Alpha‐synuclein p.H50Q, a novel pathogenic mutation for Parkinson's disease

Silke Appel‐Cresswell(University of British Columbia), Carles Vilariño‐Güell(University of British Columbia), Mary Joy Encarnacion(University of British Columbia), Holly E. Sherman(University of British Columbia), Irene Yu(University of British Columbia), Brinda Shah(University of British Columbia), David Weir(University of British Columbia), Christina Thompson(University of British Columbia), Chelsea Szu‐Tu(University of British Columbia), Joanne Trinh(University of British Columbia), Jan Aasly(St Olav's University Hospital), Alex Rajput(Saskatchewan Health Authority), Ali H. Rajput(Saskatchewan Health Authority), A. Jon Stoessl(University of British Columbia), Matthew J. Farrer(University of British Columbia)
Movement Disorders
March 1, 2013
10.1002/mds.25421
Cited by 660

Abstract

BACKGROUND: Alpha-synuclein plays a central role in the pathophysiology of Parkinson's disease. Three missense mutations in SNCA, the gene encoding alpha-synuclein, as well as genomic multiplications have been identified as causes for autosomal-dominantly inherited Parkinsonism. METHODS: Here, we describe a novel missense mutation in exon 4 of SNCA encoding a H50Q substitution in a patient with dopa-responsive Parkinson's disease with a family history of parkinsonism and dementia. RESULTS: The variant was not observed in public databases or identified in unrelated subjects. CONCLUSIONS: The substitution's evolutionary conservation and protein modeling provide additional support for pathogenicity as the amino acid perturbs the same amphipathic alpha helical structure as the previously described pathogenic mutations.

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