Abstract:
:Intranuclear inclusions have been observed in the brains of patients affected with Huntington's disease (HD). Neuro 2A cells that transiently expressed HD exon 1 bearing 74 glutamine repeats linked to the green fluorescent protein (GFP) and the nuclear localization sequence (NLS) contained aggregates in nuclei. The aggregates were purified by fractionation with centrifugation followed by fluorescence-activated cell sorting (FACS). Heat treatment of the aggregate in an SDS sample buffer caused the dense aggregate cores to disappear and generated a basket-like structure composed of fibrils. Biochemical analysis of the aggregates revealed that the HD exon 1-GFP fusion protein was the major component. The heterogeneous nuclear ribonucleoproteins F and H, histones and ubiquitin were found to be associated with the aggregates. Our observations suggest that the N-terminal fragment of huntingtin may organize the skeletal structure of the aggregates and may disturb normal cellular functions by trapping other proteins within the aggregates.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Hazeki N,Tsukamoto T,Yazawa I,Koyama M,Hattori S,Someki I,Iwatsubo T,Nakamura K,Goto J,Kanazawa Idoi
10.1016/S0006-291X(02)00498-9subject
Has Abstractpub_date
2002-06-07 00:00:00pages
429-40issue
2eissn
0006-291Xissn
1090-2104pii
S0006-291X(02)00498-9journal_volume
294pub_type
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