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Colocalization of Transactivation-Responsive DNA-Binding Protein 43 and Huntingtin in Inclusions of Huntington Disease

Transactivation-responsive DNA-binding protein 43 (TDP-43) is a component of pathological inclusions in amyotrophic lateral sclerosis and several forms of sporadic and familial frontotemporal lobar degeneration. Transactivation-responsive DNA-binding protein 43-immunostained inclusions have also bee... Full description

Journal Title: Journal of neuropathology and experimental neurology 2008-12, Vol.67 (12), p.1159-1165
Main Author: Schwab, Claudia
Other Authors: Arai, Tetsuaki , Hasegawa, Masato , Yu, Sheng , McGeer, Patrick L
Format: Electronic Article Electronic Article
Language: English
Subjects:
Quelle: Alma/SFX Local Collection
Publisher: Hagerstown, MD: American Association of Neuropathologists, Inc
ID: ISSN: 0022-3069
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recordid: cdi_proquest_miscellaneous_69871007
title: Colocalization of Transactivation-Responsive DNA-Binding Protein 43 and Huntingtin in Inclusions of Huntington Disease
format: Article
creator:
  • Schwab, Claudia
  • Arai, Tetsuaki
  • Hasegawa, Masato
  • Yu, Sheng
  • McGeer, Patrick L
subjects:
  • Adult
  • Aged
  • Aged, 80 and over
  • Antibody Specificity - immunology
  • Biological and medical sciences
  • Biomarkers - analysis
  • Biomarkers - metabolism
  • Brain - metabolism
  • Brain - pathology
  • Brain - physiopathology
  • Cell Nucleus - ultrastructure
  • Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases
  • DNA-Binding Proteins - genetics
  • DNA-Binding Proteins - metabolism
  • Female
  • Humans
  • Huntingtin Protein
  • Huntington Disease - genetics
  • Huntington Disease - metabolism
  • Huntington Disease - pathology
  • Immunohistochemistry - methods
  • Inclusion Bodies - genetics
  • Inclusion Bodies - metabolism
  • Inclusion Bodies - pathology
  • Male
  • Medical sciences
  • Middle Aged
  • Nerve Tissue Proteins - genetics
  • Nerve Tissue Proteins - metabolism
  • Neurites - metabolism
  • Neurites - pathology
  • Neurology
  • Neurons - metabolism
  • Neurons - pathology
  • Nuclear Proteins - genetics
  • Nuclear Proteins - metabolism
  • Phosphorylation
  • Ubiquitin - metabolism
ispartof: Journal of neuropathology and experimental neurology, 2008-12, Vol.67 (12), p.1159-1165
description: Transactivation-responsive DNA-binding protein 43 (TDP-43) is a component of pathological inclusions in amyotrophic lateral sclerosis and several forms of sporadic and familial frontotemporal lobar degeneration. Transactivation-responsive DNA-binding protein 43-immunostained inclusions have also been found in other neurodegenerative disorders including Alzheimer disease, dementia with Lewy bodies, and parkinsonism dementia complex of Guam. Here, we analyzed the occurrence of TDP-43 immunostaining in Huntington disease, which is characterized by inclusions containing mutated huntingtin. In all Huntington disease cases studied, TDP-43 was frequently colocalized with huntingtin in dystrophic neurites and various intracellular inclusions, but not in intranuclear inclusions; the latter were only stained with huntingtin and anti-ubiquitin antibodies. Two phosphorylation-dependent TDP-43 antibodies proved to be superior for detecting pathological inclusions because they did not stain nonphosphorylated TDP-43 in normal nuclei; staining of normal nuclei with phosphorylation-independent antibodies obscured the inclusions. Our results further add to the hypothesis that TDP-43 may be involved in the pathology of a variety of neurodegenerative disorders.
language: eng
source: Alma/SFX Local Collection
identifier: ISSN: 0022-3069
fulltext: fulltext
issn:
  • 0022-3069
  • 1554-6578
url: Link


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titleColocalization of Transactivation-Responsive DNA-Binding Protein 43 and Huntingtin in Inclusions of Huntington Disease
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creatorSchwab, Claudia ; Arai, Tetsuaki ; Hasegawa, Masato ; Yu, Sheng ; McGeer, Patrick L
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descriptionTransactivation-responsive DNA-binding protein 43 (TDP-43) is a component of pathological inclusions in amyotrophic lateral sclerosis and several forms of sporadic and familial frontotemporal lobar degeneration. Transactivation-responsive DNA-binding protein 43-immunostained inclusions have also been found in other neurodegenerative disorders including Alzheimer disease, dementia with Lewy bodies, and parkinsonism dementia complex of Guam. Here, we analyzed the occurrence of TDP-43 immunostaining in Huntington disease, which is characterized by inclusions containing mutated huntingtin. In all Huntington disease cases studied, TDP-43 was frequently colocalized with huntingtin in dystrophic neurites and various intracellular inclusions, but not in intranuclear inclusions; the latter were only stained with huntingtin and anti-ubiquitin antibodies. Two phosphorylation-dependent TDP-43 antibodies proved to be superior for detecting pathological inclusions because they did not stain nonphosphorylated TDP-43 in normal nuclei; staining of normal nuclei with phosphorylation-independent antibodies obscured the inclusions. Our results further add to the hypothesis that TDP-43 may be involved in the pathology of a variety of neurodegenerative disorders.
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subjectAdult ; Aged ; Aged, 80 and over ; Antibody Specificity - immunology ; Biological and medical sciences ; Biomarkers - analysis ; Biomarkers - metabolism ; Brain - metabolism ; Brain - pathology ; Brain - physiopathology ; Cell Nucleus - ultrastructure ; Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases ; DNA-Binding Proteins - genetics ; DNA-Binding Proteins - metabolism ; Female ; Humans ; Huntingtin Protein ; Huntington Disease - genetics ; Huntington Disease - metabolism ; Huntington Disease - pathology ; Immunohistochemistry - methods ; Inclusion Bodies - genetics ; Inclusion Bodies - metabolism ; Inclusion Bodies - pathology ; Male ; Medical sciences ; Middle Aged ; Nerve Tissue Proteins - genetics ; Nerve Tissue Proteins - metabolism ; Neurites - metabolism ; Neurites - pathology ; Neurology ; Neurons - metabolism ; Neurons - pathology ; Nuclear Proteins - genetics ; Nuclear Proteins - metabolism ; Phosphorylation ; Ubiquitin - metabolism
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descriptionTransactivation-responsive DNA-binding protein 43 (TDP-43) is a component of pathological inclusions in amyotrophic lateral sclerosis and several forms of sporadic and familial frontotemporal lobar degeneration. Transactivation-responsive DNA-binding protein 43-immunostained inclusions have also been found in other neurodegenerative disorders including Alzheimer disease, dementia with Lewy bodies, and parkinsonism dementia complex of Guam. Here, we analyzed the occurrence of TDP-43 immunostaining in Huntington disease, which is characterized by inclusions containing mutated huntingtin. In all Huntington disease cases studied, TDP-43 was frequently colocalized with huntingtin in dystrophic neurites and various intracellular inclusions, but not in intranuclear inclusions; the latter were only stained with huntingtin and anti-ubiquitin antibodies. Two phosphorylation-dependent TDP-43 antibodies proved to be superior for detecting pathological inclusions because they did not stain nonphosphorylated TDP-43 in normal nuclei; staining of normal nuclei with phosphorylation-independent antibodies obscured the inclusions. Our results further add to the hypothesis that TDP-43 may be involved in the pathology of a variety of neurodegenerative disorders.
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10Cell Nucleus - ultrastructure
11Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases
12DNA-Binding Proteins - genetics
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16Huntingtin Protein
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atitleColocalization of Transactivation-Responsive DNA-Binding Protein 43 and Huntingtin in Inclusions of Huntington Disease
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abstractTransactivation-responsive DNA-binding protein 43 (TDP-43) is a component of pathological inclusions in amyotrophic lateral sclerosis and several forms of sporadic and familial frontotemporal lobar degeneration. Transactivation-responsive DNA-binding protein 43-immunostained inclusions have also been found in other neurodegenerative disorders including Alzheimer disease, dementia with Lewy bodies, and parkinsonism dementia complex of Guam. Here, we analyzed the occurrence of TDP-43 immunostaining in Huntington disease, which is characterized by inclusions containing mutated huntingtin. In all Huntington disease cases studied, TDP-43 was frequently colocalized with huntingtin in dystrophic neurites and various intracellular inclusions, but not in intranuclear inclusions; the latter were only stained with huntingtin and anti-ubiquitin antibodies. Two phosphorylation-dependent TDP-43 antibodies proved to be superior for detecting pathological inclusions because they did not stain nonphosphorylated TDP-43 in normal nuclei; staining of normal nuclei with phosphorylation-independent antibodies obscured the inclusions. Our results further add to the hypothesis that TDP-43 may be involved in the pathology of a variety of neurodegenerative disorders.
copHagerstown, MD
pubAmerican Association of Neuropathologists, Inc
pmid19018245
doi10.1097/NEN.0b013e31818e8951
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