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Chapter 13 - Neuropathology offrontotemporal dementia and related disorders

from Section 4 - Pathology and pathophysiology

Published online by Cambridge University Press:  05 May 2016

Bradford C. Dickerson
Affiliation:
Department of Neurology, Massachusetts General Hospital
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Publisher: Cambridge University Press
Print publication year: 2016

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References

Rademakers, R, Neumann, M, Mackenzie, IR. Advances in understanding the molecular basis of frontotemporal dementia. Nat Rev Neurol 2012;8:423–34.CrossRefGoogle ScholarPubMed
Mackenzie, IR, Neumann, M, Bigio, EH, et al. Nomenclature for neuropathologic subtypes of frontotemporal lobar degeneration: consensus recommendations. Acta Neuropathol 2009;117:1518.CrossRefGoogle ScholarPubMed
Mackenzie, IR, Neumann, M, Bigio, EH, et al. Nomenclature and nosology for neuropathologic subtypes of frontotemporal lobar degeneration: an update. Acta Neuropathol 2010;119:14.Google Scholar
Weingarten, MD, Lockwood, AH, Hwo, SY, et al. A protein factor essential for microtubule assembly. Proc Natl Acad Sci USA 1975;72:1858–62.Google Scholar
Goedert, M, Spillantini, MG, Jakes, R, et al. Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease. Neuron 1989;3:519–26.Google Scholar
Spillantini, MG, Goedert, M. Tau pathology and neurodegeneration. Lancet Neurol 2013;12:609–22.Google Scholar
Lee, G, Leugers, CJ. Tau and tauopathies. Prog Mol Biol Transl Sci 2012;107:263–93.Google Scholar
Iqbal, K, Liu, F, Gong, CX, et al. Mechanisms of tau-induced neurodegeneration. Acta Neuropathol 2009;118:5369.CrossRefGoogle ScholarPubMed
Noble, W, Hanger, DP, Miller, CC, et al. The importance of tau phosphorylation for neurodegenerative diseases. Front Neurol 2013;4:83.CrossRefGoogle ScholarPubMed
van Swieten, J, Spillantini, MG. Hereditary frontotemporal dementia caused by tau gene mutations. Brain Pathol 2007;17:6373.CrossRefGoogle ScholarPubMed
Dickson, DW, Rademakers, R, Hutton, ML. Progressive supranuclear palsy: pathology and genetics. Brain Pathol 2007;17:7482.CrossRefGoogle ScholarPubMed
Myers, AJ, Pittman, AM, Zhao, AS, et al. The MAPT H1c risk haplotype is associated with increased expression of tau and especially of 4 repeat containing transcripts. Neurobiol Dis 2007;25:561–70.Google Scholar
Kovacs, GG, Rozemuller, AJ, van Swieten, JC, et al. Neuropathology of the hippocampus in FTLD-tau with Pick bodies: a study of the BrainNet Europe Consortium. Neuropathol Appl Neurobiol 2013;39:166–78.CrossRefGoogle ScholarPubMed
Dickson, DW, Ahmed, Z, Algom, AA, et al. Neuropathology of variants of progressive supranuclear palsy. Curr Opin Neurol 2010;23:394400.Google Scholar
Dickson, DW. Neuropathologic differentiation of progressive supranuclear palsy and corticobasal degeneration. J Neurol 1999;246 Suppl 2:11615.Google Scholar
Kouri, N, Whitwell, JL, Josephs, KA, et al. Corticobasal degeneration: a pathologically distinct 4R tauopathy. Nat Rev Neurol 2011;7:263–72.Google Scholar
Ahmed, Z, Bigio, EH, Budka, H, et al. Globular glial tauopathies (GGT): consensus recommendations. Acta Neuropathol 2013;126:537–44.Google Scholar
Ghetti, B, Wszolek, ZK, Boeve, BF, et al. Frontotemporal dementia and parkinsonism linked to chromosome 17. In: Dickson, DW, Weller, RO, eds. Neurodegeneration: The Molecular Pathology of Dementia and Movement Disorders. Chichester, UK: Blackwell Publishing Ltd.; 2011; 110–34.Google Scholar
Miki, Y, Mori, F, Hori, E, et al. Hippocampal sclerosis with four-repeat tau-positive round inclusions in the dentate gyrus: a new type of four-repeat tauopathy. Acta Neuropathol 2009;117:713–18.Google Scholar
Kovacs, GG, Milenkovic, I, Wohrer, A, et al. Non-Alzheimer neurodegenerative pathologies and their combinations are more frequent than commonly believed in the elderly brain: a community-based autopsy series. Acta Neuropathol 2013;126:365–84.CrossRefGoogle Scholar
Tolnay, M, Probst, A. Argyrophilic grain disease. Handb Clin Neurol 2008;89:553–63.CrossRefGoogle ScholarPubMed
Saito, Y, Ruberu, NN, Sawabe, M, et al. Staging of argyrophilic grains: an age-associated tauopathy. J Neuropathol Exp Neurol 2004;63:911–18.Google Scholar
Jellinger, KA, Attems, J. Neurofibrillary tangle-predominant dementia: comparison with classical Alzheimer disease. Acta Neuropathol 2007;113:107–17.Google Scholar
Frank, S, Clavaguera, F, Tolnay, M. Tauopathy models and human neuropathology: similarities and differences. Acta Neuropathol 2008;115:3953.CrossRefGoogle ScholarPubMed
Clavaguera, F, Akatsu, H, Fraser, G, et al. Brain homogenates from human tauopathies induce tau inclusions in mouse brain. Proc Natl Acad Sci USA 2013;110:9535–40.Google Scholar
Halliday, G, Bigio, EH, Cairns, NJ, et al. Mechanisms of disease in frontotemporal lobar degeneration: gain of function versus loss of function effects. Acta Neuropathol 2012;124:373–82.CrossRefGoogle ScholarPubMed
Neumann, M, Sampathu, DM, Kwong, LK, et al. Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Science 2006;314:130–3.Google Scholar
Buratti, E, Baralle, FE. The multiple roles of TDP-43 in pre-mRNA processing and gene expression regulation. RNA Biol 2010;7:420–9.CrossRefGoogle ScholarPubMed
Mackenzie, IR, Rademakers, R, Neumann, M. TDP-43 and FUS in amyotrophic lateral sclerosis and frontotemporal dementia. Lancet Neurol 2010;9:9951007.CrossRefGoogle ScholarPubMed
Neumann, M, Kwong, LK, Lee, EB, et al. Phosphorylation of S409/410 of TDP-43 is a consistent feature in all sporadic and familial forms of TDP-43 proteinopathies. Acta Neuropathol 2009;117:137–49.Google Scholar
Igaz, LM, Kwong, LK, Xu, Y, et al. Enrichment of C-terminal fragments in TAR DNA-binding protein-43 cytoplasmic inclusions in brain but not in spinal cord of frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Am J Pathol 2008;173:182–94.Google Scholar
Sampathu, DM, Neumann, M, Kwong, LK, et al. Pathological heterogeneity of frontotemporal lobar degeneration with ubiquitin-positive inclusions delineated by ubiquitin immunohistochemistry and novel monoclonal antibodies. Am J Pathol 2006;169:1343–52.CrossRefGoogle ScholarPubMed
Mackenzie, IR, Baborie, A, Pickering-Brown, S, et al. Heterogeneity of ubiquitin pathology in frontotemporal lobar degeneration: classification and relation to clinical phenotype. Acta Neuropathol 2006;112:539–49.CrossRefGoogle ScholarPubMed
Cairns, NJ, Neumann, M, Bigio, EH, et al. TDP-43 in familial and sporadic frontotemporal lobar degeneration with ubiquitin inclusions. Am J Pathol 2007;171:227–40.Google Scholar
Neumann, M, Mackenzie, IR, Cairns, NJ, et al. TDP-43 in the ubiquitin pathology of frontotemporal dementia with VCP gene mutations. J Neuropathol Exp Neurol 2007;66:152–7.Google Scholar
Mackenzie, IR, Neumann, M, Baborie, A, et al. A harmonized classification system for FTLD-TDP pathology. Acta Neuropathol 2011;122:111–13.Google Scholar
Baker, M, Mackenzie, IR, Pickering-Brown, SM, et al. Mutations in progranulin cause tau-negative frontotemporal dementia linked to chromosome 17. Nature 2006;442:916–19.Google Scholar
Cruts, M, Gijselinck, I, van der Zee, J, et al. Null mutations in progranulin cause ubiquitin-positive frontotemporal dementia linked to chromosome 17q21. Nature 2006;442:920–4.Google Scholar
Mackenzie, IR, Baker, M, Pickering-Brown, S, et al. The neuropathology of frontotemporal lobar degeneration caused by mutations in the progranulin gene. Brain 2006;129:3081–90.CrossRefGoogle ScholarPubMed
DeJesus-Hernandez, M, Mackenzie, IR, Boeve, BF, et al. Expanded GGGGCC hexanucleotide repeat in noncoding region of C9ORF72 causes chromosome 9p-linked FTD and ALS. Neuron 2011;72:245–56.CrossRefGoogle ScholarPubMed
Renton, AE, Majounie, E, Waite, A, et al. A hexanucleotide repeat expansion in C9ORF72 is the cause of chromosome 9p21-linked ALS-FTD. Neuron 2011;72:257–68.Google Scholar
Hsiung, GY, DeJesus-Hernandez, M, Feldman, HH, et al. Clinical and pathological features of familial frontotemporal dementia caused by C9ORF72 mutation on chromosome 9p. Brain 2012;135:709–22.Google Scholar
Mori, K, Weng, SM, Arzberger, T, et al. The C9orf72 GGGGCC repeat is translated into aggregating dipeptide-repeat proteins in FTLD/ALS. Science 2013;339:1335–8.Google Scholar
Ash, PE, Bieniek, KF, Gendron, TF, et al. Unconventional translation of C9ORF72 GGGGCC expansion generates insoluble polypeptides specific to c9FTD/ALS. Neuron 2013;77:639–46.Google Scholar
Mackenzie, IR, Arzberger, T, Kremmer, E, et al. Dipeptide repeat protein pathology in C9ORF72 mutation cases: clinico-pathological correlations. Acta Neuropathol 2013;126:859–79.Google Scholar
Kimonis, VE, Fulchiero, E, Vesa, J, et al. VCP disease associated with myopathy, Paget disease of bone and frontotemporal dementia: review of a unique disorder. Biochim Biophys Acta 2008;1782:744–8.Google ScholarPubMed
Borroni, B, Bonvicini, C, Alberici, A, et al. Mutation within TARDBP leads to frontotemporal dementia without motor neuron disease. Hum Mutat 2009;30:E974–83.Google Scholar
Benajiba, L, Le Ber, I, Camuzat, A, et al. TARDBP mutations in motoneuron disease with frontotemporal lobar degeneration. Ann Neurol 2009;65:470–3.Google Scholar
Kovacs, GG, Murrell, JR, Horvath, S, et al. TARDBP variation associated with frontotemporal dementia, supranuclear gaze palsy, and chorea. Mov Disord 2009;24:1843–7.Google Scholar
Lee, EB, Lee, VM, Trojanowski, JQ. Gains or losses: molecular mechanisms of TDP43-mediated neurodegeneration. Nat Rev Neurosci 2012;13:3850.Google Scholar
Da Cruz, S, Cleveland, DW. Understanding the role of TDP-43 and FUS/TLS in ALS and beyond. Curr Opin Neurobiol 2011;21:904–19.Google Scholar
Wu, LS, Cheng, WC, Shen, CK. Targeted depletion of TDP-43 expression in the spinal cord motor neurons leads to the development of amyotrophic lateral sclerosis-like phenotypes in mice. J Biol Chem 2012;287:27335–44.Google Scholar
Neumann, M, Rademakers, R, Roeber, S, et al. A new subtype of frontotemporal lobar degeneration with FUS pathology. Brain 2009;132:2922–31.Google Scholar
Kwiatkowski, TJ Jr., Bosco, DA, Leclerc, AL, et al. Mutations in the FUS/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosis. Science 2009;323:1205–8.Google Scholar
Vance, C, Rogelj, B, Hortobagyi, T, et al. Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosis type 6. Science 2009;323:1208–11.Google Scholar
Neumann, M, Roeber, S, Kretzschmar, HA, et al. Abundant FUS-immunoreactive pathology in neuronal intermediate filament inclusion disease. Acta Neuropathol 2009;118:605–16.Google Scholar
Munoz, DG, Neumann, M, Kusaka, H, et al. FUS pathology in basophilic inclusion body disease. Acta Neuropathol 2009;118:617–27.Google Scholar
Neumann, M, Bentmann, E, Dormann, D, et al. FET proteins TAF15 and EWS are selective markers that distinguish FTLD with FUS pathology from amyotrophic lateral sclerosis with FUS mutations. Brain 2011;134:2595–609.Google Scholar
Neumann, M, Valori, CF, Ansorge, O, et al. Transportin 1 accumulates specifically with FET proteins but no other transportin cargos in FTLD-FUS and is absent in FUS inclusions in ALS with FUS mutations. Acta Neuropathol 2012;124:705–16.CrossRefGoogle ScholarPubMed
Tan, AY, Manley, JL. The TET family of proteins: functions and roles in disease. J Mol Cell Biol 2009;1:8292.CrossRefGoogle ScholarPubMed
Kovar, H. Jekyll, Dr. and Mr. Hyde: the two faces of the FUS/EWS/TAF15 protein family. Sarcoma 2011;2011:837474.Google Scholar
Fujii, R, Takumi, T. TLS facilitates transport of mRNA encoding an actin-stabilizing protein to dendritic spines. J Cell Sci 2005;118:5755–65.Google Scholar
Dormann, D, Madl, T, Valori, CF, et al. Arginine methylation next to the PY-NLS modulates transportin binding and nuclear import of FUS. EMBO J 2012;31:4258–75.Google Scholar
Cairns, NJ, Grossman, M, Arnold, SE, et al. Clinical and neuropathologic variation in neuronal intermediate filament inclusion disease. Neurology 2004;63:1376–84.Google Scholar
Mackenzie, IR, Foti, D, Woulfe, J, et al. Atypical frontotemporal lobar degeneration with ubiquitin-positive, TDP-43-negative neuronal inclusions. Brain 2008;131:1282–93.Google Scholar
Mackenzie, IR, Munoz, DG, Kusaka, H, et al. Distinct pathological subtypes of FTLD-FUS. Acta Neuropathol 2011;121:207–18.CrossRefGoogle ScholarPubMed
Mackenzie, IR, Feldman, H. Neurofilament inclusion body disease with early onset frontotemporal dementia and primary lateral sclerosis. Clin Neuropathol 2004;23:183–93.Google Scholar
Dormann, D, Rodde, R, Edbauer, D, et al. ALS-associated fused in sarcoma (FUS) mutations disrupt transportin-mediated nuclear import. EMBO J 2010;29:2841–57.Google Scholar
Ravenscroft, TA, Baker, MC, Rutherford, NJ, et al. Mutations in protein N-arginine methyltransferases are not the cause of FTLD-FUS. Neurobiol Aging 2013;34:2235.e11–13.Google Scholar
Holm, IE, Englund, E, Mackenzie, IR, et al. A reassessment of the neuropathology of frontotemporal dementia linked to chromosome 3. J Neuropathol Exp Neurol 2007;66:884–91.Google Scholar
Holm, IE, Isaacs, AM, Mackenzie, IR. Absence of FUS-immunoreactive pathology in frontotemporal dementia linked to chromosome 3 (FTD-3) caused by mutation in the CHMP2B gene. Acta Neuropathol 2009;118:719–20.Google Scholar
Wider, C, Van Gerpen, JA, DeArmond, S, et al. Leukoencephalopathy with spheroids (HDLS) and pigmentary leukodystrophy (POLD): a single entity? Neurology 2009;72:1953–9.Google Scholar
Forman, MS, Farmer, J, Johnson, JK, et al. Frontotemporal dementia: clinicopathological correlations. Ann Neurol 2006;59:952–62.Google Scholar
Munoz, DG, Woulfe, J, Kertesz, A. Argyrophilic thorny astrocyte clusters in association with Alzheimer's disease pathology in possible primary progressive aphasia. Acta Neuropathol 2007;114:347–57.Google Scholar
Josephs, KA, Hodges, JR, Snowden, JS, et al. Neuropathological background of phenotypical variability in frontotemporal dementia. Acta Neuropathol 2011;122:137–53.Google Scholar

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