ArticleCurrent medical science2018
LRRK2 G2019S Mutation Inhibits Degradation of α-Synuclein in an In Vitro Model of Parkinson's Disease.
Article in Current medical science, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 20 citations in OpenAlex.
- Neuroinflammation and noradrenergic modulation with β2-adrenoceptors: Emerging therapeutic targets for Parkinson's diseases.Neural regeneration research · 2026Article
- Targeting Cathepsins in Neurodegeneration: Biochemical Advances.Biomedicines · 2025Review
- Recombinant cathepsins B and L promote α-synuclein clearance and restore lysosomal function in human and murine models with α-synuclein pathology.Molecular neurodegeneration · 2025Article
- Cathepsins in Neurological Diseases.International journal of molecular sciences · 2025Review
- Recent advances in targeting LRRK2 for Parkinson's disease treatment.Journal of translational medicine · 2025Review
- Cathepsin-mediated regulation of alpha-synuclein in Parkinson's disease: a Mendelian randomization study.Frontiers in aging neuroscience · 2024Article
- The Role of Cysteine Protease Cathepsins B, H, C, and X/Z in Neurodegenerative Diseases and Cancer.International journal of molecular sciences · 2023Review
- Microglia Share the Burden.Neuroscience bulletin · 2022Article
- Inhibition of LRRK2 kinase activity promotes anterograde axonal transport and presynaptic targeting of α-synuclein.Acta neuropathologica communications · 2021Article
- Article
- The industrial solvent trichloroethylene induces LRRK2 kinase activity and dopaminergic neurodegeneration in a rat model of Parkinson's disease.Neurobiology of disease · 2021Article
- Review
- Review
- "LRRK2: Autophagy and Lysosomal Activity".Frontiers in neuroscience · 2020Review
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The G2019S mutation of the leucine-rich repeat kinase 2 (LRRK2) is the most common genetic cause of Parkinson's disease (PD). However, the molecular mechanisms of LRRK2 mutation contributing to the onset and progression of PD have not been fully illustrated. We generated HEK293 cells stably transfected with α-synuclein and investigated the effect of LRRK2 G2019S mutation on the degradation of α-synuclein. The lysosomal activity was assessed by the protein degradation of glyceraldehyde-3-phosphate dehydrogenase and ribonuclease A. It was found that α-synuclein was mainly degraded in lysosomes. LRRK2 G2019S inhibited the degradation of α-synuclein, and promoted its aggregation. LRRK2 G2019S also decreased the activities of lysosomal enzymes including cathepsin B and cathepsin L. Furthermore, the inhibitory effect of LRRK2 G2019S on lysosomal functions did not depend on its kinase activity. These findings indicated that the inhibitory effect of LRRK2 G2019S on α-synuclein degradation could underlie the pathogenesis of aberrant α-synuclein aggregation in PD with LRRK2 mutation.
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