Source:http://linkedlifedata.com/resource/pubmed/id/19039597
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2009-1-26
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pubmed:abstractText |
To determine whether TAR-DNA binding protein 43 (TDP-43) immunoreactivity was present in brains of argyrophilic grain disease (AGD), we immunohistochemically examined 15 cases of AGD (mean age at death: 84 years) using a panel of anti-TDP-43 antibodies, including both phosphorylation-independent and -dependent ones. Nine AGD cases (60%) showed TDP-43 immunoreactivities mainly in the limbic regions and lateral occipitotemporal cortex. TDP-43 positive structures included neuronal cytoplasmic inclusions, dystrophic neurites, glial cytoplasmic inclusions, grain-like dot-shaped structures, and neurofibrillary tangle (NFT)-like structures. The distribution of these TDP-43 positive structures was largely consistent with that of argyrophilic grains. Double-labeling confocal microscopy revealed, however, that many of phospho-TDP-43 positive structures were not colocalized with phospho-tau staining. Colocalization of phospho-TDP-43 and phospho-tau was observed only in part of neuronal cytoplasmic inclusions, grain-like structures and NFT-like structures. There were no differences in demographics, disease duration, brain weight, NFT Braak stage, or severity of amyloid burden between AGD cases with and without TDP-43-immunoreactivity. However, cases of AGD with TDP-43-immunoreactivity were assigned to higher AGD stages than those without TDP-43-immunoreactivity (P < 0.05). Furthermore, the TDP-43 pathology tended to be prominent in cases with severe grain pathology. The results of the present study indicate for the first time a high frequency of concomitant TDP-43 pathology in AGD, and suggest that abnormal accumulation of TDP-43 may be involved in the pathological process and disease progression of AGD.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
1432-0533
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pubmed:author |
pubmed-author:AkiyamaHaruhikoH,
pubmed-author:AraiTetsuakiT,
pubmed-author:FujishiroHiroshigeH,
pubmed-author:HasegawaMasatoM,
pubmed-author:HirayasuYoshioY,
pubmed-author:IsekiEizoE,
pubmed-author:TogoTakashiT,
pubmed-author:TsuchiyaKuniakiK,
pubmed-author:UchikadoHirotakeH,
pubmed-author:YokotaOsamuO
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pubmed:issnType |
Electronic
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pubmed:volume |
117
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
151-8
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pubmed:meshHeading |
pubmed-meshheading:19039597-Aged,
pubmed-meshheading:19039597-Aged, 80 and over,
pubmed-meshheading:19039597-Brain,
pubmed-meshheading:19039597-DNA-Binding Proteins,
pubmed-meshheading:19039597-Dementia,
pubmed-meshheading:19039597-Female,
pubmed-meshheading:19039597-Humans,
pubmed-meshheading:19039597-Immunohistochemistry,
pubmed-meshheading:19039597-Inclusion Bodies,
pubmed-meshheading:19039597-Male,
pubmed-meshheading:19039597-Microscopy, Confocal,
pubmed-meshheading:19039597-Neurofibrillary Tangles,
pubmed-meshheading:19039597-Neuroglia,
pubmed-meshheading:19039597-Neurons,
pubmed-meshheading:19039597-Organ Size,
pubmed-meshheading:19039597-Phosphorylation,
pubmed-meshheading:19039597-tau Proteins
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pubmed:year |
2009
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pubmed:articleTitle |
Accumulation of phosphorylated TDP-43 in brains of patients with argyrophilic grain disease.
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pubmed:affiliation |
Department of Psychogeriatrics, Tokyo Institute of Psychiatry, 2-1-8 Kamikitazawa, Setagaya-ku, Tokyo 156-8585, Japan.
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pubmed:publicationType |
Journal Article
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