No evidence for substrate accumulation in Parkinson brains with GBA mutations

Mov Disord. 2015 Jul;30(8):1085-9. doi: 10.1002/mds.26278. Epub 2015 Jun 11.

Abstract

Background: To establish whether Parkinson's disease (PD) brains previously described to have decreased glucocerebrosidase activity exhibit accumulation of the lysosomal enzyme's substrate, glucosylceramide, or other changes in lipid composition.

Methods: Lipidomic analyses and cholesterol measurements were performed on the putamen (n = 5-7) and cerebellum (n = 7-14) of controls, Parkinson's disease brains with heterozygote GBA1 mutations (PD+GBA), or sporadic PD.

Results: Total glucosylceramide levels were unchanged in both PD+GBA and sporadic PD brains when compared with controls. No changes in glucosylsphingosine (deacetylated glucosylceramide), sphingomyelin, gangliosides (GM2, GM3), or total cholesterol were observed in either putamen or cerebellum.

Conclusions: This study did not demonstrate glucocerebrosidase substrate accumulation in PD brains with heterozygote GBA1 mutations in areas of the brain with low α-synuclein pathology.

Keywords: Parkinson's disease; glucocerebrosidase; lysosomes; sphingolipids.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cerebellum / metabolism*
  • Cerebellum / pathology
  • Glucosylceramidase / metabolism*
  • Humans
  • Mutation
  • Putamen / metabolism*
  • Putamen / pathology
  • Tissue Banks*
  • beta-Glucosidase / genetics*

Substances

  • beta-Glucosidase
  • Glucosylceramidase