Accumulation of α-synuclein mediates podocyte injury in Fabry nephropathy

J Clin Invest. 2023 Jun 1;133(11):e157782. doi: 10.1172/JCI157782.

Abstract

Current therapies for Fabry disease are based on reversing intracellular accumulation of globotriaosylceramide (Gb3) by enzyme replacement therapy (ERT) or chaperone-mediated stabilization of the defective enzyme, thereby alleviating lysosomal dysfunction. However, their effect in the reversal of end-organ damage, like kidney injury and chronic kidney disease, remains unclear. In this study, ultrastructural analysis of serial human kidney biopsies showed that long-term use of ERT reduced Gb3 accumulation in podocytes but did not reverse podocyte injury. Then, a CRISPR/Cas9-mediated α-galactosidase knockout podocyte cell line confirmed ERT-mediated reversal of Gb3 accumulation without resolution of lysosomal dysfunction. Transcriptome-based connectivity mapping and SILAC-based quantitative proteomics identified α-synuclein (SNCA) accumulation as a key event mediating podocyte injury. Genetic and pharmacological inhibition of SNCA improved lysosomal structure and function in Fabry podocytes, exceeding the benefits of ERT. Together, this work reconceptualizes Fabry-associated cell injury beyond Gb3 accumulation, and introduces SNCA modulation as a potential intervention, especially for patients with Fabry nephropathy.

Keywords: Chronic kidney disease; Drug therapy; Genetic diseases; Genetics; Nephrology.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Fabry Disease* / drug therapy
  • Fabry Disease* / genetics
  • Fabry Disease* / pathology
  • Humans
  • Kidney / metabolism
  • Podocytes* / pathology
  • Trihexosylceramides / metabolism
  • Trihexosylceramides / pharmacology
  • Trihexosylceramides / therapeutic use
  • alpha-Galactosidase / genetics
  • alpha-Galactosidase / metabolism
  • alpha-Galactosidase / therapeutic use
  • alpha-Synuclein / genetics
  • alpha-Synuclein / metabolism

Substances

  • alpha-Synuclein
  • alpha-Galactosidase
  • Trihexosylceramides