Valosin-containing protein immunoreactivity in tauopathies, synucleinopathies, polyglutamine diseases and intranuclear inclusion body disease

Neuropathology

Volumn 33, Issue 6, 2013, Pages 637-644

  Mori, Fumiaki ^a   Tanji, Kunikazu ^a   Toyoshima, Yasuko ^b   Sasaki, Hidenao ^c   Yoshida, Mari ^d   Kakita, Akiyoshi ^b   Takahashi, Hitoshi ^b   Wakabayashi, Koichi ^a  

^a HIROSAKI UNIVERSITY   (Japan)

^b NIIGATA UNIVERSITY   (Japan)

^c HOKKAIDO UNIVERSITY GRADUATE SCHOOL OF MEDICINE   (Japan)

^d AICHI MEDICAL UNIVERSITY   (Japan)

Author keywords

Lewy body; Marinesco body; Neuronal nuclear inclusion; Polyglutamine disease; Valosin containing protein

Indexed keywords

FUSED IN SARCOMA PROTEIN; OPTINEURIN; PROTEIN; UBIQUILIN 2; UNCLASSIFIED DRUG; VALOSIN CONTAINING PROTEIN;

ADULT; AGED; ANTIBODY LABELING; ARTICLE; BRAIN; BRAIN CORTEX; CELL INCLUSION; CELL NUCLEUS INCLUSION BODY; CONTROLLED STUDY; CYTOPLASM; DEGENERATIVE DISEASE; DIFFUSE LEWY BODY DISEASE; GLIA CELL; HUMAN; IMMUNOFLUORESCENCE; IMMUNOHISTOCHEMISTRY; IMMUNOREACTIVITY; INTRANUCLEAR INCLUSION BODY DISEASE; LEWY BODY; MIDDLE AGED; MOTONEURON; NEUROFIBRILLARY TANGLE; NEUROPIL; PARKINSON DISEASE; PICK PRESENILE DEMENTIA; POLYGLUTAMINE DISEASE; PRIORITY JOURNAL; SUBSTANTIA NIGRA; SYNUCLEINOPATHY; TAUOPATHY; TDP 43 PROTEINOPATHY; VERY ELDERLY;

LEWY BODY; MARINESCO BODY; NEURONAL NUCLEAR INCLUSION; POLYGLUTAMINE DISEASE; VALOSIN-CONTAINING PROTEIN;

ADENOSINE TRIPHOSPHATASES; AGED; AGED, 80 AND OVER; BRAIN; CELL CYCLE PROTEINS; FEMALE; HUMANS; IMMUNOHISTOCHEMISTRY; INTRANUCLEAR INCLUSION BODIES; MALE; MIDDLE AGED; NEURODEGENERATIVE DISEASES;

EID: 84897077024     PISSN: 09196544     EISSN: 14401789     Source Type: Journal    
DOI: 10.1111/neup.12050     Document Type: Article

References (27)

1. Wang Q, Song C, Li CC. Molecular perspectives on p97-VCP: progress in understanding its structure and diverse biological functions. J Struct Biol 2004; 146: 44-57.
2. Weihl CC, Pestronk A, Kimonis VE. Valosin-containing protein disease: inclusion body myopathy with Paget's disease of the bone and fronto-temporal dementia. Neuromuscul Disord 2009; 19: 308-315.
3. Forman MS, Mackenzie IR, Cairns NJ etal. Novel ubiquitin neuropathology in frontotemporal dementia with valosin-containing protein gene mutations. J Neuropathol Exp Neurol 2006; 65: 571-581.
4. Watts GD, Wymer J, Kovach MJ etal. Inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia is caused by mutant valosin-containing protein. Nat Genet 2004; 36: 377-381.
5. Johnson JO, Mandrioli J, Benatar M etal. Exome sequencing reveals VCP mutations as a cause of familial ALS. Neuron 2010; 68: 857-864.
6. Mizuno Y, Hori S, Kakizuka A, Okamoto K. Vacuole-creating protein in neurodegenerative diseases in humans. Neurosci Lett 2003; 343: 77-80.
7. Hirabayashi M, Inoue K, Tanaka K etal. VCP/p97 in abnormal protein aggregates, cytoplasmic vacuoles, and cell death, phenotypes relevant to neurodegeneration. Cell Death Differ 2001; 8: 977-984.
8. Ishigaki S, Hishikawa N, Niwa J etal. Physical and functional interaction between Dorfin and Valosin-containing protein that are colocalized in ubiquitylated inclusions in neurodegenerative disorders. J Biol Chem 2004; 279: 51376-51385.
9. Koike M, Fukushi J, Ichinohe Y etal. Valosin-containing protein (VCP) in novel feedback machinery between abnormal protein accumulation and transcriptional suppression. J Biol Chem 2010; 285: 21736-21749.
10. Mori F, Tanji K, Kon T etal. FUS immunoreactivity of neuronal and glial intranuclear inclusions in intranuclear inclusion body disease. Neuropathol Appl Neurobiol 2012; 38: 322-328.
11. Mori F, Tanji K, Toyoshima Y etal. Optineurin immunoreactivity in neuronal nuclear inclusions of polyglutamine diseases (Huntington's, DRPLA, SCA2, SCA3) and intranuclear inclusion body disease. Acta Neuropathol 2012; 123: 747-749.
12. Mori F, Tanji K, Odagiri S etal. Ubiquilin immunoreactivity in cytoplasmic and nuclear inclusions in synucleinopathies, polyglutamine diseases and intranuclear inclusion body disease. Acta Neuropathol 2012; 124: 149-151.
13. Mackenzie IR, Neumann M, Baborie A etal. A harmonized classification system for FTLD-TDP pathology. Acta Neuropathol 2011; 122: 111-113.
14. Braak H, Braak E. Neuropathological stageing of Alzheimer-related changes. Acta Neuropathol 1991; 82: 239-259.
15. Wakabayashi K, Hayashi S, Kakita A etal. Accumulation of alpha-synuclein/NACP is a cytopathological feature common to Lewy body disease and multiple system atrophy. Acta Neuropathol 1998; 96: 445-452.
16. Nishie M, Mori F, Fujiwara H etal. Accumulation of phosphorylated alpha-synuclein in the brain and peripheral ganglia of patients with multiple system atrophy. Acta Neuropathol 2004; 107: 292-298.
17. Woulfe J, Gray D, Prichett-Pejic W, Munoz DG, Chretien M. Intranuclear rodlets in the substantia nigra: interactions with marinesco bodies, ubiquitin, and promyelocytic leukemia protein. J Neuropathol Exp Neurol 2004; 63: 1200-1207.
18. Halawani D, Latterich M. p97: The cell's molecular purgatory? Mol Cell 2006; 22: 713-717.
19. Boyault C, Gilquin B, Zhang Y etal. HDAC6-p97/VCP controlled polyubiquitin chain turnover. EMBO J 2006; 25: 3357-3366.
20. Johnston JA, Illing ME, Kopito RR. Cytoplasmic dynein/dynactin mediates the assembly of aggresomes. Cell Motil Cytoskeleton 2002; 53: 26-38.
21. Johnston JA, Ward CL, Kopito RR. Aggresomes: a cellular response to misfolded proteins. J Cell Biol 1998; 143: 1883-1898.
22. Kawaguchi Y, Kovacs JJ, McLaurin A, Vance JM, Ito A, Yao TP. The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress. Cell 2003; 115: 727-738.
23. Miki Y, Mori F, Tanji K, Kakita A, Takahashi H, Wakabayashi K. Accumulation of histone deacetylase 6, an aggresome-related protein, is specific to Lewy bodies and glial cytoplasmic inclusions. Neuropathology 2011; 31: 561-568.
24. Odagiri S, Tanji K, Mori F etal. Immunohistochemical analysis of Marinesco bodies, using antibodies against proteins implicated in the ubiquitin-proteasome system, autophagy and aggresome formation. Neuropathology 2012; 32: 261-266.
25. Iwata A, Riley BE, Johnston JA, Kopito RR. HDAC6 and microtubules are required for autophagic degradation of aggregated huntingtin. J Biol Chem 2005; 280: 40282-40292.
26. Woulfe J, Munoz D. Tubulin immunoreactive neuronal intranuclear inclusions in the human brain. Neuropathol Appl Neurobiol 2000; 26: 161-171.
27. Borden KL. Pondering the promyelocytic leukemia protein (PML) puzzle: possible functions for PML nuclear bodies. Mol Cell Biol 2002; 22: 5259-5269.