SMPD1 mutations, activity, and α-synuclein accumulation in Parkinson's disease - Université de Montpellier
Article Dans Une Revue Movement Disorders Année : 2019

SMPD1 mutations, activity, and α-synuclein accumulation in Parkinson's disease

Oren Levy
  • Fonction : Auteur
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Wendy Chung
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Sharon Hassin-Baer
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Lior Greenbaum
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Pavlina Wolf
  • Fonction : Auteur
Petra Oliva
  • Fonction : Auteur
Xiaokui Kate Zhang
  • Fonction : Auteur
Nicolas Dupre

Résumé

Background: SMPD1 (acid-sphingomyelinase) variants have been associated with Parkinson's disease in recent studies. The objective of this study was to further investigate the role of SMPD1 mutations in PD. Methods: SMPD1 was sequenced in 3 cohorts (Israel Ashkenazi Jewish cohort, Montreal/Montpellier, and New York), including 1592 PD patients and 975 controls. Additional data were available for 10,709 Ashkenazi Jewish controls. Acid-sphingomyelinase activity was measured by a mass spectrometry-based assay in the New York cohort. α-Synuclein levels were measured in vitro following CRISPR/Cas9-mediated knockout and siRNA knockdown of SMPD1 in HeLa and BE(2)-M17 cells. Lysosomal localization of acid-sphingomyelinase with different mutations was studied, and in silico analysis of their effect on acid-sphingomyelinase structure was performed. Results: SMPD1 mutations were associated with PD in the Ashkenazi Jewish cohort, as 1.4% of PD patients carried the p.L302P or p.fsP330 mutation, compared with 0.37% in 10,709 Ashkenazi Jewish controls (OR, 3.7; 95%CI, 1.6-8.2; P = 0.0025). In the Montreal/Montpellier cohort, the p.A487V variant was nominally associated with PD (1.5% versus 0.14%; P = 0.0065, not significant after correction for multiple comparisons). Among PD patients, reduced acid-sphingomyelinase activity was associated with a 3.5- to 5.8-year earlier onset of PD in the lowest quartile versus the highest quartile of acid-sphingomyelinase activity (P = 0.01-0.001). We further demonstrated that SMPD1 knockout and knockdown resulted in increased α-synuclein levels in HeLa and BE(2)-M17 dopaminergic cells and that the p.L302P and p.fsP330 mutations impair the traffic of acid-sphingomyelinase to the lysosome. Conclusions: Our results support an association between SMPD1 variants, acid-sphingomyelinase activity, and PD. Furthermore, they suggest that reduced acid-sphingomyelinase activity may lead to α-synuclein accumulation. © 2019 International Parkinson and Movement Disorder Society.

Dates et versions

hal-02886620 , version 1 (01-07-2020)

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Citer

Roy Alcalay, Victoria Mallett, Benoît Vanderperre, Omid Tavassoly, Yves M Dauvilliers, et al.. SMPD1 mutations, activity, and α-synuclein accumulation in Parkinson's disease. Movement Disorders, 2019, 34 (4), pp.526-535. ⟨10.1002/mds.27642⟩. ⟨hal-02886620⟩
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