Bodhicharla, Rakesh, Nagarajan, Archana, Winter, Jody, Adenle, Ademola, Nazir, Aamir, Brady, Declan, Vere, Kelly, Richens, Jo, O'Shea, Paul, Bell, David R. and de Pomerai, David I.
(2012)
Effects of α-synuclein overexpression in transgenic Caenorhabditis elegans strains.
CNS and Neurological Disorders - Drug Targets, 11
(8).
pp. 965-975.
ISSN 1871-5273
Full text not available from this repository.
Abstract
The neural protein α-synuclein aggregates both in vivo and in vitro to form insoluble fibrils that are involved in
Parkinson’s disease pathogenesis. We have generated α-synuclein/fluorescent-protein fusion constructs overexpressed in muscle cells of the nematode, Caenorhabdtis elegans. Green Fluorescent Protein (GFP) variants, Cerulean (C) or Venus (V), were fused to the C-terminus of human α-synuclein (S); the resultant fusion genes were designated SV and SC, plus a CV fusion as well as S, C and V singly. The aggregation behavior of the purified fusion proteins (expressed in E. coli) will be
described elsewhere. These constructs were fused to a C. elegans unc-54 myosin promoter, and integrated transgenic lines generated by microinjection, gamma-irradiation, and outcrossing of fluorescent progeny. All transgenic lines expressing α-synuclein showed significant reductions (p < 0.05) in lifespan, motility and pharyngeal pumping, as compared to wildtype worms or lines expressing CFP and/or YFP only. We showed that CFP and YFP labels colocalised in granular inclusions throughout the body wall in transgenic lines expressing both SC and SV fusions (SC+SV), whereas SV+C worms.
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