valosin-Containing Protein Myopathy Inflammation 2017 40 21 41 10.1007/s10753-016-0449-5 27730320 PMC5800525 · DOI
  72. [77]Dobson-Stone C. Hallupp M. Shahheydari H. Ragagnin A.M.G. Chatterton Z. Carew-Jones F. Shepherd C.E. Stefen H. Paric E. Fath T. CYLD is a causative gene for frontotemporal dementia-amyotrophic lateral sclerosis Brain 2020 143 783 799 10.1093/brain/awaa039 32185393 PMC7089666 · DOI
  73. [78]Zhang M. Lee A.J. Wu X. Sun S.C. Regulation of antiviral innate immunity by deubiquitinase CYLD Cell. Mol. Immunol. 2011 8 502 504 10.1038/cmi.2011.42 21946435 PMC3210422 · DOI
  74. [79]Kovalenko A. Chable-Bessia C. Cantarella G. Israel A. Wallach D. Courtois G. The tumour suppressor CYLD negatively regulates NF-kappaB signalling by deubiquitination Nature 2003 424 801 805 10.1038/nature01802 12917691 · DOI
  75. [80]DeJesus-Hernandez M. Mackenzie I.R. Boeve B.F. Boxer A.L. Baker M. Rutherford N.J. Nicholson A.M. Finch N.A. Flynn H. Adamson J. Expanded GGGGCC hexanucleotide repeat in noncoding region of C9ORF72 causes chromosome 9p-linked FTD and ALS Neuron 2011 72 245 256 10.1016/j.neuron.2011.09.011 21944778 PMC3202986 · DOI · Paper page
  76. [83]Fredi M. Cavazzana I. Biasiotto G. Filosto M. Padovani A. Monti E. Tincani A. Franceschini F. Zanella I. C9orf72 Intermediate Alleles in Patients with Amyotrophic Lateral Sclerosis, Systemic Lupus Erythematosus, and Rheumatoid Arthritis Neuromol. Med. 2019 21 150 159 10.1007/s12017-019-08528-8 30859373 · DOI
  77. [84]Zhang Y. Burberry A. Wang J.Y. Sandoe J. Ghosh S. Udeshi N.D. Svinkina T. Mordes D.A. Mok J. Charlton M. The C9orf72-interacting protein Smcr8 is a negative regulator of autoimmunity and lysosomal exocytosis Genes. Dev. 2018 32 929 943 10.1101/gad.313932.118 29950492 PMC6075033 · DOI
  78. [85]O’Rourke J.G. Bogdanik L. Yanez A. Lall D. Wolf A.J. Muhammad A.K. Ho R. Carmona S. Vit J.P. Zarrow J. C9orf72 is required for proper macrophage and microglial function in mice Science 2016 351 1324 1329 10.1126/science.aaf1064 26989253 PMC5120541 · DOI · Paper page
  79. [87]Rostalski H. Leskela S. Huber N. Katisko K. Cajanus A. Solje E. Marttinen M. Natunen T. Remes A.M. Hiltunen M. Astrocytes and Microglia as Potential Contributors to the Pathogenesis of C9orf72 Repeat Expansion-Associated FTLD and ALS Front. Neurosci. 2019 13 486 10.3389/fnins.2019.00486 31156371 PMC6529740 · DOI
  80. [88]Mackenzie I.R. Baker M. Pickering-Brown S. Hsiung G.Y. Lindholm C. Dwosh E. Gass J. Cannon A. Rademakers R. Hutton M. The neuropathology of frontotemporal lobar degeneration caused by mutations in the progranulin gene Brain 2006 129 3081 3090 10.1093/brain/awl271 17071926 · DOI
  81. [90]Mukherjee O. Pastor P. Cairns N.J. Chakraverty S. Kauwe J.S. Shears S. Behrens M.I. Budde J. Hinrichs A.L. Norton J. HDDD2 is a familial frontotemporal lobar degeneration with ubiquitin-positive, tau-negative inclusions caused by a missense mutation in the signal peptide of progranulin Ann. Neurol. 2006 60 314 322 10.1002/ana.20963 16983685 PMC2803024 · DOI
  82. [92]Townley R.A. Boeve B.F. Benarroch E.E. Progranulin: Functions and neurologic correlations Neurology 2018 90 118 125 10.1212/WNL.0000000000004840 29263224 PMC5772162 · DOI
  83. [93]Cruts M. Gijselinck I. van der Zee J. Engelborghs S. Wils H. Pirici D. Rademakers R. Vandenberghe R. Dermaut B. Martin J.J. Null mutations in progranulin cause ubiquitin-positive frontotemporal dementia linked to chromosome 17q21 Nature 2006 442 920 924 10.1038/nature05017 16862115 · DOI · Paper page
  84. [94]Milanesi E. Bonvicini C. Alberici A. Pilotto A. Cattane N. Premi E. Gazzina S. Archetti S. Gasparotti R. Cancelli V. Molecular signature of disease onset in granulin mutation carriers: A gene expression analysis study Neurobiol. Aging 2013 34 1837 1845 10.1016/j.neurobiolaging.2012.11.016 23419701 · DOI
  85. [95]Tanaka Y. Matsuwaki T. Yamanouchi K. Nishihara M. Increased lysosomal biogenesis in activated microglia and exacerbated neuronal damage after traumatic brain injury in progranulin-deficient mice Neuroscience 2013 250 8 19 10.1016/j.neuroscience.2013.06.049 23830905 · DOI
  86. [96]Martens L.H. Zhang J. Barmada S.J. Zhou P. Kamiya S. Sun B. Min S.W. Gan L. Finkbeiner S. Huang E.J. Progranulin deficiency promotes neuroinflammation and neuron loss following toxin-induced injury J. Clin. Investig. 2012 122 3955 3959 10.1172/JCI63113 23041626 PMC3484443 · DOI
  87. [97]Yin F. Banerjee R. Thomas B. Zhou P. Qian L. Jia T. Ma X. Ma Y. Iadecola C. Beal M.F. Exaggerated inflammation, impaired host defense, and neuropathology in progranulin-deficient mice J. Exp. Med. 2010 207 117 128 10.1084/jem.20091568 20026663 PMC2812536 · DOI · Paper page
  88. [98]Huang M. Modeste E. Dammer E. Merino P. Taylor G. Duong D.M. Deng Q. Holler C.J. Gearing M. Dickson D. Network analysis of the progranulin-deficient mouse brain proteome reveals pathogenic mechanisms shared in human frontotemporal dementia caused by GRN mutations Acta. Neuropathol. Commun. 2020 8 163 10.1186/s40478-020-01037-x 33028409 PMC7541308 · DOI
  89. [101]Cirulli E.T. Lasseigne B.N. Petrovski S. Sapp P.C. Dion P.A. Leblond C.S. Couthouis J. Lu Y.F. Wang Q. Krueger B.J. Exome sequencing in amyotrophic lateral sclerosis identifies risk genes and pathways Science 2015 347 1436 1441 10.1126/science.aaa3650 25700176 PMC4437632 · DOI · Paper page
  90. [103]van der Zee J. Gijselinck I. Van Mossevelde S. Perrone F. Dillen L. Heeman B. Baumer V. Engelborghs S. De Bleecker J. Baets J. TBK1 Mutation Spectrum in an Extended European Patient Cohort with Frontotemporal Dementia and Amyotrophic Lateral Sclerosis Hum. Mutat. 2017 38 297 309 10.1002/humu.23161 28008748 PMC5324646 · DOI
  91. [104]Wild P. Farhan H. McEwan D.G. Wagner S. Rogov V.V. Brady N.R. Richter B. Korac J. Waidmann O. Choudhary C. Phosphorylation of the autophagy receptor optineurin restricts Salmonella growth Science 2011 333 228 233 10.1126/science.1205405 21617041 PMC3714538 · DOI · Paper page
  92. [105]Pilli M. Arko-Mensah J. Ponpuak M. Roberts E. Master S. Mandell M.A. Dupont N. Ornatowski W. Jiang S. Bradfute S.B. TBK-1 promotes autophagy-mediated antimicrobial defense by controlling autophagosome maturation Immunity 2012 37 223 234 10.1016/j.immuni.2012.04.015 22921120 PMC3428731 · DOI · Paper page
  93. [106]Salminen A. Huuskonen J. Ojala J. Kauppinen A. Kaarniranta K. Suuronen T. Activation of innate immunity system during aging: NF-kB signaling is the molecular culprit of inflamm-aging Ageing Res. Rev. 2008 7 83 105 10.1016/j.arr.2007.09.002 17964225 · DOI · Paper page
  94. [107]Kounatidis I. Chtarbanova S. Cao Y. Hayne M. Jayanth D. Ganetzky B. Ligoxygakis P. NF-kappaB Immunity in the Brain Determines Fly Lifespan in Healthy Aging and Age-Related Neurodegeneration Cell Rep. 2017 19 836 848 10.1016/j.celrep.2017.04.007 28445733 PMC5413584 · DOI
  95. [108]Wang Z.R. Li Y.X. Lei H.Y. Yang D.Q. Wang L.Q. Luo M.Y. Regulating effect of activated NF-kappaB on edema induced by traumatic brain injury of rats Asian Pac. J. Trop. Med. 2016 9 274 277 10.1016/j.apjtm.2016.01.027 26972401 · DOI
  96. [110]Liu T. Zhang L. Joo D. Sun S.C. NF-kappaB signaling in inflammation Signal. Transduct. Target. Ther. 2017 2 1 9 10.1038/sigtrans.2017.23 PMC5661633 29158945 · DOI · Paper page
  97. [111]Correia A.S. Patel P. Dutta K. Julien J.P. Inflammation Induces TDP-43 Mislocalization and Aggregation PLoS ONE 2015 10 e0140248 10.1371/journal.pone.0140248 26444430 PMC4596857 · DOI · Paper page
  98. [112]Zhao W. Beers D.R. Bell S. Wang J. Wen S. Baloh R.H. Appel S.H. TDP-43 activates microglia through NF-kappaB and NLRP3 inflammasome Exp. Neurol. 2015 273 24 35 10.1016/j.expneurol.2015.07.019 26222336 · DOI · Paper page
  99. [113]Frakes A.E. Ferraiuolo L. Haidet-Phillips A.M. Schmelzer L. Braun L. Miranda C.J. Ladner K.J. Bevan A.K. Foust K.D. Godbout J.P. Microglia induce motor neuron death via the classical NF-kappaB pathway in amyotrophic lateral sclerosis Neuron 2014 81 1009 1023 10.1016/j.neuron.2014.01.013 24607225 PMC3978641 · DOI · Paper page
  100. [114]Dutta K. Thammisetty S.S. Boutej H. Bareil C. Julien J.P. Mitigation of ALS Pathology by Neuron-Specific Inhibition of Nuclear Factor Kappa B Signaling J. Neurosci. 2020 40 5137 5154 10.1523/JNEUROSCI.0536-20.2020 32457070 PMC7314413 · DOI · Paper page
  101. [115]Zhu J. Cynader M.S. Jia W. TDP-43 Inhibits NF-kappaB Activity by Blocking p65 Nuclear Translocation PLoS ONE 2015 10 e0142296 10.1371/journal.pone.0142296 26571498 PMC4646651 · DOI
  102. [116]Swarup V. Phaneuf D. Dupre N. Petri S. Strong M. Kriz J. Julien J.P. Deregulation of TDP-43 in amyotrophic lateral sclerosis triggers nuclear factor kappaB-mediated pathogenic pathways J. Exp. Med. 2011 208 2429 2447 10.1084/jem.20111313 22084410 PMC3256969 · DOI
  103. [117]Pozzi S. Thammisetty S.S. Codron P. Rahimian R. Plourde K.V. Soucy G. Bareil C. Phaneuf D. Kriz J. Gravel C. Virus-mediated delivery of antibody targeting TAR DNA-binding protein-43 mitigates associated neuropathology J. Clin. Investig. 2019 129 1581 1595 10.1172/JCI123931 30667370 PMC6436898 · DOI
  104. [118]Gao J. Wang L. Huntley M.L. Perry G. Wang X. Pathomechanisms of TDP-43 in neurodegeneration J. Neurochem. 2018 146 7 20 10.1111/jnc.14327 29486049 PMC6110993 · DOI
  105. [119]Ke Y.D. van Hummel A. Stevens C.H. Gladbach A. Ippati S. Bi M. Lee W.S. Kruger S. van der Hoven J. Volkerling A. Short-term suppression of A315T mutant human TDP-43 expression improves functional deficits in a novel inducible transgenic mouse model of FTLD-TDP and ALS Acta Neuropathol. 2015 130 661 678 10.1007/s00401-015-1486-0 26437864 · DOI
  106. [120]Ohta Y. Tremblay C. Schneider J.A. Bennett D.A. Calon F. Julien J.P. Interaction of transactive response DNA binding protein 43 with nuclear factor kappaB in mild cognitive impairment with episodic memory deficits Acta Neuropathol. Commun. 2014 2 37 10.1186/2051-5960-2-37 24690380 PMC4230634 · DOI
  107. [121]Kallstig E. McCabe B.D. Schneider B.L. The Links between ALS and NF-kappaB Int. J. Mol. Sci. 2021 22 3875 10.3390/ijms22083875 33918092 PMC8070122 · DOI
  108. [122]Paul B.D. Snyder S.H. Bohr V.A. Signaling by cGAS-STING in Neurodegeneration, Neuroinflammation, and Aging Trends Neurosci. 2021 44 83 96 10.1016/j.tins.2020.10.008 33187730 PMC8662531 · DOI
  109. [123]Yu C.H. Davidson S. Harapas C.R. Hilton J.B. Mlodzianoski M.J. Laohamonthonkul P. Louis C. Low R.R.J. Moecking J. De Nardo D. TDP-43 Triggers Mitochondrial DNA Release via mPTP to Activate cGAS/STING in ALS Cell 2020 183 636 649 10.1016/j.cell.2020.09.020 33031745 PMC7599077 · DOI · Paper page
  110. [124]Magrane J. Cortez C. Gan W.B. Manfredi G. Abnormal mitochondrial transport and morphology are common pathological denominators in SOD1 and TDP43 ALS mouse models Hum. Mol. Genet. 2014 23 1413 1424 10.1093/hmg/ddt528 24154542 PMC3929084 · DOI
  111. [125]Wang W. Li L. Lin W.L. Dickson D.W. Petrucelli L. Zhang T. Wang X. The ALS disease-associated mutant TDP-43 impairs mitochondrial dynamics and function in motor neurons Hum. Mol. Genet. 2013 22 4706 4719 10.1093/hmg/ddt319 23827948 PMC3820133 · DOI
  112. [126]Zhao C. Zhao W. NLRP3 Inflammasome-A Key Player in Antiviral Responses Front. Immunol. 2020 11 211 10.3389/fimmu.2020.00211 32133002 PMC7040071 · DOI
  113. [127]He Y. Hara H. Nunez G. Mechanism and Regulation of NLRP3 Inflammasome Activation Trends Biochem. Sci. 2016 41 1012 1021 10.1016/j.tibs.2016.09.002 27669650 PMC5123939 · DOI · Paper page
  114. [129]Kadhim H. Deltenre P. Martin J.J. Sebire G. In-situ expression of Interleukin-18 and associated mediators in the human brain of sALS patients: Hypothesis for a role for immune-inflammatory mechanisms Med. Hypotheses 2016 86 14 17 10.1016/j.mehy.2015.11.022 26804591 · DOI · Paper page
  115. [130]Zhuang J. Wen X. Zhang Y.Q. Shan Q. Zhang Z.F. Zheng G.H. Fan S.H. Li M.Q. Wu D.M. Hu B. TDP-43 upregulation mediated by the NLRP3 inflammasome induces cognitive impairment in 2 2’,4,4’-tetrabromodiphenyl ether (BDE-47)-treated mice Brain Behav. Immun. 2017 65 99 110 10.1016/j.bbi.2017.05.014 28532818 · DOI
  116. [132]Hebron M.L. Lonskaya I. Sharpe K. Weerasinghe P.P. Algarzae N.K. Shekoyan A.R. Moussa C.E. Parkin ubiquitinates Tar-DNA binding protein-43 (TDP-43) and promotes its cytosolic accumulation via interaction with histone deacetylase 6 (HDAC6) J. Biol. Chem. 2013 288 4103 4115 10.1074/jbc.M112.419945 23258539 PMC3567661 · DOI
  117. [133]Wenqiang C. Lonskaya I. Hebron M.L. Ibrahim Z. Olszewski R.T. Neale J.H. Moussa C.E. Parkin-mediated reduction of nuclear and soluble TDP-43 reverses behavioral decline in symptomatic mice Hum. Mol. Genet. 2014 23 4960 4969 10.1093/hmg/ddu211 24847002 · DOI
  118. [134]Lagier-Tourenne C. Polymenidou M. Hutt K.R. Vu A.Q. Baughn M. Huelga S.C. Clutario K.M. Ling S.C. Liang T.Y. Mazur C. Divergent roles of ALS-linked proteins FUS/TLS and TDP-43 intersect in processing long pre-mRNAs Nat. Neurosci. 2012 15 1488 1497 10.1038/nn.3230 23023293 PMC3586380 · DOI
  119. [135]Sun X. Duan Y. Qin C. Li J.C. Duan G. Deng X. Ni J. Cao X. Xiang K. Tian K. Distinct multilevel misregulations of Parkin and PINK1 revealed in cell and animal models of TDP-43 proteinopathy Cell Death Dis. 2018 9 953 10.1038/s41419-018-1022-y 30237395 PMC6148241 · DOI
  120. [136]Deora V. Lee J.D. Albornoz E.A. McAlary L. Jagaraj C.J. Robertson A.A.B. Atkin J.D. Cooper M.A. Schroder K. Yerbury J.J. The microglial NLRP3 inflammasome is activated by amyotrophic lateral sclerosis proteins Glia 2020 68 407 421 10.1002/glia.23728 31596526 · DOI · Paper page
  121. [137]Trageser K.J. Smith C. Herman F.J. Ono K. Pasinetti G.M. Mechanisms of Immune Activation by c9orf72-Expansions in Amyotrophic Lateral Sclerosis and Frontotemporal Dementia Front. Neurosci. 2019 13 1298 10.3389/fnins.2019.01298 31920478 PMC6914852 · DOI
  122. [138]Guo W. Vandoorne T. Steyaert J. Staats K.A. Van Den Bosch L. The multifaceted role of kinases in amyotrophic lateral sclerosis: Genetic, pathological and therapeutic implications Brain 2020 143 1651 1673 10.1093/brain/awaa022 32206784 PMC7296858 · DOI
  123. [139]Oakes J.A. Davies M.C. Collins M.O. TBK1: A new player in ALS linking autophagy and neuroinflammation Mol. Brain 2017 10 5 10.1186/s13041-017-0287-x 28148298 PMC5288885 · DOI · Paper page
  124. [140]Asih P.R. Prikas E. Stefanoska K. Tan A.R.P. Ahel H.I. Ittner A. Functions of p38 MAP Kinases in the Central Nervous System Front. Mol. Neurosci. 2020 13 570586 10.3389/fnmol.2020.570586 33013322 PMC7509416 · DOI
  125. [141]Zhan L. Xie Q. Tibbetts R.S. Opposing roles of p38 and JNK in a Drosophila model of TDP-43 proteinopathy reveal oxidative stress and innate immunity as pathogenic components of neurodegeneration Hum. Mol. Genet. 2015 24 757 772 10.1093/hmg/ddu493 25281658 PMC4291250 · DOI
  126. [142]Van Deerlin V.M. Leverenz J.B. Bekris L.M. Bird T.D. Yuan W. Elman L.B. Clay D. Wood E.M. Chen-Plotkin A.S. Martinez-Lage M. TARDBP mutations in amyotrophic lateral sclerosis with TDP-43 neuropathology: A genetic and histopathological analysis Lancet Neurol. 2008 7 409 416 10.1016/S1474-4422(08)70071-1 18396105 PMC3546119 · DOI · Paper page
  127. [143]Huang H. Zhang Z.F. Qin F.W. Tang W. Liu D.H. Wu P.Y. Jiao F. The mechanism of TDP-43 gene expression on inflammatory factors and the JNK and p38 MAPK signalling pathways in ischaemic hypoxic stress dependence Int. Wound J. 2019 16 724 729 10.1111/iwj.13087 30784197 PMC7949179 · DOI
  128. [144]Woodruff T.M. Costantini K.J. Crane J.W. Atkin J.D. Monk P.N. Taylor S.M. Noakes P.G. The complement factor C5a contributes to pathology in a rat model of amyotrophic lateral sclerosis J. Immunol. 2008 181 8727 8734 10.4049/jimmunol.181.12.8727 19050293 · DOI
  129. [145]Sta M. Sylva-Steenland R.M. Casula M. de Jong J.M. Troost D. Aronica E. Baas F. Innate and adaptive immunity in amyotrophic lateral sclerosis: Evidence of complement activation Neurobiol. Dis. 2011 42 211 220 10.1016/j.nbd.2011.01.002 21220013 · DOI
  130. [146]Lee J.D. Levin S.C. Willis E.F. Li R. Woodruff T.M. Noakes P.G. Complement components are upregulated and correlate with disease progression in the TDP-43(Q331K) mouse model of amyotrophic lateral sclerosis J. Neuroinflamm. 2018 15 171 10.1186/s12974-018-1217-2 29859100 PMC5984816 · DOI
  131. [147]Stephan A.H. Barres B.A. Stevens B. The complement system: An unexpected role in synaptic pruning during development and disease Annu. Rev. Neurosci. 2012 35 369 389 10.1146/annurev-neuro-061010-113810 22715882 · DOI · Paper page
  132. [148]Heyburn L. Hebron M.L. Smith J. Winston C. Bechara J. Li Z. Lonskaya I. Burns M.P. Harris B.T. Moussa C.E. Tyrosine kinase inhibition reverses TDP-43 effects on synaptic protein expression, astrocytic function and amino acid dis-homeostasis J. Neurochem. 2016 139 610 623 10.1111/jnc.13763 27507246 · DOI
  133. [149]Sephton C.F. Yu G. The function of RNA-binding proteins at the synapse: Implications for neurodegeneration Cell. Mol. Life Sci. 2015 72 3621 3635 10.1007/s00018-015-1943-x 26047658 PMC4565867 · DOI
  134. [150]Naviaux J.C. Wang L. Li K. Bright A.T. Alaynick W.A. Williams K.R. Powell S.B. Naviaux R.K. Antipurinergic therapy corrects the autism-like features in the Fragile X (Fmr1 knockout) mouse model Mol. Autism 2015 6 1 10.1186/2040-2392-6-1 25705365 PMC4334917 · DOI · Paper page
  135. [151]Zhang J. Velmeshev D. Hashimoto K. Huang Y.H. Hofmann J.W. Shi X. Chen J. Leidal A.M. Dishart J.G. Cahill M.K. Neurotoxic microglia promote TDP-43 proteinopathy in progranulin deficiency Nature 2020 588 459 465 10.1038/s41586-020-2709-7 32866962 PMC7746606 · DOI
  136. [152]Miller Z.A. Rankin K.P. Graff-Radford N.R. Takada L.T. Sturm V.E. Cleveland C.M. Criswell L.A. Jaeger P.A. Stan T. Heggeli K.A. TDP-43 frontotemporal lobar degeneration and autoimmune disease J. Neurol. Neurosurg. Psychiatry 2013 84 956 962 10.1136/jnnp-2012-304644 23543794 PMC3840954 · DOI · Paper page
  137. [153]Miller Z.A. Sturm V.E. Camsari G.B. Karydas A. Yokoyama J.S. Grinberg L.T. Boxer A.L. Rosen H.J. Rankin K.P. Gorno-Tempini M.L. Increased prevalence of autoimmune disease within C9 and FTD/MND cohorts: Completing the picture Neurol. Neuroimmunol. Neuroinflamm. 2016 3 e301 10.1212/NXI.0000000000000301 27844039 PMC5087253 · DOI · Paper page
  138. [154]Katisko K. Solje E. Koivisto A.M. Kruger J. Kinnunen T. Hartikainen P. Helisalmi S. Korhonen V. Herukka S.K. Haapasalo A. Prevalence of immunological diseases in a Finnish frontotemporal lobar degeneration cohort with the C9orf72 repeat expansion carriers and non-carriers J. Neuroimmunol. 2018 321 29 35 10.1016/j.jneuroim.2018.05.011 29957385 · DOI
  139. [155]Lan Y. Sullivan P.M. Hu F. SMCR8 negatively regulates AKT and MTORC1 signaling to modulate lysosome biogenesis and tissue homeostasis Autophagy 2019 15 871 885 10.1080/15548627.2019.1569914 30696333 PMC6526807 · DOI
  140. [156]Jian J. Li G. Hettinghouse A. Liu C. Progranulin: A key player in autoimmune diseases Cytokine 2018 101 48 55 10.1016/j.cyto.2016.08.007 27527809 PMC5303690 · DOI
  141. [157]Thurner L. Stoger E. Fadle N. Klemm P. Regitz E. Kemele M. Bette B. Held G. Dauer M. Lammert F. Proinflammatory progranulin antibodies in inflammatory bowel diseases Dig. Dis. Sci. 2014 59 1733 1742 10.1007/s10620-014-3089-3 24591016 · DOI
  142. [158]Jayaraj R.L. Azimullah S. Beiram R. Jalal F.Y. Rosenberg G.A. Neuroinflammation: Friend and foe for ischemic stroke J. Neuroinflamm. 2019 16 142 10.1186/s12974-019-1516-2 PMC6617684 31291966 · DOI
  143. [159]Lee E.B. Lee V.M. Trojanowski J.Q. Neumann M. TDP-43 immunoreactivity in anoxic, ischemic and neoplastic lesions of the central nervous system Acta. Neuropathol. 2008 115 305 311 10.1007/s00401-007-0331-5 18087705 · DOI
  144. [160]Kanazawa M. Kakita A. Igarashi H. Takahashi T. Kawamura K. Takahashi H. Nakada T. Nishizawa M. Shimohata T. Biochemical and histopathological alterations in TAR DNA-binding protein-43 after acute ischemic stroke in rats J. Neurochem. 2011 116 957 965 10.1111/j.1471-4159.2010.06860.x 20557425 · DOI
  145. [161]Thammisetty S.S. Pedragosa J. Weng Y.C. Calon F. Planas A. Kriz J. Age-related deregulation of TDP-43 after stroke enhances NF-kappaB-mediated inflammation and neuronal damage J. Neuroinflamm. 2018 15 312 10.1186/s12974-018-1350-y PMC6230239 30413172 · DOI
  146. [162]He T. Zuo Y. Ai-Zakwani K. Luo J. Zhu H. Yan X.X. Liu F. Subarachnoid hemorrhage enhances the expression of TDP-43 in the brain of experimental rats and human subjects Exp. Ther. Med. 2018 16 3363 3368 10.3892/etm.2018.6636 30233682 PMC6143865 · DOI
  147. [163]Kahl A. Blanco I. Jackman K. Baskar J. Milaganur Mohan H. Rodney-Sandy R. Zhang S. Iadecola C. Hochrainer K. Cerebral ischemia induces the aggregation of proteins linked to neurodegenerative diseases Sci. Rep. 2018 8 2701 10.1038/s41598-018-21063-z 29426953 PMC5807442 · DOI
  148. [164]Sun M. Yamashita T. Shang J. Liu N. Deguchi K. Liu W. Ikeda Y. Feng J. Abe K. Acceleration of TDP43 and FUS/TLS protein expressions in the preconditioned hippocampus following repeated transient ischemia J. Neurosci. Res. 2014 92 54 63 10.1002/jnr.23301 24265138 · DOI
  149. [165]Blennow K. Hardy J. Zetterberg H. The neuropathology and neurobiology of traumatic brain injury Neuron 2012 76 886 899 10.1016/j.neuron.2012.11.021 23217738 · DOI · Paper page
  150. [166]McKee A.C. Gavett B.E. Stern R.A. Nowinski C.J. Cantu R.C. Kowall N.W. Perl D.P. Hedley-Whyte E.T. Price B. Sullivan C. TDP-43 proteinopathy and motor neuron disease in chronic traumatic encephalopathy J. Neuropathol. Exp. Neurol. 2010 69 918 929 10.1097/NEN.0b013e3181ee7d85 20720505 PMC2951281 · DOI · Paper page
  151. [167]McKee A.C. Robinson M.E. Military-related traumatic brain injury and neurodegeneration Alzheimers Dement. 2014 10 S242 S253 10.1016/j.jalz.2014.04.003 24924675 PMC4255273 · DOI · Paper page
  152. [168]Kenney K. Iacono D. Edlow B.L. Katz D.I. Diaz-Arrastia R. Dams-O’Connor K. Daneshvar D.H. Stevens A. Moreau A.L. Tirrell L.S. Dementia After Moderate-Severe Traumatic Brain Injury: Coexistence of Multiple Proteinopathies J. Neuropathol. Exp. Neurol. 2018 77 50 63 10.1093/jnen/nlx101 29155947 PMC5939622 · DOI
  153. [169]Wang H.K. Lee Y.C. Huang C.Y. Liliang P.C. Lu K. Chen H.J. Li Y.C. Tsai K.J. Traumatic brain injury causes frontotemporal dementia and TDP-43 proteolysis Neuroscience 2015 300 94 103 10.1016/j.neuroscience.2015.05.013 25982564 · DOI
  154. [170]Huang C.Y. Lee Y.C. Li P.C. Liliang P.C. Lu K. Wang K.W. Chang L.C. Shiu L.Y. Chen M.F. Sun Y.T. TDP-43 proteolysis is associated with astrocyte reactivity after traumatic brain injury in rodents J. Neuroimmunol. 2017 313 61 68 10.1016/j.jneuroim.2017.10.011 29153610 · DOI
  155. [171]Zhang J. Teng Z. Song Y. Hu M. Chen C. Inhibition of monoacylglycerol lipase prevents chronic traumatic encephalopathy-like neuropathology in a mouse model of repetitive mild closed head injury J. Cereb. Blood Flow Metab. 2015 35 706 10.1038/jcbfm.2014.247 25826320 PMC4420888 · DOI
  156. [172]Wiesner D. Tar L. Linkus B. Chandrasekar A. Olde Heuvel F. Dupuis L. Tsao W. Wong P.C. Ludolph A. Roselli F. Reversible induction of TDP-43 granules in cortical neurons after traumatic injury Exp. Neurol. 2018 299 15 25 10.1016/j.expneurol.2017.09.011 28941811 · DOI
  157. [173]Heyburn L. Sajja V. Long J.B. The Role of TDP-43 in Military-Relevant TBI and Chronic Neurodegeneration Front. Neurol. 2019 10 680 10.3389/fneur.2019.00680 31316455 PMC6610302 · DOI
  158. [174]Braak H. Brettschneider J. Ludolph A.C. Lee V.M. Trojanowski J.Q. Del Tredici K. Amyotrophic lateral sclerosis--a model of corticofugal axonal spread Nat. Rev. Neurol. 2013 9 708 714 10.1038/nrneurol.2013.221 24217521 PMC3943211 · DOI
  159. [175]Anderson E.N. Gochenaur L. Singh A. Grant R. Patel K. Watkins S. Wu J.Y. Pandey U.B. Traumatic injury induces stress granule formation and enhances motor dysfunctions in ALS/FTD models Hum. Mol. Genet. 2018 27 1366 1381 10.1093/hmg/ddy047 29432563 PMC6455923 · DOI · Paper page
  160. [176]Anderson E.N. Morera A.A. Kour S. Cherry J.D. Ramesh N. Gleixner A. Schwartz J.C. Ebmeier C. Old W. Donnelly C.J. Traumatic injury compromises nucleocytoplasmic transport and leads to TDP-43 pathology eLife 2021 10 e67587 10.7554/eLife.67587 34060470 PMC8169113 · DOI

Cited by

Sorted by citations

Authors
Bright, F., Chan, G., van Hummel, A., Ittner, L. M., & Ke, Y. D.
Affiliations
  • Macquarie University (AU)
  • Dementia Research Centre, Department of Biomedical Science, Faculty of Medicine Health and Human Sciences, Macquarie University, Sydney, NSW 2109, Australia
Corresponding author
  • Bright, Fiona
  • Ke, Yazi D.
ORCID
Venue
International Journal of Molecular Sciences
Publisher
MDPI AG
Published
2021-07-21
Volume
22
Issue
15
Pages
7781
ISSN
1422-0067 (ISSN-L)
DOI
10.3390/ijms22157781
PMC
PMC8346169
OpenAlex
W3183448209
Cited by
71
References
16
Citations by year
2026: 14 · 2025: 19 · 2024: 17 · 2023: 11 · 2022: 7 · 2021: 3
FWCI
1.22
Type
journal article
Language
en
Open access
Licence
Locations
  • International Journal of Molecular Sciences (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
  • Motor Neurone Disease Australia (BJLP2105)
  • Motor Neurone Disease Research Australia
  • Macquarie University (#1136241, 1123564)
  • Medical Research Council
  • National Health and Medical Research Council (1143978, 1136241, 1132524, 2001572, 1123564, 1143848)
Topics
  • Health Sciences › Medicine › Neurology › Amyotrophic Lateral Sclerosis Research
  • Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
  • Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
Keywords
TDP-43, amyotrophic lateral sclerosis, frontotemporal dementia, neuroinflammation, protein aggregation, immune-mediated neurodegeneration, neurodegeneration pathogenesis, ubiquitinated protein aggregates
MeSH terms
Amyotrophic Lateral Sclerosis, Animals, DNA-Binding Proteins, Humans, Inflammation, Mutation, Frontotemporal Dementia

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