Journal
NEUROBIOLOGY OF AGING
Volume 34, Issue 9, Pages -Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.neurobiolaging.2013.04.004
Keywords
Frontotemporal lobar degeneration; FUS; FET proteins; PRMT1; PRMT3; PRMT8; Protein N-arginine methyltransferase
Categories
Funding
- Mayo Benefactor
- Mayo Foundation
- National Institute of Health [P50 AG016574, R01 NS065782, R01 AG026251, R01 AG037491, P50 AG023501]
- The Consortium for Frontotemporal Dementia Research
- Swiss National Science Foundation [31003A-132864]
- Canadian Institutes of Health Research [74580]
- Pacific Alzheimer's Research Foundation [C06-01]
- Sydney Brain Bank
- National Health and Medical Research Council of Australia
- The University of New South Wales
- Neuroscience Research Australia
- Swiss National Science Foundation (SNF) [31003A_132864] Funding Source: Swiss National Science Foundation (SNF)
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The nuclear protein fused in sarcoma (FUS) is found in cytoplasmic inclusions in a subset of patients with the neurodegenerative disorder frontotemporal lobar degeneration (FTLD-FUS). FUS contains a methylated arginine-glycine-glycine domain that is required for transport into the nucleus. Recent findings have shown that this domain is hypomethylated in patients with FTLD-FUS. To determine whether the cause of hypomethylation is the result of mutations in protein N-arginine methyltransferases (PRMTs), we selected 3 candidate genes (PRMT1, PRMT3, and PRMT8) and performed complete sequencing analysis and real-time polymerase chain reaction mRNA expression analysis in 20 FTLD-FUS cases. No mutations or statistically significant changes in expression were observed in our patient samples, suggesting that defects in PRMTs are not the cause of FTLD-FUS. (C) 2013 Elsevier Inc. All rights reserved.
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