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  • αB-Crystallin is a Major Component of Glial Cytoplasmic Inclusions in Multiple System Atrophy

    Author(s)
    Pountney, DL
    Treweek, TM
    Chataway, T
    Huang, Y
    Chegini, F
    Blumbergs, PC
    Raftery, MJ
    Gai, WP
    Griffith University Author(s)
    Pountney, Dean L.
    Year published
    2005
    Metadata
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    Abstract
    Multiple system atrophy (MSA) is characterized by the formation of oligodendroglial cytoplasmic inclusions (GCIs) consisting of a-synuclein filaments. aB-crystallin, a small chaperone protein that binds to unfolded proteins and inhibits aggregation, has been documented in GCIs. We investigated the relative abundance and speciation of aB-crystallin in GCIs in MSA brains. We also examined the influence of aB-crystallin on the formation of cytoplasmic inclusions in cultured glial cells. Immunohistochemistry and confocal microscopy revealed aBcrystallin is a prominent component of GCIs, more abundant than in Lewy bodies in Lewy ...
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    Multiple system atrophy (MSA) is characterized by the formation of oligodendroglial cytoplasmic inclusions (GCIs) consisting of a-synuclein filaments. aB-crystallin, a small chaperone protein that binds to unfolded proteins and inhibits aggregation, has been documented in GCIs. We investigated the relative abundance and speciation of aB-crystallin in GCIs in MSA brains. We also examined the influence of aB-crystallin on the formation of cytoplasmic inclusions in cultured glial cells. Immunohistochemistry and confocal microscopy revealed aBcrystallin is a prominent component of GCIs, more abundant than in Lewy bodies in Lewy body dementia. One- and two-dimensional gel electrophoresis and mass spectrometric analysis of GCIs immunopurified from MSA brains indicated that aB-crystallin is a major protein component with multiple post-translationally modified species. In cultured C6 glioma cells treated with the proteasomal inhibitor, lactacystin, to induce accumulation of ubiquitinated proteins, a subset of cells showed increased cytoplasmic staining for aB-crystallin. Proteasomeinhibited cells transfected with GFP-tagged a-synuclein resulted in ubiquitin- and aB-crystallin-positive aggregates resembling GCIs in MSA brains. Our results indicate that aB-crystallin is a major chaperone in MSA, and suggest a role of the protein in the formation of inclusion bodies in glial cells.
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    Journal Title
    Neurotoxicity Research
    Volume
    7
    Issue
    1-2
    Publisher URI
    http://www.springer.com/biomed/neuroscience/journal/12640
    DOI
    https://doi.org/10.1007/BF03033778
    Subject
    Biochemistry and cell biology
    Clinical sciences
    Neurosciences
    Publication URI
    http://hdl.handle.net/10072/27519
    Collection
    • Journal articles

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