Aggregation of Huntingtin in Neuronal Intranuclear Inclusions and Dystrophic Neurites in Brain
Marian DiFigliaG. P. Bates, Division of Medical and Molecular Genetics, UMDS Guy's Hospital, London SE1 7E H, UKEllen SappG. P. Bates, Division of Medical and Molecular Genetics, UMDS Guy's Hospital, London SE1 7E H, UKKathryn ChaseG. P. Bates, Division of Medical and Molecular Genetics, UMDS Guy's Hospital, London SE1 7E H, UKStephen W. DaviesG. P. Bates, Division of Medical and Molecular Genetics, UMDS Guy's Hospital, London SE1 7E H, UKGillian P. BatesG. P. Bates, Division of Medical and Molecular Genetics, UMDS Guy's Hospital, London SE1 7E H, UKJ.-P. G. VonsattelG. P. Bates, Division of Medical and Molecular Genetics, UMDS Guy's Hospital, London SE1 7E H, UKNeil AroninG. P. Bates, Division of Medical and Molecular Genetics, UMDS Guy's Hospital, London SE1 7E H, UK
1997en
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Аннотация
The cause of neurodegeneration in Huntington's disease (HD) is unknown. Patients with HD have an expanded NH2-terminal polyglutamine region in huntingtin. An NH2-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.
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