• myGriffith
    • Staff portal
    • Contact Us⌄
      • Future student enquiries 1800 677 728
      • Current student enquiries 1800 154 055
      • International enquiries +61 7 3735 6425
      • General enquiries 07 3735 7111
      • Online enquiries
      • Staff phonebook
    View Item 
    •   Home
    • Griffith Research Online
    • Journal articles
    • View Item
    • Home
    • Griffith Research Online
    • Journal articles
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Browse

  • All of Griffith Research Online
    • Communities & Collections
    • Authors
    • By Issue Date
    • Titles
  • This Collection
    • Authors
    • By Issue Date
    • Titles
  • Statistics

  • Most Popular Items
  • Statistics by Country
  • Most Popular Authors
  • Support

  • Contact us
  • FAQs
  • Admin login

  • Login
  • Annular α-synuclein species from purified multiple system atrophy inclusions

    Author(s)
    Pountney, DL
    Lowe, R
    Quilty, M
    Vickers, JC
    Voelcker, NH
    Gai, WP
    Griffith University Author(s)
    Pountney, Dean L.
    Year published
    2004
    Metadata
    Show full item record
    Abstract
    Oligodendroglial cytoplasmic inclusions composed of a-synuclein filamentous aggregates are the pathological hallmark of multiple system atrophy (MSA). We found that cortical tissue from MSA cases contains increased detergent-resistant high-molecular-weight a-synuclein species. To analyse these species, we immunopurified a-synuclein aggregates from pathological samples and examined their ultrastructures using scanning electron and atomic force microscopies. Purified aggregates consisted of bundles of filaments. After treatment with 1% sarcosine or 2% 3-[(3-cholamidopropyl) dimethyl-ammonio]-1-propanesulfonate (CHAPS) detergents, ...
    View more >
    Oligodendroglial cytoplasmic inclusions composed of a-synuclein filamentous aggregates are the pathological hallmark of multiple system atrophy (MSA). We found that cortical tissue from MSA cases contains increased detergent-resistant high-molecular-weight a-synuclein species. To analyse these species, we immunopurified a-synuclein aggregates from pathological samples and examined their ultrastructures using scanning electron and atomic force microscopies. Purified aggregates consisted of bundles of filaments. After treatment with 1% sarcosine or 2% 3-[(3-cholamidopropyl) dimethyl-ammonio]-1-propanesulfonate (CHAPS) detergents, we observed frequent 30-50 nm annular particles, probably released from pathological aggregates due to the dissociation of filaments by the detergents. Antibody recognition imaging using a specific anti-a-synuclein antibody confirmed that the annular structures were positive for a-synuclein. In contrast to pathological a-synuclein, detergent treatment of recombinant a-synuclein yielded only smaller, 10-18 nm spherical particles. Our results demonstrate that detergent treatment of pathological MSA a-synuclein aggregates, but not recombinant a-synuclein, yields discrete a-synuclein-positive species with annular morphologies. The ability of the pathological a-synuclein to form annular aggregates may be an important factor contributing to the toxicity of the protein in disease that may have implications in designing therapeutic strategies aimed at detoxifying a-synuclein aggregates.
    View less >
    Journal Title
    Journal of Neurochemistry
    Volume
    90
    Issue
    2
    DOI
    https://doi.org/10.1111/j.1471-4159.2004.02533.x
    Subject
    Biochemistry and cell biology
    Neurosciences
    Publication URI
    http://hdl.handle.net/10072/16891
    Collection
    • Journal articles

    Footer

    Disclaimer

    • Privacy policy
    • Copyright matters
    • CRICOS Provider - 00233E
    • TEQSA: PRV12076

    Tagline

    • Gold Coast
    • Logan
    • Brisbane - Queensland, Australia
    First Peoples of Australia
    • Aboriginal
    • Torres Strait Islander