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  • Chen, Xin,1980Chalmers tekniska högskola,Chalmers University of Technology (author)

FMN reduces Amyloid-beta toxicity in yeast by regulating redox status and cellular metabolism

  • Article/chapterEnglish2020

Publisher, publication year, extent ...

  • 2020-02-13
  • Springer Science and Business Media LLC,2020

Numbers

  • LIBRIS-ID:oai:gup.ub.gu.se/293174
  • https://gup.ub.gu.se/publication/293174URI
  • https://doi.org/10.1038/s41467-020-14525-4DOI
  • https://research.chalmers.se/publication/515586URI

Supplementary language notes

  • Language:English

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  • Subject category:ref swepub-contenttype
  • Subject category:art swepub-publicationtype

Notes

  • Alzheimer's disease (AD) is defined by progressive neurodegeneration, with oligomerization and aggregation of amyloid-beta peptides (A beta) playing a pivotal role in its pathogenesis. In recent years, the yeast Saccharomyces cerevisiae has been successfully used to clarify the roles of different human proteins involved in neurodegeneration. Here, we report a genome-wide synthetic genetic interaction array to identify toxicity modifiers of A beta 42, using yeast as the model organism. We find that FMN1, the gene encoding riboflavin kinase, and its metabolic product flavin mononucleotide (FMN) reduce A beta 42 toxicity. Classic experimental analyses combined with RNAseq show the effects of FMN supplementation to include reducing misfolded protein load, altering cellular metabolism, increasing NADH/(NADH+NAD(+)) and NADPH/(NADPH+NADP(+)) ratios and increasing resistance to oxidative stress. Additionally, FMN supplementation modifies Htt103QP toxicity and alpha-synuclein toxicity in the humanized yeast. Our findings offer insights for reducing cytotoxicity of A beta 42, and potentially other misfolded proteins, via FMN-dependent cellular pathways.Saccharomyces cerevisiae is a model organism to study proteins involved in neurodegeneration. Here, the authors performed a yeast genome-wide synthetic genetic interaction array (SGA) to screen for toxicity modifiers of A beta 42 and identify riboflavin kinase and its metabolic product flavin mononucleotide as modulators that alleviate cellular A beta 42 toxicity, which is supported by further experimental analyses.

Subject headings and genre

Added entries (persons, corporate bodies, meetings, titles ...)

  • Ji, Boyang,1983Chalmers tekniska högskola,Chalmers University of Technology(Swepub:cth)boyang (author)
  • Hao, XinxinGothenburg University,Göteborgs universitet,Institutionen för biomedicin,Centrum för åldrande och hälsa (AgeCap),Institute of Biomedicine,Centre for Ageing and Health (Agecap),University of Gothenburg(Swepub:gu)xxinha (author)
  • Li, Xiaowei,1986Chalmers tekniska högskola,Chalmers University of Technology(Swepub:cth)lixiaow (author)
  • Eisele, FrederikGothenburg University,Göteborgs universitet,Institutionen för biomedicin,Centrum för åldrande och hälsa (AgeCap),Institute of Biomedicine,Centre for Ageing and Health (Agecap),University of Gothenburg (author)
  • Nyström, Thomas,1960Gothenburg University,Göteborgs universitet,Institutionen för biomedicin,Centrum för åldrande och hälsa (AgeCap),Institute of Biomedicine,Centre for Ageing and Health (Agecap),University of Gothenburg(Swepub:gu)xnysth (author)
  • Petranovic Nielsen, Dina,1975Chalmers tekniska högskola,Chalmers University of Technology(Swepub:cth)dinap (author)
  • Chalmers tekniska högskolaInstitutionen för biomedicin (creator_code:org_t)

Related titles

  • In:Nature Communications: Springer Science and Business Media LLC11:12041-1723

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