Aggregation of Huntingtin in Neuronal Intranuclear Inclusions and Dystrophic Neurites in Brain

DOI Web Site 被引用文献45件
  • Marian DiFiglia
    M. DiFiglia, E. Sapp, J. P. Vonsattel, Department of Neurology, Massachusetts General Hospital, Boston, MA 02114, USA.
  • Ellen Sapp
    M. DiFiglia, E. Sapp, J. P. Vonsattel, Department of Neurology, Massachusetts General Hospital, Boston, MA 02114, USA.
  • Kathryn O. Chase
    M. DiFiglia, E. Sapp, J. P. Vonsattel, Department of Neurology, Massachusetts General Hospital, Boston, MA 02114, USA.
  • Stephen W. Davies
    M. DiFiglia, E. Sapp, J. P. Vonsattel, Department of Neurology, Massachusetts General Hospital, Boston, MA 02114, USA.
  • Gillian P. Bates
    M. DiFiglia, E. Sapp, J. P. Vonsattel, Department of Neurology, Massachusetts General Hospital, Boston, MA 02114, USA.
  • J. P. Vonsattel
    M. DiFiglia, E. Sapp, J. P. Vonsattel, Department of Neurology, Massachusetts General Hospital, Boston, MA 02114, USA.
  • Neil Aronin
    M. DiFiglia, E. Sapp, J. P. Vonsattel, Department of Neurology, Massachusetts General Hospital, Boston, MA 02114, USA.

抄録

<jats:p> The cause of neurodegeneration in Huntington's disease (HD) is unknown. Patients with HD have an expanded NH <jats:sub>2</jats:sub> -terminal polyglutamine region in huntingtin. An NH <jats:sub>2</jats:sub> -terminal fragment of mutant huntingtin was localized to neuronal intranuclear inclusions (NIIs) and dystrophic neurites (DNs) in the HD cortex and striatum, which are affected in HD, and polyglutamine length influenced the extent of huntingtin accumulation in these structures. Ubiquitin was also found in NIIs and DNs, which suggests that abnormal huntingtin is targeted for proteolysis but is resistant to removal. The aggregation of mutant huntingtin may be part of the pathogenic mechanism in HD. </jats:p>

収録刊行物

  • Science

    Science 277 (5334), 1990-1993, 1997-09-26

    American Association for the Advancement of Science (AAAS)

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