Premium
Ataxin 1 and ataxin 3 in neuronal intranuclear inclusion disease
Author(s) -
Lieberman Andrew P.,
Trojanowski John Q.,
Leonard Debra G. B.,
Chen KeLian,
Barnett Jeffrey L.,
Leverenz James B.,
Bird Thomas D.,
Robitaille Yves,
Malandrini Alessandro,
Fischbeck Kenneth H.
Publication year - 1999
Publication title -
annals of neurology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.764
H-Index - 296
eISSN - 1531-8249
pISSN - 0364-5134
DOI - 10.1002/1531-8249(199908)46:2<271::aid-ana21>3.0.co;2-m
Subject(s) - disease , biology , inclusion bodies , trinucleotide repeat expansion , protein aggregation , neuroscience , microbiology and biotechnology , pathology , gene , medicine , genetics , allele , escherichia coli
Neuronal intranuclear inclusion disease (NIID) is a multisystem neurodegenerative disorder characterized by large intranuclear aggregates in neurons of the central and peripheral nervous system. These ubiquitinated intranuclear inclusions are morphologically similar to the intraneuronal aggregates that have been identified in the CAG/polyglutamine expansion diseases. As rare aggregates in NIID contain a polyglutamine epitope, we further investigated the relationship between this disease and the CAG/polyglutamine expansion diseases. Here, we show that ataxin 1 and ataxin 3 proteins are recruited into aggregates in NIID in the absence of a CAG expansion in the SCA1 and SCA3 genes. These data support an association of NIID with the polyglutamine disorders and provide evidence of in vivo recruitment of proteins with polyglutamine tracts into intraneuronal aggregates.