Neuronal intranuclear hyaline inclusion disease
- 27 November 2003
- journal article
- review article
- Published by Wiley in Neuropathology
- Vol. 23 (4), 351-359
- https://doi.org/10.1046/j.1440-1789.2003.00524.x
Abstract
Neuronal intranuclear hyaline inclusion disease (NIHID) is a rare neurodegenerative disorder characterized pathologically by the presence of eosinophilic intranuclear inclusions in neuronal and glial cells. It has been considered to be a heterogeneous disease entity because the clinical pictures of previously described cases were highly variable. In the present review, reported NIHID cases have been categorized into three clinical subgroups according to onset and disease duration, and the clinical phenotype of each subgroup is discussed. Neuronal intranuclear inclusions (NII) in NIHID are ubiquitinated and their prevalence is inversely correlated with neuronal loss, suggesting that NII formation is a protective mechanism involving the ubiquitin-proteasome-dependent proteolytic pathway. In several polyglutamine diseases, disease-related proteins containing abnormally expanded polyglutamine tracts aggregate in neuronal nuclei, resulting in NII formation. The similarity between NII in NIHID and polyglutamine diseases suggests that they are formed during a common proteolysis-related process that takes place in the nucleus. Although the pathogenetic mechanism underlying NIHID remains unknown, the data reviewed here suggest that it might be related to accumulation of as yet unidentified abnormal proteins or dysfunction of the intranuclear ubiquitin-proteasome pathway.Keywords
This publication has 53 references indexed in Scilit:
- The promyelocytic leukemia nuclear body: sites of activity?Biochemistry and Cell Biology, 2002
- Interaction between Neuronal Intranuclear Inclusions and Promyelocytic Leukemia Protein Nuclear and Coiled Bodies in CAG Repeat DiseasesThe American Journal of Pathology, 2001
- Cellular proteins localized at and interacting within ND10/PML nuclear bodies/PODs suggest functions of a nuclear depotOncogene, 2001
- The PML nuclear bodies: actors or extras?Current Opinion in Genetics & Development, 1999
- Recruitment and the Role of Nuclear Localization in Polyglutamine-mediated AggregationThe Journal of cell biology, 1998
- A novel ubiquitin-specific protease is dynamically associated with the PML nuclear domain and binds to a herpesvirus regulatory proteinThe EMBO Journal, 1997
- Polyglutamine expansion as a pathological epitope in Huntington's disease and four dominant cerebellar ataxiasNature, 1995
- Neuronal intranuclear hyaline inclusion disease with progressive cerebellar ataxiaPediatric Neurology, 1994
- Neuronal intranuclear inclusion disease in a child: Diagnosis by rectal biopsyAnnals of Neurology, 1990
- Neuronal intranuclear inclusion disease in identical twinsAnnals of Neurology, 1984