Literature DB >> 19330339

TDP-43 in ubiquitinated inclusions in the inferior olives in frontotemporal lobar degeneration and in other neurodegenerative diseases: a degenerative process distinct from normal ageing.

Yvonne Davidson1, Hanan Amin, Thomas Kelley, Jing Shi, Jinzhou Tian, Ravindran Kumaran, Tammaryn Lashley, Andrew J Lees, Daniel DuPlessis, David Neary, Julie Snowden, Haruhiko Akiyama, Tetsuaki Arai, Masato Hasegawa, Rina Bandopadhyay, Steve Sikkink, Stuart Pickering-Brown, David M A Mann.   

Abstract

Ubiquitin immunoreactive (UBQ-ir) inclusions were present to variable extents in the inferior olivary nucleus (ION) in 37/48 (77%) patients with frontotemporal lobar degeneration (FTLD), in 10/11 (91%) patients with motor neurone disease (MND), in 5/5 (100%) patients with Alzheimer's disease (AD), 5/7 (71%) patients with dementia with Lewy bodies, 13/19 (68%) patients with Parkinson's disease, 11/11(100%) patients with Progressive Supranuclear Palsy, 2/6 (33%) patients with Multisystem Atrophy, 1/3 (33%) patients with Huntington's disease and in 14/14 (100%) normal elderly control subjects. In FTLD, UBQ-ir inclusions were present in 26/32 (81%) patients with FTLD-U, in 10/15 (67%) patients with tauopathy, and in the single patient with Dementia Lacking Distinctive Histology. In 13 FTLD-U patients, and in a single AD and in 2 MND patients, the UBQ-ir inclusions had a rounded, spicular or skein-type appearance, and these were also TDP-43 immunoreactive (TDP-43-ir). In all other affected patients in all diagnostic groups, and in control subjects, the UBQ-ir neuronal cytoplasmic inclusions (NCI) were of a conglomerated type, resembling a cluster of large granules or globules, but were never TDP-43-ir. In 3 of the 13 FTLD-U patients with spicular NCI, conglomerated NCI were also present but in separate cells. Double-labelling immunohistochemistry, and confocal microscopy, for UBQ and TDP-43 confirmed that only the spicular UBQ-ir inclusions in patients with FTLD-U, AD and MND contained TDP-43, though in these patients there were occasional TDP-43 immunoreactive inclusions that were not UBQ-ir. Nuclear TDP-43 immunoreactivity was absent in ION in FTLD-U, AD or MND when TDP-43 cytoplasmic inclusions were present, but remained in neurones with UBQ-ir, TDP-43 negative inclusions. The target protein within the UBQ-ir, TDP-43-negative inclusions remains unknown, but present studies indicate that this is not tau, neurofilament or internexin proteins. These TDP-43 negative, UBQ-ir inclusions appear to be more related to ageing than neurodegeneration, and are without apparent diagnostic significance. The pathophysiological mechanism leading to their formation, and any consequences their presence may have on nerve cell function, remain unknown.

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Year:  2009        PMID: 19330339     DOI: 10.1007/s00401-009-0526-z

Source DB:  PubMed          Journal:  Acta Neuropathol        ISSN: 0001-6322            Impact factor:   17.088


  15 in total

Review 1.  On the development of markers for pathological TDP-43 in amyotrophic lateral sclerosis with and without dementia.

Authors:  F Geser; D Prvulovic; L O'Dwyer; O Hardiman; P Bede; A L W Bokde; J Q Trojanowski; H Hampel
Journal:  Prog Neurobiol       Date:  2011-09-03       Impact factor: 11.685

2.  The ALS disease-associated mutant TDP-43 impairs mitochondrial dynamics and function in motor neurons.

Authors:  Wenzhang Wang; Li Li; Wen-Lang Lin; Dennis W Dickson; Leonard Petrucelli; Teng Zhang; Xinglong Wang
Journal:  Hum Mol Genet       Date:  2013-07-04       Impact factor: 6.150

Review 3.  TDP-43 and FUS/TLS: emerging roles in RNA processing and neurodegeneration.

Authors:  Clotilde Lagier-Tourenne; Magdalini Polymenidou; Don W Cleveland
Journal:  Hum Mol Genet       Date:  2010-04-15       Impact factor: 6.150

4.  Pathological 43-kDa transactivation response DNA-binding protein in older adults with and without severe mental illness.

Authors:  Felix Geser; John L Robinson; Joseph A Malunda; Sharon X Xie; Chris M Clark; Linda K Kwong; Paul J Moberg; Erika M Moore; Vivianna M Van Deerlin; Virginia M-Y Lee; Steven E Arnold; John Q Trojanowski
Journal:  Arch Neurol       Date:  2010-10

5.  Motor-Coordinative and Cognitive Dysfunction Caused by Mutant TDP-43 Could Be Reversed by Inhibiting Its Mitochondrial Localization.

Authors:  Wenzhang Wang; Hiroyuki Arakawa; Luwen Wang; Ogoegbunam Okolo; Sandra L Siedlak; Yinfei Jiang; Ju Gao; Fei Xie; Robert B Petersen; Xinglong Wang
Journal:  Mol Ther       Date:  2017-01-04       Impact factor: 11.454

6.  Granular expression of prolyl-peptidyl isomerase PIN1 is a constant and specific feature of Alzheimer's disease pathology and is independent of tau, Aβ and TDP-43 pathology.

Authors:  Ayoub Dakson; Osamu Yokota; Margaret Esiri; Eileen H Bigio; Michael Horan; Neil Pendleton; Anna Richardson; David Neary; Julie S Snowden; Andrew Robinson; Yvonne S Davidson; David M A Mann
Journal:  Acta Neuropathol       Date:  2011-01-18       Impact factor: 17.088

Review 7.  Pathomechanisms of TDP-43 in neurodegeneration.

Authors:  Ju Gao; Luwen Wang; Mikayla L Huntley; George Perry; Xinglong Wang
Journal:  J Neurochem       Date:  2018-02-27       Impact factor: 5.372

8.  Brainstem: neglected locus in neurodegenerative diseases.

Authors:  Lea Tenenholz Grinberg; Udo Rueb; Helmut Heinsen
Journal:  Front Neurol       Date:  2011-07-11       Impact factor: 4.003

9.  Axotrophin/MARCH7 acts as an E3 ubiquitin ligase and ubiquitinates tau protein in vitro impairing microtubule binding.

Authors:  Katharina Flach; Ellen Ramminger; Isabel Hilbrich; Annika Arsalan-Werner; Franziska Albrecht; Lydia Herrmann; Michel Goedert; Thomas Arendt; Max Holzer
Journal:  Biochim Biophys Acta       Date:  2014-06-04

10.  Expression of one important chaperone protein, heat shock protein 27, in neurodegenerative diseases.

Authors:  Xuekai Zhang; Jing Shi; Jinzhou Tian; Andrew C Robinson; Yvonne S Davidson; David M Mann
Journal:  Alzheimers Res Ther       Date:  2014-12-17       Impact factor: 6.982

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