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    Neuronal phosphorylated RNA-dependent protein kinase in Creutzfeldt-Jakob disease.

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    Authors
    Paquet, Claire
    Bose, Anindita
    Polivka, Marc
    Peoc'h, Katell
    Brouland, Jean Philippe
    Keohane, Catherine
    Hugon, Jacques
    Gray, Françoise
    Affiliation
    Service Central d'Anatomie et de Cytologie Pathologiques, APHP, Hôpital Lariboisière-Université Paris VII, France.
    Issue Date
    2009-02
    MeSH
    Aged
    Aged, 80 and over
    Apoptosis
    Brain
    Caspase 3
    Cell Nucleus
    Creutzfeldt-Jakob Syndrome
    Female
    Glial Fibrillary Acidic Protein
    Gliosis
    Humans
    Immunohistochemistry
    In Situ Nick-End Labeling
    Male
    Middle Aged
    Nerve Degeneration
    Neurons
    Phosphorylation
    Prions
    Stress, Physiological
    eIF-2 Kinase
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    Citation
    Neuronal phosphorylated RNA-dependent protein kinase in Creutzfeldt-Jakob disease. 2009, 68 (2):190-8 J. Neuropathol. Exp. Neurol.
    Journal
    Journal of neuropathology and experimental neurology
    URI
    http://hdl.handle.net/10147/201228
    DOI
    10.1097/NEN.0b013e318196cd7c
    PubMed ID
    19151623
    Abstract
    The mechanisms of neuronal apoptosis in Creutzfeldt-Jakob disease (CJD) and their relationship to accumulated prion protein (PrP) are unclear. A recent cell culture study showed that intracytoplasmic PrP may induce phosphorylated RNA-dependent protein kinase (PKR(p))-mediated cell stress. The double-stranded RNA protein kinase PKR is a proapoptotic and stress kinase that accumulates in degenerating neurons in Alzheimer disease. To determine whether neuronal apoptosis in human CJD is associated with activation of the PKR(p) signaling pathway, we assessed in situ end labeling and immunocytochemistry for PrP, glial fibrillary acidic protein, CD68, activated caspase 3, and phosphorylated PKR (Thr451) in samples of frontal, occipital, and temporal cortex, striatum, and cerebellum from 6 patients with sporadic CJD and 5 controls. Neuronal immunostaining for activated PKR was found in all CJD cases. The most staining was in nuclei and, in contrast to findings in Alzheimer disease, cytoplasmic labeling was not detected. Both the number and distribution of PKR(p)-positive neurons correlated closely with the extent of neuronal apoptosis, spongiosis, astrocytosis, and microglial activation and with the phenotype and disease severity. There was no correlation with the type, topography, or amount of extracellular PrP deposits. These findings suggest that neuronal apoptosis in human CJD may result from PKR(p)-mediated cell stress and are consistent with recent studies supporting a pathogenic role for intracellular or transmembrane PrP.
    Item Type
    Article
    Language
    en
    ISSN
    0022-3069
    ae974a485f413a2113503eed53cd6c53
    10.1097/NEN.0b013e318196cd7c
    Scopus Count
    Collections
    Cork University Hospital

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