Peer-reviewed veterinary case report
GAPDH binders as potential drugs for the therapy of polyglutamine diseases: design of a new screening assay.
- Journal:
- FEBS letters
- Year:
- 2015
- Authors:
- Lazarev, Vladimir F et al.
- Affiliation:
- Institute of Cytology of Russian Academy of Sciences
Abstract
Proteins with long polyglutamine repeats form a complex with glyceraldehyde-3-phosphate dehydrogenase (GAPDH), which enhances aggregation and cytotoxicity in models of Huntington disease. The aim of this study was to develop a novel assay for the screening of anti-aggregation compounds with a focus on the aggregation-promoting capacity of GAPDH. The assay includes a pure Q58 polyglutamine fragment, GAPDH, and a transglutaminase that links the two proteins. The feasibility of the new assay was verified using two GAPDH binders, hydroxynonenal and -(-)deprenyl, and the benzothiazole derivative PGL-135 which exhibits anti-aggregation effect. All three substances were shown to reduce aggregation and cytotoxicity in the cell and in the fly model of Spinocerebellar ataxia.
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Search related cases →Original publication: https://pubmed.ncbi.nlm.nih.gov/25625921/