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Astrocytes: Dissecting Their Diverse Roles in Amyotrophic Lateral Sclerosis and Frontotemporal Dementia

Valori, Chiara F., Sulmona, Claudia, Brambilla, Liliana, Rossi, Daniela·2023·Cells
DOI 10.3390/cells12111450PMC PMC10252425
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Abstract

Amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD) are fatal neurodegenerative disorders often co-occurring in the same patient, a feature that suggests a common origin of the two diseases. Consistently, pathological inclusions of the same proteins as well as mutations in the same genes can be identified in both ALS/FTD. Although many studies have described several disrupted pathways within neurons, glial cells are also regarded as crucial pathogenetic contributors in ALS/FTD. Here, we focus our attention on astrocytes, a heterogenous population of glial cells that perform several functions for optimal central nervous system homeostasis. Firstly, we discuss how post-mortem material from ALS/FTD patients supports astrocyte dysfunction around three pillars: neuroinflammation, abnormal protein aggregation, and atrophy/degeneration. Furthermore, we summarize current attempts at monitoring astrocyte functions in living patients using either novel imaging strategies or soluble biomarkers. We then address how astrocyte pathology is recapitulated in animal and cellular models of ALS/FTD and how we used these models both to understand the molecular mechanisms driving glial dysfunction and as platforms for pre-clinical testing of therapeutics. Finally, we present the current clinical trials for ALS/FTD, restricting our discussion to treatments that modulate astrocyte functions, directly or indirectly.

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  • Understanding of the role of astrocytes in FTD pathogenesis is limited.

    “Given the limited understanding of the role of astrocytes in FTD pathogenesis [39] we have decided to investigate the role of miR-129-5p in astrocytes in more detail.”

    From A role for astrocytic miR-129-5p in frontotemporal dementia (2025) · cites this paper as [39]

  • The role of astrocytes in the pathogenesis of FTD and other neurodegenerative diseases is increasingly being recognized.

    “Although most of the research in FTD has been focused on neuronal dysfunction and neuronal cell death, the role of astrocytes in the pathogenesis of FTD and other neurodegenerative diseases is increasingly being recognized [39, 81–83].”

    From A role for astrocytic miR-129-5p in frontotemporal dementia (2025) · cites this paper as [39]

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Research works printed but not linked: 207

  1. Feldman, 2022, Amyotrophic lateral sclerosis, Lancet, 400, 1363, 10.1016/S0140-6736(22)01272-7 · DOI
  2. Kirola, 2022, Recent Updates on the Genetics of Amyotrophic Lateral Sclerosis and Frontotemporal Dementia, Mol. Neurobiol., 59, 5673, 10.1007/s12035-022-02934-z · DOI
  3. Hardiman, 2017, Amyotrophic lateral sclerosis, Nat. Rev. Dis. Primers, 3, 17071, 10.1038/nrdp.2017.71 · DOI
  4. Vahsen, 2021, Non-neuronal cells in amyotrophic lateral sclerosis—From pathogenesis to biomarkers, Nat. Rev. Neurol., 17, 333, 10.1038/s41582-021-00487-8 · DOI · Paper page
  5. Ghasemi, M., Keyhanian, K., and Douthwright, C. (2021). Glial Cell Dysfunction in C9orf72-Related Amyotrophic Lateral Sclerosis and Frontotemporal Dementia. Cells, 10. · DOI
  6. Tam, 2019, Postmortem Cortex Samples Identify Distinct Molecular Subtypes of ALS: Retrotransposon Activation, Oxidative Stress, and Activated Glia, Cell Rep., 29, 1164, 10.1016/j.celrep.2019.09.066 · DOI · Paper page
  7. Eshima, 2023, Molecular subtypes of ALS are associated with differences in patient prognosis, Nat. Commun., 14, 95, 10.1038/s41467-022-35494-w · DOI
  8. Verkhratsky, 2017, Stratification of astrocytes in healthy and diseased brain, Brain Pathol., 27, 629, 10.1111/bpa.12537 · DOI · Paper page
  9. Khakh, 2019, The Emerging Nature of Astrocyte Diversity, Annu. Rev. Neurosci., 42, 187, 10.1146/annurev-neuro-070918-050443 · DOI
  10. Endo, 2022, Molecular basis of astrocyte diversity and morphology across the CNS in health and disease, Science, 378, eadc9020, 10.1126/science.adc9020 · DOI · Paper page
  11. Rossi, 2015, Astrocyte physiopathology: At the crossroads of intercellular networking, inflammation and cell death, Prog. Neurobiol., 130, 86, 10.1016/j.pneurobio.2015.04.003 · DOI
  12. Verkhratsky, 2019, Physiology of Astroglia, Adv. Exp. Med. Biol., 1175, 45, 10.1007/978-981-13-9913-8_3 · DOI
  13. Zhang, 2016, Purification and Characterization of Progenitor and Mature Human Astrocytes Reveals Transcriptional and Functional Differences with Mouse, Neuron, 89, 37, 10.1016/j.neuron.2015.11.013 · DOI · Paper page
  14. Li, 2021, Conservation and divergence of vulnerability and responses to stressors between human and mouse astrocytes, Nat. Commun., 12, 3958, 10.1038/s41467-021-24232-3 · DOI
  15. Franklin, 2021, Astrocytes and microglia in neurodegenerative diseases: Lessons from human in vitro models, Prog. Neurobiol., 200, 101973, 10.1016/j.pneurobio.2020.101973 · DOI · Paper page
  16. Yu, 2020, Context-Specific Striatal Astrocyte Molecular Responses Are Phenotypically Exploitable, Neuron, 108, 1146, 10.1016/j.neuron.2020.09.021 · DOI
  17. Burda, 2022, Divergent transcriptional regulation of astrocyte reactivity across disorders, Nature, 606, 557, 10.1038/s41586-022-04739-5 · DOI · Paper page
  18. Zamanian, 2012, Genomic analysis of reactive astrogliosis, J. Neurosci., 32, 6391, 10.1523/JNEUROSCI.6221-11.2012 · DOI · Paper page
  19. Valori, 2019, Astrocytes in Motor Neuron Diseases, Adv. Exp. Med. Biol., 1175, 227, 10.1007/978-981-13-9913-8_10 · DOI
  20. Black, 1996, Focal Cortical Atrophy Syndromes, Brain Cogn., 31, 188, 10.1006/brcg.1996.0042 · DOI
  21. Schiffer, 1996, Reactive astrogliosis of the spinal cord in amyotrophic lateral sclerosis, J. Neurol. Sci., 139, 27, 10.1016/0022-510X(96)00073-1 · DOI
  22. Roedica, 1995, Motor neuron-astrocyte interactions and levels of Cu,Zn superoxide dismutase in sporadic amyotrophic lateral sclerosis, Exp. Neurol., 131, 203, 10.1016/0014-4886(95)90042-X · DOI
  23. Manberg, 2021, Altered perivascular fibroblast activity precedes ALS disease onset, Nat. Med., 27, 640, 10.1038/s41591-021-01295-9 · DOI · Paper page
  24. Kato, 1999, Recent advances in research on neuropathological aspects of familial amyotrophic lateral sclerosis with superoxide dismutase 1 gene mutations: Neuronal Lewy body-like hyaline inclusions and astrocytic hyaline inclusions, Histol. Histopathol., 14, 973
  25. Martorana, 2012, The BH4 domain of Bcl-X(L) rescues astrocyte degeneration in amyotrophic lateral sclerosis by modulating intracellular calcium signals, Hum. Mol. Genet., 21, 826, 10.1093/hmg/ddr513 · DOI
  26. Mendonca, 2006, Expression of ubiquitin and proteasome in motorneurons and astrocytes of spinal cords from patients with amyotrophic lateral sclerosis, Neurosci. Lett., 404, 315, 10.1016/j.neulet.2006.06.009 · DOI
  27. Pasinelli, 2000, Caspase-1 and -3 are sequentially activated in motor neuron death in Cu,Zn superoxide dismutase-mediated familial amyotrophic lateral sclerosis, Proc. Natl. Acad. Sci. USA, 97, 13901, 10.1073/pnas.240305897 · DOI
  28. Nishihira, 2008, Sporadic amyotrophic lateral sclerosis: Two pathological patterns shown by analysis of distribution of TDP-43-immunoreactive neuronal and glial cytoplasmic inclusions, Acta Neuropathol., 116, 169, 10.1007/s00401-008-0385-z · DOI · Paper page
  29. Reid, 2020, Astrocytes in Tauopathies, Front. Neurol., 11, 572850, 10.3389/fneur.2020.572850 · DOI
  30. Gelpi, 2021, Atypical astroglial pTDP-43 pathology in astroglial predominant tauopathy, Neuropathol. Appl. Neurobiol., 47, 1109, 10.1111/nan.12707 · DOI
  31. Lee, 2021, A novel temporal-predominant neuro-astroglial tauopathy associated with TMEM106B gene polymorphism in FTLD/ALS-TDP, Brain Pathol., 31, 267, 10.1111/bpa.12924 · DOI
  32. Su, 2000, DNA damage and activated caspase-3 expression in neurons and astrocytes: Evidence for apoptosis in frontotemporal dementia, Exp. Neurol., 163, 9, 10.1006/exnr.2000.7340 · DOI
  33. Martinac, 2001, Astrocytes degenerate in frontotemporal dementia: Possible relation to hypoperfusion, Neurobiol. Aging, 22, 195, 10.1016/S0197-4580(00)00231-1 · DOI
  34. Broe, 2004, Astrocytic degeneration relates to the severity of disease in frontotemporal dementia, Brain, 127, 2214, 10.1093/brain/awh250 · DOI · Paper page
  35. Gerrits, 2022, Neurovascular dysfunction in GRN-associated frontotemporal dementia identified by single-nucleus RNA sequencing of human cerebral cortex, Nat. Neurosci., 25, 1034, 10.1038/s41593-022-01124-3 · DOI · Paper page
  36. Marsan, 2023, Astroglial toxicity promotes synaptic degeneration in the thalamocortical circuit in frontotemporal dementia with GRN mutations, J. Clin. Investig., 133, e164919, 10.1172/JCI164919 · DOI · Paper page
  37. Miedema, 2022, Distinct cell type-specific protein signatures in GRN and MAPT genetic subtypes of frontotemporal dementia, Acta Neuropathol. Commun., 10, 100, 10.1186/s40478-022-01387-8 · DOI
  38. Tisdall, 2022, Ex vivo MRI and histopathology detect novel iron-rich cortical inflammation in frontotemporal lobar degeneration with tau versus TDP-43 pathology, Neuroimage Clin., 33, 102913, 10.1016/j.nicl.2021.102913 · DOI
  39. Pineda, S.S., Lee, H., Fitzwalter, B.E., Mohammadi, S., Pregent, L.J., Gardashli, M.E., Mantero, J., Engelberg-Cook, E., DeJesus-Hernandez, M., and van Blitterswijk, M. (2021). Single-cell profiling of the human primary motor cortex in ALS and FTLD. bioRxiv. · DOI
  40. Limone, F., Mordes, D., Couto, A., Pietiläinen, O., Joseph, B.J., Burberry, A., Ghosh, S.D., Meyer, D., Goldman, M., and Bortolin, L. (2021). Single-nucleus sequencing reveals enriched expression of genetic risk factors sensitises Motor Neurons to degeneration in ALS. bioRxiv. · DOI
  41. Masrori, P., Bijnens, B., Davie, K., Poovathingal, S.K., Storm, A., Hersmus, N., Fumagalli, L., Van Den Bosch, L., Fiers, M., and Thal, D.R. (2022). Hexanucleotide repeat expansions in C9orf72 alter microglial responses and prevent a coordinated glial reaction in ALS. bioRxiv. · DOI
  42. Li, J., Jaiswal, M.K., Chien, J.-F., Kozlenkov, A., Zhou, P., Gardashli, M., Pregent, L.J., Engelberg-Cook, E., Dickson, D.W., and Belzil, V.V. (2022). Divergent impacts of C9orf72 repeat expansion on neurons and glia in ALS and FTD. bioRxiv. · DOI
  43. Wang, H.-L.V., Veire, A.M., Gendron, T.F., Gearing, M., Glass, J.D., Jin, P., Corces, V.G., and McEachin, Z.T. (2023). Single nucleus multiome analysis of the prefrontal cortex from C9orf72 ALS/FTD patients illuminates pathways affected during disease progression. bioRxiv. · DOI
  44. Gregory, 2020, Spatial transcriptomics identifies spatially dysregulated expression of GRM3 and USP47 in amyotrophic lateral sclerosis, Neuropathol. Appl. Neurobiol., 46, 441, 10.1111/nan.12597 · DOI
  45. Johansson, 2007, Evidence for astrocytosis in ALS demonstrated by [11C](L)-deprenyl-D2 PET, J. Neurol. Sci., 255, 17, 10.1016/j.jns.2007.01.057 · DOI
  46. Taoka, 2017, Evaluation of glymphatic system activity with the diffusion MR technique: Diffusion tensor image analysis along the perivascular space (DTI-ALPS) in Alzheimer’s disease cases, Jpn. J. Radiol., 35, 172, 10.1007/s11604-017-0617-z · DOI
  47. Hsu, 2022, Magnetic Resonance Images Implicate That Glymphatic Alterations Mediate Cognitive Dysfunction in Alzheimer Disease, Ann. Neurol., 93, 164, 10.1002/ana.26516 · DOI
  48. Cai, 2022, Diffusion along perivascular spaces provides evidence interlinking compromised glymphatic function with aging in Parkinson’s disease, CNS Neurosci. Ther., 29, 111, 10.1111/cns.13984 · DOI
  49. Langen, 2019, Development and Cell Biology of the Blood-Brain Barrier, Annu. Rev. Cell Dev. Biol., 35, 591, 10.1146/annurev-cellbio-100617-062608 · DOI
  50. Apostolski, 1991, Serum and CSF immunological findings in ALS, Acta Neurol. Scand., 83, 96, 10.1111/j.1600-0404.1991.tb04656.x · DOI · Paper page
  51. Li, 2022, Blood-brain barrier dysfunction and myelin basic protein in survival of amyotrophic lateral sclerosis with or without frontotemporal dementia, Neurol. Sci., 43, 3201, 10.1007/s10072-021-05731-z · DOI
  52. Assialioui, A., Domínguez, R., Ferrer, I., Andrés-Benito, P., and Povedano, M. (2022). Elevated Cerebrospinal Fluid Proteins and Albumin Determine a Poor Prognosis for Spinal Amyotrophic Lateral Sclerosis. Int. J. Mol. Sci., 23. · DOI
  53. Skillback, 2017, CSF/serum albumin ratio in dementias: A cross-sectional study on 1861 patients, Neurobiol. Aging, 59, 1, 10.1016/j.neurobiolaging.2017.06.028 · DOI
  54. Steinacker, 2019, CSF biomarkers of neuroinflammation in distinct forms and subtypes of neurodegenerative dementia, Alzheimer’s Res. Ther., 12, 2
  55. Vu, 2020, Cross-sectional and longitudinal measures of chitinase proteins in amyotrophic lateral sclerosis and expression of CHI3L1 in activated astrocytes, J. Neurol. Neurosurg. Psychiatry, 91, 350, 10.1136/jnnp-2019-321916 · DOI
  56. Woollacott, 2020, Cerebrospinal Fluid YKL-40 and Chitotriosidase Levels in Frontotemporal Dementia Vary by Clinical, Genetic and Pathological Subtype, Dement. Geriatr. Cogn. Disord., 49, 56, 10.1159/000506282 · DOI
  57. Falzone, 2022, Integrated evaluation of a panel of neurochemical biomarkers to optimize diagnosis and prognosis in amyotrophic lateral sclerosis, Eur. J. Neurol., 29, 1930, 10.1111/ene.15321 · DOI
  58. Verde, 2023, Serum levels of glial fibrillary acidic protein in patients with amyotrophic lateral sclerosis, Ann. Clin. Transl. Neurol., 10, 118, 10.1002/acn3.51708 · DOI
  59. Cousins, 2022, Distinguishing Frontotemporal Lobar Degeneration Tau From TDP-43 Using Plasma Biomarkers, JAMA Neurol., 79, 1155, 10.1001/jamaneurol.2022.3265 · DOI
  60. Ramirez, A.E., Gil-Jaramillo, N., Tapias, M.A., Gonzalez-Giraldo, Y., Pinzon, A., Puentes-Rozo, P.J., Aristizabal-Pachon, A.F., and Gonzalez, J. (2022). MicroRNA: A Linking between Astrocyte Dysfunction, Mild Cognitive Impairment, and Neurodegenerative Diseases. Life, 12. · DOI
  61. Rothhammer, 2016, Type I interferons and microbial metabolites of tryptophan modulate astrocyte activity and central nervous system inflammation via the aryl hydrocarbon receptor, Nat. Med., 22, 586, 10.1038/nm.4106 · DOI · Paper page
  62. Sanmarco, 2021, Gut-licensed IFNgamma(+) NK cells drive LAMP1(+)TRAIL(+) anti-inflammatory astrocytes, Nature, 590, 473, 10.1038/s41586-020-03116-4 · DOI · Paper page
  63. Margineanu, 2020, Gut microbiota modulates expression of genes involved in the astrocyte-neuron lactate shuttle in the hippocampus, Eur. Neuropsychopharmacol., 41, 152, 10.1016/j.euroneuro.2020.11.006 · DOI
  64. Kim, H.S., Son, J., Lee, D., Tsai, J., Wang, D., Chocron, E.S., Jeong, S., Kittrell, P., Murchison, C.F., and Kennedy, R.E. (2022). Gut- and oral-dysbiosis differentially impact spinal- and bulbar-onset ALS, predicting ALS severity and potentially determining the location of disease onset. BMC Neurol., 22. · DOI
  65. Todd, 2022, Modelling amyotrophic lateral sclerosis in rodents, Nat. Rev. Neurosci., 23, 231, 10.1038/s41583-022-00564-x · DOI
  66. Rosen, 1993, Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis, Nature, 362, 59, 10.1038/362059a0 · DOI · Paper page
  67. Gong, 2000, Restricted expression of G86R Cu/Zn superoxide dismutase in astrocytes results in astrocytosis but does not cause motoneuron degeneration, J. Neurosci., 20, 660, 10.1523/JNEUROSCI.20-02-00660.2000 · DOI
  68. Clement, 2003, Wild-type nonneuronal cells extend survival of SOD1 mutant motor neurons in ALS mice, Science, 302, 113, 10.1126/science.1086071 · DOI
  69. Papadeas, 2011, Astrocytes carrying the superoxide dismutase 1 (SOD1G93A) mutation induce wild-type motor neuron degeneration in vivo, Proc. Natl. Acad. Sci. USA, 108, 17803, 10.1073/pnas.1103141108 · DOI · Paper page
  70. Chen, 2015, Human-derived neural progenitors functionally replace astrocytes in adult mice, J. Clin. Investig., 125, 1033, 10.1172/JCI69097 · DOI
  71. Tong, 2013, Expression of ALS-linked TDP-43 mutant in astrocytes causes non-cell-autonomous motor neuron death in rats, EMBO J., 32, 1917, 10.1038/emboj.2013.122 · DOI
  72. Estes, 2013, Motor neurons and glia exhibit specific individualized responses to TDP-43 expression in a Drosophila model of amyotrophic lateral sclerosis, Dis. Model. Mech., 6, 721
  73. Yang, 2014, Partial loss of TDP-43 function causes phenotypes of amyotrophic lateral sclerosis, Proc. Natl. Acad. Sci. USA, 111, E1121
  74. Peng, 2020, Loss of TDP-43 in astrocytes leads to motor deficits by triggering A1-like reactive phenotype and triglial dysfunction, Proc. Natl. Acad. Sci. USA, 117, 29101, 10.1073/pnas.2007806117 · DOI
  75. Jensen, 2022, Targeting TNFalpha produced by astrocytes expressing amyotrophic lateral sclerosis-linked mutant fused in sarcoma prevents neurodegeneration and motor dysfunction in mice, Glia, 70, 1426, 10.1002/glia.24183 · DOI
  76. Lepore, 2008, Focal transplantation-based astrocyte replacement is neuroprotective in a model of motor neuron disease, Nat. Neurosci., 11, 1294, 10.1038/nn.2210 · DOI · Paper page
  77. Kondo, 2014, Focal transplantation of human iPSC-derived glial-rich neural progenitors improves lifespan of ALS mice, Stem Cell Rep., 3, 242, 10.1016/j.stemcr.2014.05.017 · DOI
  78. Izrael, 2018, Safety and efficacy of human embryonic stem cell-derived astrocytes following intrathecal transplantation in SOD1(G93A) and NSG animal models, Stem Cell Res. Ther., 9, 152, 10.1186/s13287-018-0890-5 · DOI
  79. Smethurst, 2020, Distinct responses of neurons and astrocytes to TDP-43 proteinopathy in amyotrophic lateral sclerosis, Brain, 143, 430, 10.1093/brain/awz419 · DOI
  80. Marchi, 2022, C9ORF72-derived poly-GA DPRs undergo endocytic uptake in iAstrocytes and spread to motor neurons, Life Sci. Alliance, 5, e202101276, 10.26508/lsa.202101276 · DOI
  81. Schmitz, 2021, Emerging Perspectives on Dipeptide Repeat Proteins in C9ORF72 ALS/FTD, Front. Cell. Neurosci., 15, 637548, 10.3389/fncel.2021.637548 · DOI
  82. Rossi, 2008, Focal degeneration of astrocytes in amyotrophic lateral sclerosis, Cell Death Differ., 15, 1691, 10.1038/cdd.2008.99 · DOI · Paper page
  83. Serio, 2013, Astrocyte pathology and the absence of non-cell autonomy in an induced pluripotent stem cell model of TDP-43 proteinopathy, Proc. Natl. Acad. Sci. USA, 110, 4697, 10.1073/pnas.1300398110 · DOI · Paper page
  84. Allen, 2019, Astrocyte adenosine deaminase loss increases motor neuron toxicity in amyotrophic lateral sclerosis, Brain, 142, 586, 10.1093/brain/awy353 · DOI
  85. Allen, 2019, C9orf72 expansion within astrocytes reduces metabolic flexibility in amyotrophic lateral sclerosis, Brain, 142, 3771, 10.1093/brain/awz302 · DOI
  86. Hallmann, 2017, Astrocyte pathology in a human neural stem cell model of frontotemporal dementia caused by mutant TAU protein, Sci. Rep., 7, 42991, 10.1038/srep42991 · DOI
  87. Mahali, 2021, Defective proteostasis in patient-derived iPSC-astrocytes and neurons carrying a MAPT IVS10+16 mutation, Alzheimer’s Dement., 17, e058727, 10.1002/alz.058727 · DOI
  88. Szebenyi, 2021, Human ALS/FTD brain organoid slice cultures display distinct early astrocyte and targetable neuronal pathology, Nat. Neurosci., 24, 1542, 10.1038/s41593-021-00923-4 · DOI
  89. Chandrasekaran, 2021, Astrocytic reactivity triggered by defective autophagy and metabolic failure causes neurotoxicity in frontotemporal dementia type 3, Stem Cell Rep., 16, 2736, 10.1016/j.stemcr.2021.09.013 · DOI
  90. Chen, 2012, Activation of the Wnt/beta-catenin signaling pathway is associated with glial proliferation in the adult spinal cord of ALS transgenic mice, Biochem. Biophys. Res. Commun., 420, 397, 10.1016/j.bbrc.2012.03.006 · DOI
  91. Lepore, 2008, Selective ablation of proliferating astrocytes does not affect disease outcome in either acute or chronic models of motor neuron degeneration, Exp. Neurol., 211, 423, 10.1016/j.expneurol.2008.02.020 · DOI
  92. Trias, 2011, Phenotypically aberrant astrocytes that promote motoneuron damage in a model of inherited amyotrophic lateral sclerosis, Proc. Natl. Acad. Sci. USA, 108, 18126, 10.1073/pnas.1110689108 · DOI
  93. Komine, 2018, Innate immune adaptor TRIF deficiency accelerates disease progression of ALS mice with accumulation of aberrantly activated astrocytes, Cell Death Differ., 25, 2130, 10.1038/s41418-018-0098-3 · DOI
  94. Vergouts, 2018, Constitutive downregulation protein kinase C epsilon in hSOD1(G93A) astrocytes influences mGluR5 signaling and the regulation of glutamate uptake, Glia, 66, 749, 10.1002/glia.23279 · DOI
  95. Almad, 2016, Connexin 43 in astrocytes contributes to motor neuron toxicity in amyotrophic lateral sclerosis, Glia, 64, 1154, 10.1002/glia.22989 · DOI
  96. Kawamata, 2014, Abnormal intracellular calcium signaling and SNARE-dependent exocytosis contributes to SOD1G93A astrocyte-mediated toxicity in amyotrophic lateral sclerosis, J. Neurosci., 34, 2331, 10.1523/JNEUROSCI.2689-13.2014 · DOI · Paper page
  97. Norante, R.P., Peggion, C., Rossi, D., Martorana, F., De Mario, A., Lia, A., Massimino, M.L., and Bertoli, A. (2019). ALS-Associated SOD1(G93A) Decreases SERCA Pump Levels and Increases Store-Operated Ca2+ Entry in Primary Spinal Cord Astrocytes from a Transgenic Mouse Model. Int. J. Mol. Sci., 20. · DOI
  98. Barbosa, M., Gomes, C., Sequeira, C., Gonçalves-Ribeiro, J., Pina, C.C., Carvalho, L.A., Moreira, R., Vaz, S.H., Vaz, A.R., and Brites, D. (2021). Recovery of Depleted miR-146a in ALS Cortical Astrocytes Reverts Cell Aberrancies and Prevents Paracrine Pathogenicity on Microglia and Motor Neurons. Front. Cell Dev. Biol., 9. · DOI
  99. Milosevic, 2016, The effect of amyotrophic lateral sclerosis-linked exogenous SOD1-G93A on electrophysiological properties and intracellular calcium in cultured rat astrocytes, Amyotroph Lateral Scler Front. Degener, 17, 443, 10.3109/21678421.2016.1143516 · DOI
  100. Lim, 2021, Ca(2+) handling at the mitochondria-ER contact sites in neurodegeneration, Cell Calcium., 98, 102453, 10.1016/j.ceca.2021.102453 · DOI
  101. Baker, 2015, Lysosomal and phagocytic activity is increased in astrocytes during disease progression in the SOD1 (G93A) mouse model of amyotrophic lateral sclerosis, Front. Cell Neurosci., 9, 410, 10.3389/fncel.2015.00410 · DOI
  102. Miller, 2018, Cortical astroglia undergo transcriptomic dysregulation in the G93A SOD1 ALS mouse model, J. Neurogenet., 32, 322, 10.1080/01677063.2018.1513508 · DOI
  103. Miller, 2017, Astroglial transcriptome dysregulation in early disease of an ALS mutant SOD1 mouse model, J. Neurogenet., 31, 37, 10.1080/01677063.2016.1260128 · DOI
  104. Liu, 2020, Single-cell RNA-seq analysis of the brainstem of mutant SOD1 mice reveals perturbed cell types and pathways of amyotrophic lateral sclerosis, Neurobiol. Dis., 141, 104877, 10.1016/j.nbd.2020.104877 · DOI
  105. Ferraiuolo, 2016, Oligodendrocytes contribute to motor neuron death in ALS via SOD1-dependent mechanism, Proc. Natl. Acad. Sci. USA, 113, E6496, 10.1073/pnas.1607496113 · DOI
  106. Taha, 2022, Astrocytes display cell autonomous and diverse early reactive states in familial amyotrophic lateral sclerosis, Brain, 145, 481, 10.1093/brain/awab328 · DOI
  107. Glasauer, 2022, Human tau mutations in cerebral organoids induce a progressive dyshomeostasis of cholesterol, Stem Cell Rep., 17, 2127, 10.1016/j.stemcr.2022.07.011 · DOI · Paper page
  108. Ziff, 2022, Meta-analysis of human and mouse ALS astrocytes reveals multi-omic signatures of inflammatory reactive states, Genome Res., 32, 71, 10.1101/gr.275939.121 · DOI
  109. Guttenplan, 2020, Knockout of reactive astrocyte activating factors slows disease progression in an ALS mouse model, Nat. Commun., 11, 3753, 10.1038/s41467-020-17514-9 · DOI · Paper page
  110. Mishra, 2020, Systematic elucidation of neuron-astrocyte interaction in models of amyotrophic lateral sclerosis using multi-modal integrated bioinformatics workflow, Nat. Commun., 11, 5579, 10.1038/s41467-020-19177-y · DOI
  111. Leng, 2022, CRISPRi screens in human iPSC-derived astrocytes elucidate regulators of distinct inflammatory reactive states, Nat. Neurosci., 25, 1528, 10.1038/s41593-022-01180-9 · DOI
  112. Tyzack, 2017, A neuroprotective astrocyte state is induced by neuronal signal EphB1 but fails in ALS models, Nat. Commun., 8, 1164, 10.1038/s41467-017-01283-z · DOI · Paper page
  113. Kim, 2022, Reactive astrocytes transduce inflammation in a blood-brain barrier model through a TNF-STAT3 signaling axis and secretion of alpha 1-antichymotrypsin, Nat. Commun., 13, 6581, 10.1038/s41467-022-34412-4 · DOI · Paper page
  114. Morales, 2022, Mlc1-Expressing Perivascular Astrocytes Promote Blood–Brain Barrier Integrity, J. Neurosci., 42, 1406, 10.1523/JNEUROSCI.1918-21.2021 · DOI
  115. Figueroa-Romero, C., Hur, J., Bender, D.E., Delaney, C.E., Cataldo, M.D., Smith, A.L., Yung, R., Ruden, D.M., Callaghan, B.C., and Feldman, E.L. (2012). Identification of Epigenetically Altered Genes in Sporadic Amyotrophic Lateral Sclerosis. PLoS ONE, 7. · DOI
  116. Brignone, 2019, Megalencephalic Leukoencephalopathy with Subcortical Cysts Protein-1 (MLC1) Counteracts Astrocyte Activation in Response to Inflammatory Signals, Mol. Neurobiol., 56, 8237, 10.1007/s12035-019-01657-y · DOI
  117. Lanciotti, A., Brignone, M.S., Belfiore, M., Columba-Cabezas, S., Mallozzi, C., Vincentini, O., Molinari, P., Petrucci, T.C., Visentin, S., and Ambrosini, E. (2020). Megalencephalic Leukoencephalopathy with Subcortical Cysts Disease-Linked MLC1 Protein Favors Gap-Junction Intercellular Communication by Regulating Connexin 43 Trafficking in Astrocytes. Cells, 9. · DOI
  118. Sun, 2015, Translational profiling identifies a cascade of damage initiated in motor neurons and spreading to glia in mutant SOD1-mediated ALS, Proc. Natl. Acad. Sci. USA, 112, E6993, 10.1073/pnas.1520639112 · DOI
  119. Stella, R., Bonadio, R.S., Cagnin, S., Massimino, M.L., Bertoli, A., and Peggion, C. (2021). Perturbations of the Proteome and of Secreted Metabolites in Primary Astrocytes from the hSOD1(G93A) ALS Mouse Model. Int. J. Mol. Sci., 22. · DOI
  120. Ferraiuolo, 2011, Dysregulation of astrocyte-motoneuron cross-talk in mutant superoxide dismutase 1-related amyotrophic lateral sclerosis, Brain, 134, 2627, 10.1093/brain/awr193 · DOI
  121. Mavel, 2017, Wildtype motoneurons, ALS-Linked SOD1 mutation and glutamate profoundly modify astrocyte metabolism and lactate shuttling, Glia, 65, 592, 10.1002/glia.23114 · DOI
  122. Egawa, 2022, TDP-43 regulates cholesterol biosynthesis by inhibiting sterol regulatory element-binding protein 2, Sci. Rep., 12, 7988, 10.1038/s41598-022-12133-4 · DOI
  123. Tortarolo, 2015, Lack of TNF-alpha receptor type 2 protects motor neurons in a cellular model of amyotrophic lateral sclerosis and in mutant SOD1 mice but does not affect disease progression, J. Neurochem., 135, 109, 10.1111/jnc.13154 · DOI
  124. Phatnani, 2013, Intricate interplay between astrocytes and motor neurons in ALS, Proc. Natl. Acad. Sci. USA, 110, E756, 10.1073/pnas.1222361110 · DOI
  125. Kia, 2018, Astrocytes expressing ALS-linked mutant FUS induce motor neuron death through release of tumor necrosis factor-alpha, Glia, 66, 1016, 10.1002/glia.23298 · DOI
  126. Carrasco, 2007, Non-cell autonomous effect of glia on motor neurons in an embryonic stem cell-based ALS model, Nat. Neurosci., 10, 608, 10.1038/nn1885 · DOI · Paper page
  127. Bilsland, 2008, Expression of mutant SOD1 in astrocytes induces functional deficits in motoneuron mitochondria, J. Neurochem., 107, 1271, 10.1111/j.1471-4159.2008.05699.x · DOI
  128. Provenzano, F., Nyberg, S., Giunti, D., Torazza, C., Parodi, B., Bonifacino, T., Usai, C., Kerlero de Rosbo, N., Milanese, M., and Uccelli, A. (2022). Micro-RNAs Shuttled by Extracellular Vesicles Secreted from Mesenchymal Stem Cells Dampen Astrocyte Pathological Activation and Support Neuroprotection in In-Vitro Models of ALS. Cells, 11. · DOI
  129. Re, 2014, Necroptosis drives motor neuron death in models of both sporadic and familial ALS, Neuron, 81, 1001, 10.1016/j.neuron.2014.01.011 · DOI
  130. Meyer, 2014, Direct conversion of patient fibroblasts demonstrates non-cell autonomous toxicity of astrocytes to motor neurons in familial and sporadic ALS, Proc. Natl. Acad. Sci. USA, 111, 829, 10.1073/pnas.1314085111 · DOI · Paper page
  131. Marchetto, 2008, Non-cell-autonomous effect of human SOD1 G37R astrocytes on motor neurons derived from human embryonic stem cells, Cell Stem Cell, 3, 649, 10.1016/j.stem.2008.10.001 · DOI · Paper page
  132. Boulting, 2008, Human embryonic stem cell-derived motor neurons are sensitive to the toxic effect of glial cells carrying an ALS-causing mutation, Cell Stem Cell, 3, 637, 10.1016/j.stem.2008.09.017 · DOI
  133. Song, 2016, Major histocompatibility complex class I molecules protect motor neurons from astrocyte-induced toxicity in amyotrophic lateral sclerosis, Nat. Med., 22, 397, 10.1038/nm.4052 · DOI
  134. Ikiz, 2015, The Regulatory Machinery of Neurodegeneration in In Vitro Models of Amyotrophic Lateral Sclerosis, Cell Rep., 12, 335, 10.1016/j.celrep.2015.06.019 · DOI
  135. Arredondo, 2022, Excessive release of inorganic polyphosphate by ALS/FTD astrocytes causes non-cell-autonomous toxicity to motoneurons, Neuron, 110, 1656, 10.1016/j.neuron.2022.02.010 · DOI
  136. Fritz, 2013, Mutant SOD1-expressing astrocytes release toxic factors that trigger motoneuron death by inducing hyperexcitability, J. Neurophysiol., 109, 2803, 10.1152/jn.00500.2012 · DOI
  137. Rojas, 2017, Chronic infusion of SOD1(G93A) astrocyte-secreted factors induces spinal motoneuron degeneration and neuromuscular dysfunction in healthy rats, J. Cell Physiol., 232, 2610, 10.1002/jcp.25827 · DOI
  138. Rojas, 2014, Astrocytes expressing mutant SOD1 and TDP43 trigger motoneuron death that is mediated via sodium channels and nitroxidative stress, Front. Cell Neurosci., 8, 24, 10.3389/fncel.2014.00024 · DOI
  139. Rojas, 2015, Reactive oxygen species trigger motoneuron death in non-cell-autonomous models of ALS through activation of c-Abl signaling, Front. Cell Neurosci., 9, 203, 10.3389/fncel.2015.00203 · DOI
  140. Lee, 2020, The overexpression of TDP-43 in astrocytes causes neurodegeneration via a PTP1B-mediated inflammatory response, J. Neuroinflamm., 17, 299, 10.1186/s12974-020-01963-6 · DOI
  141. Decker, 2016, The Tau/A152T mutation, a risk factor for frontotemporal-spectrum disorders, leads to NR2B receptor-mediated excitotoxicity, EMBO Rep., 17, 552, 10.15252/embr.201541439 · DOI
  142. Aldana, 2020, Glutamate-glutamine homeostasis is perturbed in neurons and astrocytes derived from patient iPSC models of frontotemporal dementia, Mol. Brain, 13, 125, 10.1186/s13041-020-00658-6 · DOI
  143. Dennys, 2022, CuATSM effectively ameliorates ALS patient astrocyte-mediated motor neuron toxicity in human in vitro models of amyotrophic lateral sclerosis, Glia, 71, 350, 10.1002/glia.24278 · DOI
  144. Gomes, C., Sequeira, C., Likhite, S., Dennys, C.N., Kolb, S.J., Shaw, P.J., Vaz, A.R., Kaspar, B.K., Meyer, K., and Brites, D. (2022). Neurotoxic Astrocytes Directly Converted from Sporadic and Familial ALS Patient Fibroblasts Reveal Signature Diversities and miR-146a Theragnostic Potential in Specific Subtypes. Cells, 11. · DOI
  145. Saba, 2014, MicroRNA-146a: A Dominant, Negative Regulator of the Innate Immune Response, Front. Immunol., 5, 578, 10.3389/fimmu.2014.00578 · DOI · Paper page
  146. Li, 2015, miR-494-3p Regulates Cellular Proliferation, Invasion, Migration, and Apoptosis by PTEN/AKT Signaling in Human Glioblastoma Cells, Cell. Mol. Neurobiol., 35, 679, 10.1007/s10571-015-0163-0 · DOI
  147. Yang, 2014, PTEN regulates AMPA receptor-mediated cell viability in iPS-derived motor neurons, Cell Death Dis., 5, e1096, 10.1038/cddis.2014.55 · DOI
  148. Zhang, 2019, miR-494-3p regulates lipopolysaccharide-induced inflammatory responses in RAW264.7 cells by targeting PTEN, Mol. Med. Rep., 19, 4288
  149. Guttenplan, 2021, Neurotoxic reactive astrocytes induce cell death via saturated lipids, Nature, 599, 102, 10.1038/s41586-021-03960-y · DOI · Paper page
  150. Raffaele, S., Boccazzi, M., and Fumagalli, M. (2021). Oligodendrocyte Dysfunction in Amyotrophic Lateral Sclerosis: Mechanisms and Therapeutic Perspectives. Cells, 10. · DOI
  151. Traiffort, E., Morisset-Lopez, S., Moussaed, M., and Zahaf, A. (2021). Defective Oligodendroglial Lineage and Demyelination in Amyotrophic Lateral Sclerosis. Int. J. Mol. Sci., 22. · DOI
  152. Valori, 2021, Contribution of RNA/DNA Binding Protein Dysfunction in Oligodendrocytes in the Pathogenesis of the Amyotrophic Lateral Sclerosis/Frontotemporal Lobar Degeneration Spectrum Diseases, Front Neurosci., 15, 724891, 10.3389/fnins.2021.724891 · DOI
  153. Rodrigues, 2012, Impaired blood-brain/spinal cord barrier in ALS patients, Brain Res., 1469, 114, 10.1016/j.brainres.2012.05.056 · DOI
  154. Garbuzova-Davis, S., Saporta, S., Haller, E., Kolomey, I., Bennett, S.P., Potter, H., and Sanberg, P.R. (2007). Evidence of compromised blood-spinal cord barrier in early and late symptomatic SOD1 mice modeling ALS. PLoS ONE, 2. · DOI
  155. Haller, 2007, Ultrastructure of blood-brain barrier and blood-spinal cord barrier in SOD1 mice modeling ALS, Brain Res., 1157, 126, 10.1016/j.brainres.2007.04.044 · DOI · Paper page
  156. Milane, 2010, P-glycoprotein expression and function are increased in an animal model of amyotrophic lateral sclerosis, Neurosci. Lett., 472, 166, 10.1016/j.neulet.2010.01.078 · DOI
  157. Stamenkovic, 2017, In vivo EPR pharmacokinetic evaluation of the redox status and the blood brain barrier permeability in the SOD1(G93A) ALS rat model, Free Radic. Biol. Med., 108, 258, 10.1016/j.freeradbiomed.2017.03.034 · DOI
  158. Nicaise, 2009, Impaired blood-brain and blood-spinal cord barriers in mutant SOD1-linked ALS rat, Brain Res., 1301, 152, 10.1016/j.brainres.2009.09.018 · DOI · Paper page
  159. Zamudio, 2020, TDP-43 mediated blood-brain barrier permeability and leukocyte infiltration promote neurodegeneration in a low-grade systemic inflammation mouse model, J. Neuroinflamm., 17, 283, 10.1186/s12974-020-01952-9 · DOI
  160. Jablonski, 2012, Selective increase of two ABC drug efflux transporters at the blood-spinal cord barrier suggests induced pharmacoresistance in ALS, Neurobiol. Dis., 47, 194, 10.1016/j.nbd.2012.03.040 · DOI
  161. Mohamed, 2019, Excess glutamate secreted from astrocytes drives upregulation of P-glycoprotein in endothelial cells in amyotrophic lateral sclerosis, Exp. Neurol., 316, 27, 10.1016/j.expneurol.2019.04.002 · DOI
  162. Qosa, 2016, Astrocytes drive upregulation of the multidrug resistance transporter ABCB1 (P-Glycoprotein) in endothelial cells of the blood–brain barrier in mutant superoxide dismutase 1-linked amyotrophic lateral sclerosis, Glia, 64, 1298, 10.1002/glia.23003 · DOI
  163. Moriwaki, 2018, Dissociation of blood-brain barrier disruption and disease manifestation in an aquaporin-4-deficient mouse model of amyotrophic lateral sclerosis, Neurosci. Res., 133, 48, 10.1016/j.neures.2017.11.001 · DOI
  164. Nicaise, 2009, Aquaporin-4 overexpression in rat ALS model, Anat. Rec. (Hoboken), 292, 207, 10.1002/ar.20838 · DOI
  165. Khalfallah, 2018, TDP-43 regulation of stress granule dynamics in neurodegenerative disease-relevant cell types, Sci. Rep., 8, 7551, 10.1038/s41598-018-25767-0 · DOI
  166. Dai, 2017, Alterations in AQP4 expression and polarization in the course of motor neuron degeneration in SOD1G93A mice, Mol. Med. Rep., 16, 1739, 10.3892/mmr.2017.6786 · DOI
  167. Bataveljic, 2012, Changes in the astrocytic aquaporin-4 and inwardly rectifying potassium channel expression in the brain of the amyotrophic lateral sclerosis SOD1(G93A) rat model, Glia, 60, 1991, 10.1002/glia.22414 · DOI
  168. Mader, S., and Brimberg, L. (2019). Aquaporin-4 Water Channel in the Brain and Its Implication for Health and Disease. Cells, 8. · DOI
  169. Thomsen, 2018, Transplantation of Neural Progenitor Cells Expressing Glial Cell Line-Derived Neurotrophic Factor into the Motor Cortex as a Strategy to Treat Amyotrophic Lateral Sclerosis, Stem Cells, 36, 1122, 10.1002/stem.2825 · DOI
  170. Brambilla, 2016, Disruption of the astrocytic TNFR1-GDNF axis accelerates motor neuron degeneration and disease progression in amyotrophic lateral sclerosis, Hum. Mol. Genet., 25, 3080
  171. Baloh, 2022, Transplantation of human neural progenitor cells secreting GDNF into the spinal cord of patients with ALS: A phase 1/2a trial, Nat. Med., 28, 1813, 10.1038/s41591-022-01956-3 · DOI
  172. Wang, 2011, Astrocyte loss of mutant SOD1 delays ALS disease onset and progression in G85R transgenic mice, Hum. Mol. Genet., 20, 286, 10.1093/hmg/ddq463 · DOI
  173. Foust, 2013, Therapeutic AAV9-mediated suppression of mutant SOD1 slows disease progression and extends survival in models of inherited ALS, Mol. Ther., 21, 2148, 10.1038/mt.2013.211 · DOI
  174. Rochat, 2022, Astrocyte-targeting RNA interference against mutated superoxide dismutase 1 induces motoneuron plasticity and protects fast-fatigable motor units in a mouse model of amyotrophic lateral sclerosis, Glia, 70, 842, 10.1002/glia.24140 · DOI
  175. Fang, T., Je, G., Pacut, P., Keyhanian, K., Gao, J., and Ghasemi, M. (2022). Gene Therapy in Amyotrophic Lateral Sclerosis. Cells, 11. · DOI
  176. Cudkowicz, 2014, Safety and efficacy of ceftriaxone for amyotrophic lateral sclerosis: A multi-stage, randomised, double-blind, placebo-controlled trial, Lancet Neurol., 13, 1083, 10.1016/S1474-4422(14)70222-4 · DOI
  177. Abulseoud, O.A., Alasmari, F., Hussein, A.M., and Sari, Y. (2022). Ceftriaxone as a Novel Therapeutic Agent for Hyperglutamatergic States: Bridging the Gap Between Preclinical Results and Clinical Translation. Front. Neurosci., 16. · DOI
  178. Ferraiuolo, 2021, NRF2 as a therapeutic opportunity to impact in the molecular roadmap of ALS, Free Radic. Biol. Med., 173, 125, 10.1016/j.freeradbiomed.2021.07.022 · DOI
  179. Sarlette, 2008, Nuclear erythroid 2-related factor 2-antioxidative response element signaling pathway in motor cortex and spinal cord in amyotrophic lateral sclerosis, J. Neuropathol. Exp. Neurol., 67, 1055, 10.1097/NEN.0b013e31818b4906 · DOI
  180. Bakkar, 2015, RBM45 Modulates the Antioxidant Response in Amyotrophic Lateral Sclerosis through Interactions with KEAP1, Mol. Cell Biol., 35, 2385, 10.1128/MCB.00087-15 · DOI
  181. Cassina, 2008, Mitochondrial dysfunction in SOD1G93A-bearing astrocytes promotes motor neuron degeneration: Prevention by mitochondrial-targeted antioxidants, J. Neurosci., 28, 4115, 10.1523/JNEUROSCI.5308-07.2008 · DOI
  182. Duan, 2010, Mutant TAR DNA-binding protein-43 induces oxidative injury in motor neuron-like cell, Neuroscience, 169, 1621, 10.1016/j.neuroscience.2010.06.018 · DOI
  183. Goode, 2016, ALS-FTLD associated mutations of SQSTM1 impact on Keap1-Nrf2 signalling, Mol Cell Neurosci., 76, 52, 10.1016/j.mcn.2016.08.004 · DOI
  184. Moujalled, 2017, TDP-43 mutations causing amyotrophic lateral sclerosis are associated with altered expression of RNA-binding protein hnRNP K and affect the Nrf2 antioxidant pathway, Hum. Mol. Genet., 26, 1732, 10.1093/hmg/ddx093 · DOI
  185. Mimoto, 2012, Impaired antioxydative Keap1/Nrf2 system and the downstream stress protein responses in the motor neuron of ALS model mice, Brain Res., 1446, 109, 10.1016/j.brainres.2011.12.064 · DOI
  186. Pehar, 2007, Mitochondrial superoxide production and nuclear factor erythroid 2-related factor 2 activation in p75 neurotrophin receptor-induced motor neuron apoptosis, J. Neurosci., 27, 7777, 10.1523/JNEUROSCI.0823-07.2007 · DOI
  187. Tian, Y.P., Che, F.Y., Su, Q.P., Lu, Y.C., You, C.P., Huang, L.M., Wang, S.G., Wang, L., and Yu, J.X. (2017). Effects of mutant TDP-43 on the Nrf2/ARE pathway and protein expression of MafK and JDP2 in NSC-34 cells. Genet. Mol. Res., 16. · DOI
  188. Wang, 2014, Effect of the human SOD1-G93A gene on the Nrf2/ARE signaling pathway in NSC-34 cells, Mol. Med. Rep., 9, 2453, 10.3892/mmr.2014.2087 · DOI
  189. Foster, 2020, ALS-associated TBK1 variant p.G175S is defective in phosphorylation of p62 and impacts TBK1-mediated signalling and TDP-43 autophagic degradation, Mol. Cell Neurosci., 108, 103539, 10.1016/j.mcn.2020.103539 · DOI
  190. Miquel, 2016, Electrophilic nitro-fatty acids prevent astrocyte-mediated toxicity to motor neurons in a cell model of familial amyotrophic lateral sclerosis via nuclear factor erythroid 2-related factor activation, Free Radic. Biol. Med., 95, 112, 10.1016/j.freeradbiomed.2016.03.013 · DOI
  191. Vargas, 2006, Increased glutathione biosynthesis by Nrf2 activation in astrocytes prevents p75NTR-dependent motor neuron apoptosis, J. Neurochem., 97, 687, 10.1111/j.1471-4159.2006.03742.x · DOI
  192. Vargas, 2005, Fibroblast growth factor-1 induces heme oxygenase-1 via nuclear factor erythroid 2-related factor 2 (Nrf2) in spinal cord astrocytes: Consequences for motor neuron survival, J. Biol. Chem., 280, 25571, 10.1074/jbc.M501920200 · DOI
  193. Vargas, 2008, Nrf2 activation in astrocytes protects against neurodegeneration in mouse models of familial amyotrophic lateral sclerosis, J. Neurosci., 28, 13574, 10.1523/JNEUROSCI.4099-08.2008 · DOI · Paper page
  194. Valori, C.F., Possenti, A., Brambilla, L., and Rossi, D. (2021). Challenges and Opportunities of Targeting Astrocytes to Halt Neurodegenerative Disorders. Cells, 10. · DOI
  195. Ashrafizadeh, 2020, Curcumin Activates the Nrf2 Pathway and Induces Cellular Protection Against Oxidative Injury, Curr. Mol. Med., 20, 116
  196. Mohorko, 2010, Curcumin Labeling of Neuronal Fibrillar Tau Inclusions in Human Brain Samples, J. Neuropathol. Exp. Neurol., 69, 405, 10.1097/NEN.0b013e3181d709eb · DOI
  197. Nicholson, 2018, Pilot trial of inosine to elevate urate levels in amyotrophic lateral sclerosis, Ann. Clin. Transl. Neurol., 5, 1522, 10.1002/acn3.671 · DOI
  198. Zhang, 2018, Serum uric acid levels in patients with amyotrophic lateral sclerosis: A meta-analysis, Sci. Rep., 8, 1100, 10.1038/s41598-018-19609-2 · DOI
  199. Williams, 2016, Copper delivery to the CNS by CuATSM effectively treats motor neuron disease in SODG93A mice co-expressing the Copper-Chaperone-for-SOD, Neurobiol. Dis., 89, 1, 10.1016/j.nbd.2016.01.020 · DOI · Paper page
  200. Vieira, 2017, CuATSM efficacy is independently replicated in a SOD1 mouse model of ALS while unmetallated ATSM therapy fails to reveal benefits, IBRO Rep., 2, 47, 10.1016/j.ibror.2017.03.001 · DOI

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Metadata

Authors
Valori, C. F., Sulmona, C., Brambilla, L., & Rossi, D.
Affiliations
  • Molecular Neuropathology of Neurodegenerative Diseases, German Centre for Neurodegenerative Diseases (DZNE), 72072 Tübingen, Germany
  • Laboratory for Research on Neurodegenerative Disorders, Istituti Clinici Scientifici Maugeri IRCCS, 27100 Pavia, Italy
ORCID
Venue
Cells
Publisher
MDPI AG
Published
2023-05-23
Volume
12
Issue
11
Pages
1450
ISSN
2073-4409
DOI
10.3390/cells12111450
PMC
PMC10252425
Cited by
30
References
22
Language
en
Licence
creativecommons.org/licenses/by/4.0/ (vor)
Funders
  • AFM-Téléthon (#16177, #18221, #21565) (JPND2022-DC4MND)
  • Italian Ministry of Health (JPND2022-DC4MND)

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