Inhibiting Stearoyl-CoA Desaturase Ameliorates α-Synuclein Cytotoxicity

Cell Rep. 2018 Dec 4;25(10):2742-2754.e31. doi: 10.1016/j.celrep.2018.11.028.

Abstract

The lack of disease-modifying treatments for neurodegenerative disease stems in part from our rudimentary understanding of disease mechanisms and the paucity of targets for therapeutic intervention. Here we used an integrated discovery paradigm to identify a new therapeutic target for diseases caused by α-synuclein (α-syn), a small lipid-binding protein that misfolds and aggregates in Parkinson's disease and other disorders. Using unbiased phenotypic screening, we identified a series of compounds that were cytoprotective against α-syn-mediated toxicity by inhibiting the highly conserved enzyme stearoyl-CoA desaturase (SCD). Critically, reducing the levels of unsaturated membrane lipids by inhibiting SCD reduced α-syn toxicity in human induced pluripotent stem cell (iPSC) neuronal models. Taken together, these findings suggest that inhibition of fatty acid desaturation has potential as a therapeutic approach for the treatment of Parkinson's disease and other synucleinopathies.

Keywords: Parkinson’s disease; chemical genetics; fatty acid desaturation; phenotypic drug screen; stearoyl-CoA desaturase; target identification; vesicle trafficking; α-synuclein.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cytoprotection / drug effects
  • Fatty Acids / metabolism
  • Humans
  • Lipid Metabolism / drug effects
  • Neurons / drug effects
  • Neurons / metabolism
  • Oxadiazoles / chemistry
  • Oxadiazoles / pharmacology
  • Protein Aggregates
  • Rats
  • Saccharomyces cerevisiae / drug effects
  • Stearoyl-CoA Desaturase / antagonists & inhibitors*
  • Stearoyl-CoA Desaturase / metabolism
  • Triglycerides / metabolism
  • alpha-Synuclein / toxicity*

Substances

  • Fatty Acids
  • Oxadiazoles
  • Protein Aggregates
  • Triglycerides
  • alpha-Synuclein
  • Stearoyl-CoA Desaturase