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In vitro evidence consistent with an interaction between wild-type and mutant SOD1 protein associated with canine degenerative myelopathy.
Qi, Yao; Montague, Paul; Loney, Colin; Campbell, Clare; Shafie, Intan N F; Anderson, Thomas J; McLaughlin, Mark.
Afiliación
  • Qi Y; School of Veterinary Medicine, College of Medical, Veterinary and Life Science, University of Glasgow, Scotland, UK.
  • Montague P; Institute of Infection, Immunity and Inflammation, College of Medical, Veterinary and Life Science (MVLS), University of Glasgow, Glasgow, UK.
  • Loney C; MRC, Centre for Virus Research, MVLS, University of Glasgow, Glasgow, UK.
  • Campbell C; Institute of Infection, Immunity and Inflammation, College of Medical, Veterinary and Life Science (MVLS), University of Glasgow, Glasgow, UK.
  • Shafie INF; Department of Veterinary Clinical Studies, Faculty of Veterinary Medicine, University Putra Malaysia, Serdang, Malaysia.
  • Anderson TJ; School of Veterinary Medicine, College of Medical, Veterinary and Life Science, University of Glasgow, Scotland, UK.
  • McLaughlin M; School of Veterinary Medicine, College of Medical, Veterinary and Life Science, University of Glasgow, Scotland, UK.
Eur J Neurosci ; 50(12): 3896-3905, 2019 12.
Article en En | MEDLINE | ID: mdl-31336405
Canine degenerative myelopathy (DM) is a progressive neurological disorder that may be considered to be a large animal model for specific forms of the fatal human disease, familial amyotrophic lateral sclerosis (fALS). DM is associated with a c118G>A mutation of the superoxide dismutase 1 (Sod1) gene, and a significant proportion of cases are inherited in an autosomal recessive manner in contrast to the largely, but not exclusively, dominant mode of inheritance in fALS. The consensus view is that these Sod1/SOD1 mutations result in a toxic gain of function but the mechanisms remain unclear. Here we used an in vitro neuroblastoma cell line transfection system to monitor wild-type and mutant forms of SOD1 fusion proteins containing either a Cherry or an enhanced green fluorescent protein (EGFP) tag. These fusion proteins retained SOD1 enzymatic activity on a native gel assay system. We demonstrate that SOD1 aggregate density is significantly higher in DM transfectants compared to wild-type. In addition, we show by co-immunoprecipitation and confocal microscopy, evidence for a potential interaction between wild-type and mutant forms of SOD1 in co-transfected cells. While in vitro studies have shown SOD1 heterodimer formation in fALS models, this is the first report for DM SOD1. Therefore, despite for the majority of cases there is a difference in the mode of inheritance between fALS and DM, a similar interaction between wild-type and mutant SOD1 forms can occur. Clarifying the role of SOD1 in DM may also be of benefit to understanding the role of SOD1 in fALS.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Superóxido Dismutasa / Superóxido Dismutasa-1 / Esclerosis Amiotrófica Lateral / Mutación Tipo de estudio: Risk_factors_studies Límite: Animals / Humans Idioma: En Revista: Eur J Neurosci Asunto de la revista: NEUROLOGIA Año: 2019 Tipo del documento: Article Pais de publicación: Francia
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Superóxido Dismutasa / Superóxido Dismutasa-1 / Esclerosis Amiotrófica Lateral / Mutación Tipo de estudio: Risk_factors_studies Límite: Animals / Humans Idioma: En Revista: Eur J Neurosci Asunto de la revista: NEUROLOGIA Año: 2019 Tipo del documento: Article Pais de publicación: Francia