Neuronal Intranuclear Inclusion Disease Without Polyglutamine Inclusions in a Child

Autor: Majeed Al-Mateen, Lawrence Lavine, Sam J. Insalaco, Clayton A. Wiley, Ronald L. Hamilton, Kathryn McFadden, Guoji Wang
Rok vydání: 2005
Předmět:
Male
Protein sumoylation
Cerebellum
Pathology
medicine.medical_specialty
Neurofilament
Ataxia
Adolescent
Intranuclear Inclusion Bodies
Synucleins
Antigens
Differentiation
Myelomonocytic
Nerve Tissue Proteins
tau Proteins
Promyelocytic Leukemia Protein
Biology
Article
Pathology and Forensic Medicine
Cellular and Molecular Neuroscience
Receptors
Glucocorticoid
Microscopy
Electron
Transmission
Antigens
CD
Neurofilament Proteins
Glial Fibrillary Acidic Protein
medicine
Humans
HSP90 Heat-Shock Proteins
Neurons
Ubiquitin
Tumor Suppressor Proteins
Neurodegeneration
Brain
Nuclear Proteins
Neurodegenerative Diseases
General Medicine
Spinal cord
medicine.disease
Crystallins
Immunohistochemistry
Neoplasm Proteins
Dentate nucleus
medicine.anatomical_structure
nervous system
Neurology
Gliosis
alpha-Synuclein
Neurology (clinical)
medicine.symptom
Peptides
Transcription Factors
Zdroj: Journal of Neuropathology & Experimental Neurology. 64:545-552
ISSN: 1554-6578
0022-3069
DOI: 10.1093/jnen/64.6.545
Popis: Neuronal intranuclear inclusion disease (NIID) is a rare and heterogeneous group of slowly progressive neurodegenerative disorders characterized by the widespread presence of eosinophilic neuronal intranuclear inclusions (NII) accompanied by a more restricted pattern of neuronal loss. We report here the pathologic findings in a 13-year-old boy who died after a 6-year clinical history of progressive ataxia, extrapyramidal manifestations, and lower motor neuron abnormalities. Histological evaluation of the brain revealed widespread NII in most neurons. Marked loss of cerebellar Purkinje cells and neurons in the dentate nucleus, red nucleus, and spinal cord anterior horns was accompanied by a modest astrocytosis. Because of the abundance of NII and the absence of a relationship between NII and neuronal loss or microglial activation, we conclude that loss of cerebellar, brainstem, and spinal cord neurons reflects selective neuronal vulnerability. NII were immunoreactive for ubiquitin, glucocorticoid receptor, and SUMO-1, a small, ubiquitin-like protein purportedly involved in protein transport and gene transcription. NII were non-reactive for polyglutamine (1C2), TATA binding protein, promyelocytic leukemia protein, heat shock protein 90, tau, alpha-synuclein, neurofilament, and beta amyloid. The moderate ubiquitin and strong SUMO-1 staining of NII in juvenile cases is the reverse of the pattern noted in adult diseases, suggesting the two age groups are pathogenically distinct. We suggest that juvenile NIID is a spinocerebellar brainstem ataxic disease possibly related to an abnormality in SUMOylation.
Databáze: OpenAIRE
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