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Oligomeric α-synuclein and glucocerebrosidase activity levels in GBA-associated Parkinson's disease.

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Affiliations

  • 1. Petersburg Nuclear Physics Institute, St. Petersburg, Russia; First Pavlov State Medical University of St. Petersburg, St. Petersburg, Russia; St. Petersburg Academic University-Nanothecnology Research and Education Centre, RAS, St. Petersburg, Russia; Institute of Experimental Medicine, St. Petersburg, Russia.
      Authors
    • Pchelina S 1
    (1 author)
  • 2. Petersburg Nuclear Physics Institute, St. Petersburg, Russia; First Pavlov State Medical University of St. Petersburg, St. Petersburg, Russia; St. Petersburg Academic University-Nanothecnology Research and Education Centre, RAS, St. Petersburg, Russia.
      Authors
    • Emelyanov A 2
    (1 author)
  • 3. Research Center of Medical Genetics, Moscow, Russia.
      Authors
    • Baydakova G 3
    • Zakharova E 3
    (2 authors)
  • 4. Petersburg Nuclear Physics Institute, St. Petersburg, Russia.
      Authors
    • Andoskin P 4
    • Kulabukhova D 4
    • Lavrinova A 4
    • Kopytova A 4
    • Garaeva L 4
    (5 authors)
  • 5. First Pavlov State Medical University of St. Petersburg, St. Petersburg, Russia; Institute of Experimental Medicine, St. Petersburg, Russia.
      Authors
    • Senkevich K 5
    • Miliukhina I 5
    (2 authors)
    • Show all (9)

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Neuroscience Letters, 22 Oct 2016, 636:70-76
https://doi.org/10.1016/j.neulet.2016.10.039 PMID: 27780739 

Abstract 

Alpha-synuclein oligomerization plays a key role in the development of Parkinson's disease (PD). Being the most common genetic contributor to PD, glucocerebrosidase 1 (GBA) mutations have been associated with decreased GBA enzymatic activity in PD patients with mutations in the GBA gene (GBA-PD). However, it is unknown whether the activities of other lysosomal hydrolases are being altered in GBA-PD patients and are accompanied by an increase in alpha-synuclein oligomerization. The aim of our study was to estimate GBA enzymatic activity as well as the activities of five other lysosomal hydrolases (galactocerebrosidase, alpha-glucosidase, alpha-galactosidase, sphingomyelinase, alpha-iduronidase) in dried blood spots with assessing plasma oligomeric alpha-synuclein levels in sporadic PD (sPD) patients, in GBA-PD patients and in controls. GBA enzymatic activity and plasma oligomeric alpha-synuclein levels were assessed in sPD patients (N=84), in GBA-PD patients (N=21) and controls (N=62) by LC-MS/MS and ELISA methods accordingly. GBA-PD patients showed lower GBA enzymatic activity compared to controls (p=0.001) and to sPD (p=0.0001). We also found the reduction of GLA enzymatic activity (but not of other lysosomal hydrolases) in GBA-PD (p=0.001). At the same time plasma oligomeric alpha-synuclein levels were increased in GBA-PD group compared to sPD and controls (p=0.002 and p<0.0001, respectively). Our results suggest that the decrease in enzymatic activity of lysosomal hydrolases in GBA mutation carriers may contribute to PD pathogenesis by increasing the level of neurotoxic oligomeric alpha-synuclein species.

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RFBR

    Russian Foundation for Basic Research (RFBR) (1)