Database : MEDLINE
Search on : frontotemporal and dementia [Words]
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[PMID]: 29462608
[Au] Autor:Khalil B; Morderer D; Price PL; Liu F; Rossoll W
[Ad] Address:Department of Neuroscience, Mayo Clinic, Jacksonville, FL 32224 USA.
[Ti] Title:mRNP assembly, axonal transport, and local translation in neurodegenerative diseases.
[So] Source:Brain Res;, 2018 Feb 17.
[Is] ISSN:1872-6240
[Cp] Country of publication:Netherlands
[La] Language:eng
[Ab] Abstract:The development, maturation, and maintenance of the mammalian nervous system rely on complex spatiotemporal patterns of gene expression. In neurons, this is achieved by the expression of differentially localized isoforms and specific sets of mRNA-binding proteins (mRBPs) that regulate RNA processing, mRNA trafficking, and local protein synthesis at remote sites within dendrites and axons. There is growing evidence that axons contain a specialized transcriptome and are endowed with the machinery that allows them to rapidly alter their local proteome via local translation and protein degradation. This enables axons to quickly respond to changes in their environment during development, and to facilitate axon regeneration and maintenance in adult organisms. Aside from providing autonomy to neuronal processes, local translation allows axons to send retrograde injury signals to the cell soma. In this review, we discuss evidence that disturbances in mRNP transport, granule assembly, axonal localization, and local translation contribute to pathology in various neurodegenerative diseases, including spinal muscular atrophy (SMA), amyotrophic lateral sclerosis (ALS), frontotemporal dementia (FTD), and Alzheimer's disease (AD).
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1802
[Cu] Class update date: 180311
[Lr] Last revision date:180311
[St] Status:Publisher

  2 / 7515 MEDLINE  
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[PMID]: 29400714
[Au] Autor:Shi Y; Lin S; Staats KA; Li Y; Chang WH; Hung ST; Hendricks E; Linares GR; Wang Y; Son EY; Wen X; Kisler K; Wilkinson B; Menendez L; Sugawara T; Woolwine P; Huang M; Cowan MJ; Ge B; Koutsodendris N; Sandor KP; Komberg J; Vangoor VR; Senthilkumar K; Hennes V; Seah C; Nelson AR; Cheng TY; Lee SJ; August PR; Chen JA; Wisniewski N; Hanson-Smith V; Belgard TG; Zhang A; Coba M; Grunseich C; Ward ME; van den Berg LH; Pasterkamp RJ; Trotti D; Zlokovic BV; Ichida JK
[Ad] Address:Department of Stem Cell Biology and Regenerative Medicine, Keck School of Medicine, University of Southern California, Los Angeles, California, USA.
[Ti] Title:Haploinsufficiency leads to neurodegeneration in C9ORF72 ALS/FTD human induced motor neurons.
[So] Source:Nat Med;24(3):313-325, 2018 Mar.
[Is] ISSN:1546-170X
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:An intronic GGGGCC repeat expansion in C9ORF72 is the most common cause of amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD), but the pathogenic mechanism of this repeat remains unclear. Using human induced motor neurons (iMNs), we found that repeat-expanded C9ORF72 was haploinsufficient in ALS. We found that C9ORF72 interacted with endosomes and was required for normal vesicle trafficking and lysosomal biogenesis in motor neurons. Repeat expansion reduced C9ORF72 expression, triggering neurodegeneration through two mechanisms: accumulation of glutamate receptors, leading to excitotoxicity, and impaired clearance of neurotoxic dipeptide repeat proteins derived from the repeat expansion. Thus, cooperativity between gain- and loss-of-function mechanisms led to neurodegeneration. Restoring C9ORF72 levels or augmenting its function with constitutively active RAB5 or chemical modulators of RAB5 effectors rescued patient neuron survival and ameliorated neurodegenerative processes in both gain- and loss-of-function C9ORF72 mouse models. Thus, modulating vesicle trafficking was able to rescue neurodegeneration caused by the C9ORF72 repeat expansion. Coupled with rare mutations in ALS2, FIG4, CHMP2B, OPTN and SQSTM1, our results reveal mechanistic convergence on vesicle trafficking in ALS and FTD.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1802
[Cu] Class update date: 180311
[Lr] Last revision date:180311
[St] Status:In-Data-Review
[do] DOI:10.1038/nm.4490

  3 / 7515 MEDLINE  
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[PMID]: 29228211
[Au] Autor:Irwin DJ; McMillan CT; Xie SX; Rascovsky K; Van Deerlin VM; Coslett HB; Hamilton R; Aguirre GK; Lee EB; Lee VMY; Trojanowski JQ; Grossman M
[Ad] Address:Penn Frontotemporal Degeneration Center, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA.
[Ti] Title:Asymmetry of post-mortem neuropathology in behavioural-variant frontotemporal dementia.
[So] Source:Brain;141(1):288-301, 2018 Jan 01.
[Is] ISSN:1460-2156
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:Antemortem behavioural and anatomic abnormalities have largely been associated with right hemisphere disease in behavioural-variant frontotemporal dementia, but post-mortem neuropathological examination of bilateral hemispheres remains to be defined. Here we measured the severity of post-mortem pathology in both grey and white matter using a validated digital image analysis method in four cortical regions sampled from each hemisphere in 26 patients with behavioural-variant frontotemporal dementia, including those with frontotemporal degeneration (i.e. tau = 9, TDP-43 = 14, or FUS = 1 proteinopathy) or Alzheimer's pathology (n = 2). We calculated an asymmetry index based on the difference in measured pathology from each left-right sample pair. Analysis of the absolute value of the asymmetry index (i.e. degree of asymmetry independent of direction) revealed asymmetric pathology for both grey and white matter in all four regions sampled in frontototemporal degeneration patients with tau or TDP-43 pathology (P ≤ 0.01). Direct interhemispheric comparisons of regional pathology measurements within-subjects in the combined tauopathy and TDP-43 proteinopathy group found higher pathology in the right orbitofrontal grey matter compared to the left (P < 0.01) and increased pathology in ventrolateral temporal lobe grey matter of the left hemisphere compared to the right (P < 0.02). Preliminary group-wise comparisons between tauopathy and TDP-43 proteinopathy groups found differences in patterns of interhemispheric burden of grey and white matter regional pathology, with greater relative white matter pathology in tauopathies. To test the association of pathology measurement with ante-mortem observations, we performed exploratory analyses in the subset of patients with imaging data (n = 15) and found a direct association for increasing pathologic burden with decreasing cortical thickness in frontotemporal regions on ante-mortem imaging in tauopathy (P = 0.001) and a trend for TDP-43 proteinopathy (P = 0.06). Exploratory clinicopathological correlations demonstrated an association of socially-inappropriate behaviours with asymmetric right orbitofrontal grey matter pathology, and reduced semantically-guided category naming fluency was associated asymmetric white matter pathology in the left ventrolateral temporal region. We conclude that pathologic disease burden is distributed asymmetrically in behavioural-variant frontotemporal dementia, although not universally in the right hemisphere, and this asymmetry contributes to the clinical heterogeneity of the disorder. The basis for this asymmetric profile is enigmatic but may reflect distinct species or strains of tau and TDP-43 pathologies with propensities to spread by distinct cell- and region-specific mechanisms. Patterns of region-specific pathology in the right hemisphere as well as the left hemisphere may play a role in antemortem clinical observations, and these observations may contribute to antemortem identification of molecular pathology in frontotemporal degeneration.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1712
[Cu] Class update date: 180311
[Lr] Last revision date:180311
[St] Status:In-Data-Review
[do] DOI:10.1093/brain/awx319

  4 / 7515 MEDLINE  
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[PMID]: 29523639
[Au] Autor:Willemse EAJ; De Vos A; Herries EM; Andreasson U; Engelborghs S; van der Flier WM; Scheltens P; Crimmins D; Ladenson JH; Vanmechelen E; Zetterberg H; Fagan AM; Blennow K; Bjerke M; Teunissen CE
[Ad] Address:Neurochemistry laboratory, Department of Clinical Chemistry, Amsterdam Neuroscience, VU University Medical Center Amsterdam, the Netherlands; e.willemse@vumc.nl.
[Ti] Title:Neurogranin as Cerebrospinal Fluid Biomarker for Alzheimer Disease: An Assay Comparison Study.
[So] Source:Clin Chem;, 2018 Mar 09.
[Is] ISSN:1530-8561
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:BACKGROUND: Neurogranin in cerebrospinal fluid (CSF) correlates with cognitive decline and is a potential novel biomarker for Alzheimer disease (AD) dementia. We investigated the analytical and diagnostic performance of 3 commonly used neurogranin assays in the same cohort of patients to improve the interpretability of CSF neurogranin test results. METHODS: The neurogranin Singulex assay from Washington University, St. Louis, MO (WashU); ELISA from ADx Neurosciences; and ELISA from Gothenburg University, Mölndal, Sweden (UGot), were compared using silver staining and Western blot after gel electrophoresis. Clinical performance of the 3 assays was compared in samples from individuals diagnosed with subjective cognitive decline (n = 22), and in patients with AD (n = 22), frontotemporal dementia (n = 22), dementia with Lewy bodies (n = 22), or vascular dementia (n = 20), adjusted for sex and age. RESULTS: The assays detected different epitopes of neurogranin: the WashU assay the N-terminal part of neurogranin (S10-D23) and a C-terminal part (G49-G60), the ADx assay C-terminal neurogranin truncated at P75, and the UGot assay the C-terminal neurogranin with intact ending (D78). Spearman ρ was 0.95 between ADx and WashU, 0.87 between UGot and WashU, and 0.81 between UGot and ADx. ANCOVA (analysis of covariance) showed group differences for ranked neurogranin concentrations in each assay (all < 0.05), with specific increases in AD. CONCLUSIONS: Although the 3 assays target different epitopes on neurogranin and have different calibrators, the high correlations and the similar group differences suggest that the different forms of neurogranin in CSF carry similar diagnostic information, at least in the context of neurodegenerative diseases.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180310
[Lr] Last revision date:180310
[St] Status:Publisher

  5 / 7515 MEDLINE  
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[PMID]: 29522758
[Au] Autor:Yeh TH; Liu HF; Li YW; Lu CS; Shih HY; Chiu CC; Lin SJ; Huang YC; Cheng YC
[Ad] Address:Neuroscience Research Center, Chang Gung Memorial Hospital, Linkou, Taoyuan, Taiwan; College of Medicine, Chang Gung University, Taoyuan, Taiwan; Section of Movement Disorders, Department of Neurology, Chang Gung Memorial Hospital at Linkou Medical Center, Taoyuan, Taiwan; Department of Neurology, T
[Ti] Title:C9orf72 is essential for neurodevelopment and motility mediated by cyclin G1.
[So] Source:Exp Neurol;, 2018 Mar 06.
[Is] ISSN:1090-2430
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Hexanucleotide repeat expansions in the C9orf72 gene are a common genetic cause of familial and sporadic amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD). However, the function of C9orf72 in neural development and the pathogenic mechanism underlying neurodegeneration are unknown. We found that disrupting C9orf72 expression by using C9orf72 constructs that lack the complete DENN domain result in reduced GTPase activity in zebrafish embryos, demonstrating the indispensability of the complete DENN domain. This effect was phenocopied by knocking down endogenous C9orf72 expression by using morpholinos. C9orf72-deficient zebrafish embryos exhibited impaired axonogenesis and motility defects. The C9orf72 deficiency upregulated the expression of tp53 and caused neuronal apoptosis. Knockdown Tp53 in the C9orf72-deficient embryos rescued only the apoptotic phenotype but not the phenotype with axonal and motility defects. The C9orf72 deficiency also induced ccng1 (encodes Cyclin G1) mRNA expression, and injection of a dominant-negative Cyclin G1 construct rescued the axonal impairment, apoptosis, and motility defects in the C9orf72-deficient embryos. Our results revealed the GTPase activity of C9orf72 and demonstrated that Cyclin G1 is an essential downstream mediator for C9orf72 in neural development and motility. Furthermore, downregulating Cyclin G1 was sufficient to rescue all the defects caused by C9orf72 deficiency. In summary, we revealed a novel regulatory mechanism underlying the role of C9orf72 in neurological and motility defects. This result facilitates understanding the function of the C9orf72 gene in the developing nervous system and provides a potential mechanism underlying the pathogenesis of ALS-FTD.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180309
[Lr] Last revision date:180309
[St] Status:Publisher

  6 / 7515 MEDLINE  
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[PMID]: 29519717
[Au] Autor:Rubino E; Zhang M; Mongini T; Boschi S; Vercelli L; Vacca A; Govone F; Gai A; Giordana MT; Grinberg M; Rogaeva E; Rainero I
[Ad] Address:Department of Neuroscience "Rita Levi Montalcini", University of Torino, Torino, Italy. Electronic address: elisa.rubino@unito.it.
[Ti] Title:Mutation analysis of CHCHD2 and CHCHD10 in Italian patients with mitochondrial myopathy.
[So] Source:Neurobiol Aging;, 2018 Feb 14.
[Is] ISSN:1558-1497
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Mutations in CHCHD2 and CHCHD10 were recently reported in a broad spectrum of neurodegenerative diseases, for example, Parkinson's disease, amyotrophic lateral sclerosis, frontotemporal dementia, or mitochondrial myopathy (MM). The aim of the study was to evaluate the prevalence of CHCHD2 and CHCHD10 mutations in Italian MM patients without mitochondrial DNA mutations. The coding regions of CHCHD2 and CHCHD10 were sequenced in 62 MM patients. None of the patients showed CHCHD2 mutations, whereas 1 sporadic MM patient carried a homozygous Pro96Thr substitution in CHCHD10. Muscle biopsy of this patient showed intracellular glycogen accumulation with cytochrome c oxidase negative and ragged red fibers. Our study suggests that the homozygous Pro96Thr mutation in CHCHD10 might be pathogenic but does not support a major role for CHCHD2 in MM pathogenesis.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180309
[Lr] Last revision date:180309
[St] Status:Publisher

  7 / 7515 MEDLINE  
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[PMID]: 29507424
[Au] Autor:Kramer NJ; Haney MS; Morgens DW; Jovicic A; Couthouis J; Li A; Ousey J; Ma R; Bieri G; Tsui CK; Shi Y; Hertz NT; Tessier-Lavigne M; Ichida JK; Bassik MC; Gitler AD
[Ad] Address:Department of Genetics, Stanford University School of Medicine, Stanford, CA, USA.
[Ti] Title:CRISPR-Cas9 screens in human cells and primary neurons identify modifiers of C9ORF72 dipeptide-repeat-protein toxicity.
[So] Source:Nat Genet;, 2018 Mar 05.
[Is] ISSN:1546-1718
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Hexanucleotide-repeat expansions in the C9ORF72 gene are the most common cause of amyotrophic lateral sclerosis and frontotemporal dementia (c9ALS/FTD). The nucleotide-repeat expansions are translated into dipeptide-repeat (DPR) proteins, which are aggregation prone and may contribute to neurodegeneration. We used the CRISPR-Cas9 system to perform genome-wide gene-knockout screens for suppressors and enhancers of C9ORF72 DPR toxicity in human cells. We validated hits by performing secondary CRISPR-Cas9 screens in primary mouse neurons. We uncovered potent modifiers of DPR toxicity whose gene products function in nucleocytoplasmic transport, the endoplasmic reticulum (ER), proteasome, RNA-processing pathways, and chromatin modification. One modifier, TMX2, modulated the ER-stress signature elicited by C9ORF72 DPRs in neurons and improved survival of human induced motor neurons from patients with C9ORF72 ALS. Together, our results demonstrate the promise of CRISPR-Cas9 screens in defining mechanisms of neurodegenerative diseases.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180309
[Lr] Last revision date:180309
[St] Status:Publisher
[do] DOI:10.1038/s41588-018-0070-7

  8 / 7515 MEDLINE  
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[PMID]: 29457785
[Au] Autor:Lee Y; Jonson PH; Sarparanta J; Palmio J; Sarkar M; Vihola A; Evilä A; Suominen T; Penttilä S; Savarese M; Johari M; Minot MC; Hilton-Jones D; Maddison P; Chinnery P; Reimann J; Kornblum C; Kraya T; Zierz S; Sue C; Goebel H; Azfer A; Ralston SH; Hackman P; Bucelli RC; Taylor JP; Weihl CC; Udd B
[Ad] Address:Department of Neurology, Hope Center for Neurological Diseases, Washington University School of Medicine, St. Louis, Missouri, USA.
[Ti] Title:TIA1 variant drives myodegeneration in multisystem proteinopathy with SQSTM1 mutations.
[So] Source:J Clin Invest;128(3):1164-1177, 2018 Mar 01.
[Is] ISSN:1558-8238
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Multisystem proteinopathy (MSP) involves disturbances of stress granule (SG) dynamics and autophagic protein degradation that underlie the pathogenesis of a spectrum of degenerative diseases that affect muscle, brain, and bone. Specifically, identical mutations in the autophagic adaptor SQSTM1 can cause varied penetrance of 4 distinct phenotypes: amyotrophic lateral sclerosis (ALS), frontotemporal dementia, Paget's disease of the bone, and distal myopathy. It has been hypothesized that clinical pleiotropy relates to additional genetic determinants, but thus far, evidence has been lacking. Here, we provide evidence that a TIA1 (p.N357S) variant dictates a myodegenerative phenotype when inherited, along with a pathogenic SQSTM1 mutation. Experimentally, the TIA1-N357S variant significantly enhances liquid-liquid-phase separation in vitro and impairs SG dynamics in living cells. Depletion of SQSTM1 or the introduction of a mutant version of SQSTM1 similarly impairs SG dynamics. TIA1-N357S-persistent SGs have increased association with SQSTM1, accumulation of ubiquitin conjugates, and additional aggregated proteins. Synergistic expression of the TIA1-N357S variant and a SQSTM1-A390X mutation in myoblasts leads to impaired SG clearance and myotoxicity relative to control myoblasts. These findings demonstrate a pathogenic connection between SG homeostasis and ubiquitin-mediated autophagic degradation that drives the penetrance of an MSP phenotype.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1802
[Cu] Class update date: 180309
[Lr] Last revision date:180309
[St] Status:In-Data-Review

  9 / 7515 MEDLINE  
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[PMID]: 29186630
[Au] Autor:Clark CN; Golden HL; McCallion O; Nicholas JM; Cohen MH; Slattery CF; Paterson RW; Fletcher PD; Mummery CJ; Rohrer JD; Crutch SJ; Warren JD
[Ad] Address:Dementia Research Centre, UCL Institute of Neurology, University College London, London, UK.
[Ti] Title:Music models aberrant rule decoding and reward valuation in dementia.
[So] Source:Soc Cogn Affect Neurosci;, 2017 Nov 24.
[Is] ISSN:1749-5024
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:Aberrant rule- and reward-based processes underpin abnormalities of socio-emotional behaviour in major dementias. However, these processes remain poorly characterised. Here we used music to probe rule decoding and reward valuation in patients with frontotemporal dementia syndromes and Alzheimer's disease relative to healthy age-matched individuals. We created short melodies that were either harmonically resolved ('finished') or unresolved ('unfinished'); the task was to classify each melody as finished or unfinished (rule processing) and rate its subjective pleasantness (reward valuation). Results were adjusted for elementary pitch and executive processing; neuroanatomical correlates were assessed using voxel-based morphometry. Relative to healthy older controls, patients with behavioural variant frontotemporal dementia showed impairments of both musical rule decoding and reward valuation, while patients with semantic dementia showed impaired reward valuation but intact rule decoding, patients with Alzheimer's disease showed impaired rule decoding but intact reward valuation and patients with progressive nonfluent aphasia performed comparably to healthy controls. Grey matter associations with task performance were identified in anterior temporal, medial and lateral orbitofrontal cortices, previously implicated in computing diverse biological and non-biological rules and rewards. The processing of musical rules and reward distils cognitive and neuroanatomical mechanisms relevant to complex socio-emotional dysfunction in major dementias.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1711
[Cu] Class update date: 180309
[Lr] Last revision date:180309
[St] Status:Publisher
[do] DOI:10.1093/scan/nsx140

  10 / 7515 MEDLINE  
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[PMID]: 29514947
[Au] Autor:Meeter LHH; Vijverberg EG; Del Campo M; Rozemuller AJM; Donker Kaat L; de Jong FJ; van der Flier WM; Teunissen CE; van Swieten JC; Pijnenburg YAL
[Ad] Address:From the Alzheimer Center and Department of Neurology (L.H.H.M., L.D.K., F.J.d.J., J.C.v.S.), Erasmus Medical Center, Rotterdam; Alzheimer Center and Department of Neurology (E.G.V., W.M.v.d.F., Y.A.L.P.), Neurochemistry Laboratory, Department of Clinical Chemistry (M.D.C., C.E.T.), Department of Pa
[Ti] Title:Clinical value of neurofilament and phospho-tau/tau ratio in the frontotemporal dementia spectrum.
[So] Source:Neurology;, 2018 Mar 07.
[Is] ISSN:1526-632X
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:OBJECTIVE: To examine the clinical value of neurofilament light chain (NfL) and the phospho-tau/total tau ratio (p/t-tau) across the entire frontotemporal dementia (FTD) spectrum in a large, well-defined cohort. METHODS: CSF NfL and p/t-tau levels were studied in 361 patients with FTD: 179 behavioral variant FTD, 17 FTD with motor neuron disease (FTD-MND), 36 semantic variant primary progressive aphasia (PPA), 19 nonfluent variant PPA, 4 logopenic variant PPA (lvPPA), 42 corticobasal syndrome, and 64 progressive supranuclear palsy. Forty-five cognitively healthy controls were also included. Definite pathology was known in 68 patients (49 frontotemporal lobar degeneration [FTLD]-TDP, 18 FTLD-tau, 1 FTLD-FUS). RESULTS: NfL was higher in all diagnoses, except lvPPA (n = 4), than in controls, equally elevated in behavioral variant FTD, semantic variant PPA, nonfluent variant PPA, and corticobasal syndrome, and highest in FTD-MND. The p/t-tau was lower in all clinical groups, except lvPPA, than in controls and lowest in FTD-MND. NfL did not discriminate between TDP and tau pathology, while the p/t-tau ratio had a good specificity (76%) and moderate sensitivity (67%). Both high NfL and low p/t-tau were associated with poor survival (hazard ratio on tertiles 1.7 for NfL, 0.7 for p/t-tau). CONCLUSION: NfL and p/t-tau similarly discriminated FTD from controls, but not between clinical subtypes, apart from FTD-MND. Both markers predicted survival and are promising monitoring biomarkers for clinical trials. Of note, p/t-tau, but not NfL, was specific to discriminate TDP from tau pathology in vivo. CLASSIFICATION OF EVIDENCE: This study provides Class III evidence that for patients with cognitive issues, CSF NfL and p/t-tau levels discriminate between those with and without FTD spectrum disorders.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180308
[Lr] Last revision date:180308
[St] Status:Publisher


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