Nuclear carrier and RNA-binding proteins in frontotemporal lobar degeneration associated with fused in sarcoma (FUS) pathological changes

Autor:	Eileen H. Bigio, Alexander Gerhard, Yvonne S Davidson, Robert H. Perry, Andrew C Robinson, Anna Richardson, David M. A. Mann, Atik Baborie, Julie S. Snowden, Quan Hu, David Neary, Evelyn Jaros, Nigel J. Cairns, Manjari Mishra
Rok vydání:	2013
Předmět:	Pathology medicine.medical_specialty Histology business.industry nutritional and metabolic diseases RNA-binding protein Frontotemporal lobar degeneration Neuropathology medicine.disease Inclusion bodies nervous system diseases Pathology and Forensic Medicine Neurology Physiology (medical) mental disorders medicine Beta Karyopherins Neurology (clinical) business Immunostaining TAF15 RNA-Binding Protein FUS
Zdroj:	Neuropathology and Applied Neurobiology. 39:157-165
ISSN:	0305-1846
DOI:	10.1111/j.1365-2990.2012.01274.x
Popis:	Aims:? We aimed to investigate the role of the nuclear carrier and binding proteins, transportin-1 (TRN1) and transportin-2 (TRN2), TATA-binding protein-associated factor 15 (TAF15) and Ewing's Sarcoma protein (EWS) in inclusion body formation in cases of Frontotemporal Lobar Degeneration (FTLD) associated with Fused in Sarcoma protein (FTLD-FUS). Methods:? Eight cases of FTLD-FUS (5 cases of atypical FTLD-U (aFTLD-U), 2 of Neuronal Intermediate Filament Inclusion Body Disease (NIFID) and 1 of Basophilic Inclusion Body Disease (BIBD)) were immunostained for FUS, TRN1, TRN2, TAF15 and EWS. 10 cases of FTLD associated with TDP-43 inclusions served as reference cases. Results:? The inclusion bodies in FTLD-FUS contained TRN1 and TAF15 and, to a lesser extent, EWS, but not TRN2. The patterns of immunostaining for TRN1 and TAF15 were very similar to that of FUS. None of these proteins was associated with tau or TDP-43 aggregations in FTLD. Conclusion:? Data suggest that FUS, TRN1 and TAF15 may participate in a functional pathway in an interdependent way, and imply that the function of TDP-43 may not necessarily be in parallel with, or complementary to, that of FUS, despite each protein sharing many similar structural elements. � 2012 The Authors. Neuropathology and Applied Neurobiology � 2012 British Neuropathological Society.
Databáze:	OpenAIRE
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