We are analyzing https://link.springer.com/article/10.1007/s00401-013-1181-y.

Title:
Dipeptide repeat protein pathology in C9ORF72 mutation cases: clinico-pathological correlations | Acta Neuropathologica
Description:
Hexanucleotide repeat expansion in C9ORF72 is the most common genetic cause of frontotemporal dementia and motor neuron disease. Recently, unconventional non-ATG translation of the expanded hexanucleotide repeat, resulting in the production and aggregation of dipeptide repeat (DPR) proteins (poly-GA, -GR and GP), was identified as a potential pathomechanism of C9ORF72 mutations. Besides accumulation of DPR proteins, the second neuropathological hallmark lesion in C9ORF72 mutation cases is the accumulation of TDP-43. In this study, we characterized novel monoclonal antibodies against poly-GA and performed a detailed analysis of the neuroanatomical distribution of DPR and TDP-43 pathology in a cohort of 35 cases with the C9ORF72 mutation that included a broad spectrum of clinical phenotypes. We found the pattern of DPR pathology to be highly consistent among cases regardless of the phenotype with high DPR load in the cerebellum, all neocortical regions (frontal, motor cortex and occipital) and hippocampus, moderate pathology in subcortical areas and minimal pathology in lower motor neurons. No correlation between DPR pathology and the degree of neurodegeneration was observed, while a good association between TDP-43 pathology with clinical phenotype and degeneration in key anatomical regions was present. Our data confirm that the presence of DPR pathology is intimately related to C9ORF72 mutations. The observed dissociation between DPR inclusion body load and neurodegeneration might suggest inclusion body formation as a potentially protective response to cope with soluble toxic DPR species. Moreover, our data imply that alterations due to the C9ORF72 mutation resulting in TDP-43 accumulation and dysmetabolism as secondary downstream effects likely play a central role in the neurodegenerative process in C9ORF72 pathogenesis.
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Keywords {🔍}

article, google, scholar, pubmed, corf, cas, repeat, expansion, pathology, frontotemporal, tdp, clinical, hexanucleotide, disease, dpr, lateral, sclerosis, acta, mutation, dementia, amyotrophic, van, research, neumann, neuron, neuropathol, munich, germany, mackenzie, neurodegeneration, inclusions, arzberger, motor, translation, neurodegenerative, brain, neurol, privacy, cookies, content, data, dipeptide, protein, cases, dieter, edbauer, study, phenotype, access, neuropathology,

Topics {✒️}

month download article/chapter aggregating dipeptide-repeat proteins chromosome 9p21-linked als-ftd poly-ga-positive cytoplasmic inclusions c9orf72 related dipeptide-repeats combination-specific phenotypic profiles iba1-positive microglia cells amyotrophic lateral sclerosis expanded hexanucleotide repeat chromosome 9p-linked ftd poly-ga-positive inclusions frontotemporal lobar degeneration atg-initiated translation directed full article pdf flanders–belgian ftld cohort population-based cohort study ggggcc repeat expansion related subjects c9orf72 ggggcc repeat hexanucleotide repeat expansion motor neuron disease cohn-hokke pe toxic protein species privacy choices/manage cookies c9orf72 repeat expansion dieter edbauer clinico-pathological correlations c9orf72 hexanucleotide expansion atg translation access dipeptide repeat van der zee lower motor neurons flanders–belgian cohort c9orf72-linked ftld cag expansion transcripts article mackenzie christian haass gfap-positive astrocytes cnpase-positive oligodendrocytes clinico-pathological features van deerlin vm multiple neurodegenerative syndromes mackenzie ir european economic area potentially protective response secondary downstream effects graff-radford nr visuo-spatial dysfunction harmonized classification system alzheimer disease neuropathologic

Questions {❓}

Floris G, Borghero G, Cannas A et al (2012) Frontotemporal dementia with psychosis, parkinsonism, visuo-spatial dysfunction, upper motor neuron involvement associated to expansion of C9ORF72: a peculiar phenotype?
Treusch S, Cyr DM, Lindquist S (2009) Amyloid deposits: protection against toxic protein species?

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      description:Hexanucleotide repeat expansion in C9ORF72 is the most common genetic cause of frontotemporal dementia and motor neuron disease. Recently, unconventional non-ATG translation of the expanded hexanucleotide repeat, resulting in the production and aggregation of dipeptide repeat (DPR) proteins (poly-GA, -GR and GP), was identified as a potential pathomechanism of C9ORF72 mutations. Besides accumulation of DPR proteins, the second neuropathological hallmark lesion in C9ORF72 mutation cases is the accumulation of TDP-43. In this study, we characterized novel monoclonal antibodies against poly-GA and performed a detailed analysis of the neuroanatomical distribution of DPR and TDP-43 pathology in a cohort of 35 cases with the C9ORF72 mutation that included a broad spectrum of clinical phenotypes. We found the pattern of DPR pathology to be highly consistent among cases regardless of the phenotype with high DPR load in the cerebellum, all neocortical regions (frontal, motor cortex and occipital) and hippocampus, moderate pathology in subcortical areas and minimal pathology in lower motor neurons. No correlation between DPR pathology and the degree of neurodegeneration was observed, while a good association between TDP-43 pathology with clinical phenotype and degeneration in key anatomical regions was present. Our data confirm that the presence of DPR pathology is intimately related to C9ORF72 mutations. The observed dissociation between DPR inclusion body load and neurodegeneration might suggest inclusion body formation as a potentially protective response to cope with soluble toxic DPR species. Moreover, our data imply that alterations due to the C9ORF72 mutation resulting in TDP-43 accumulation and dysmetabolism as secondary downstream effects likely play a central role in the neurodegenerative process in C9ORF72 pathogenesis.
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      name:Department of Pathology, Vancouver General Hospital, University of British Columbia, Vancouver, Canada
      name:DZNE Munich, German Center for Neurodegenerative Diseases, Munich, Germany
      name:Center for Neuropathology and Prion Research, Ludwig-Maximilians-University, Munich, Germany
      name:DZNE Munich, German Center for Neurodegenerative Diseases, Munich, Germany
      name:Institute of Molecular Immunology, Helmholtz Zentrum München, Munich, Germany
      name:Department of Neuropathology, Academic Medical Centre, University of Amsterdam, Amsterdam, The Netherlands
      name:Department of Palliative Care and Department of Neurology, Ludwig-Maximilians-University, Munich, Germany
      name:Adolf Butenandt Institute, Biochemistry, Ludwig-Maximilians University, Munich, Germany
      name:DZNE Munich, German Center for Neurodegenerative Diseases, Munich, Germany
      name:DZNE Munich, German Center for Neurodegenerative Diseases, Munich, Germany
      name:Adolf Butenandt Institute, Biochemistry, Ludwig-Maximilians University, Munich, Germany
      name:Munich Cluster of Systems Neurology (SyNergy), Munich, Germany
      name:Center for Neuropathology and Prion Research, Ludwig-Maximilians-University, Munich, Germany
      name:DZNE Munich, German Center for Neurodegenerative Diseases, Munich, Germany
      name:Adolf Butenandt Institute, Biochemistry, Ludwig-Maximilians University, Munich, Germany
      name:Munich Cluster of Systems Neurology (SyNergy), Munich, Germany
      name:Department of Neuropathology, University of Tübingen, Tübingen, Germany
      name:DZNE, German Center for Neurodegenerative Diseases, Tübingen, Germany
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