ArticleCells2018
Alpha-Synuclein and Calpains Disrupt SNARE-Mediated Synaptic Vesicle Fusion During Manganese Exposure in SH-SY5Y Cells.
Article in Cells, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 23 citations in OpenAlex.
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- pH Effects Can Dominate Chemical Shift Perturbations inACS chemical neuroscience · 2023Article
- Single point mutations at the S129 residue of α-synuclein and their effect on structure, aggregation, and neurotoxicity.Frontiers in chemistry · 2023Article
- Loss of slc39a14 causes simultaneous manganese hypersensitivity and deficiency in zebrafish.Disease models & mechanisms · 2022Article
- Behavioral and neurochemical studies of inherited manganese-induced dystonia-parkinsonism in Slc39a14-knockout mice.Neurobiology of disease · 2021Article
- Inhibition of Ceramide Synthesis Reduces α-Synuclein Proteinopathy in a Cellular Model of Parkinson's Disease.International journal of molecular sciences · 2021Article
- Molecular Targets of Manganese-Induced Neurotoxicity: A Five-Year Update.International journal of molecular sciences · 2021Review
- LncRNA and mRNA expression profiles and functional networks of hyposalivation of the submandibular gland in hypertension.Scientific reports · 2020Article
- Integrated network modeling approach defines key metabolic responses of soil microbiomes to perturbations.Scientific reports · 2020Article
- GLAST Activity is Modified by Acute Manganese Exposure in Bergmann Glial Cells.Neurochemical research · 2020Article
- The ubiquitin ligase Ariadne-1 regulates neurotransmitter release via ubiquitination of NSF.The Journal of biological chemistryArticle
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
Synaptic vesicle fusion is mediated by an assembly of soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptors (SNAREs), composed of syntaxin 1, soluble NSF-attachment protein (SNAP)-25, and synaptobrevin-2/VAMP-2. Previous studies have suggested that over-exposure to manganese (Mn) could disrupt synaptic vesicle fusion by influencing SNARE complex formation, both in vitro and in vivo. However, the mechanisms underlying this effect remain unclear. Here we employed calpeptin, an inhibitor of calpains, along with a lentivirus vector containing alpha-synuclein (α-Syn) shRNA, to examine whether specific SNAP-25 cleavage and the over-expression of α-Syn disturbed the formation of the SNARE complex in SH-SY5Y cells. After cells were treated with Mn for 24 h, fragments of SNAP-25-N-terminal protein began to appear; however, this effect was reduced in the group of cells which were pre-treated with calpeptin. FM1-43-labeled synaptic vesicle fusion decreased with Mn treatment, which was consistent with the formation of SNARE complexes. The interaction of VAMP-2 and α-Syn increased significantly in normal cells in response to 100 μM Mn treatment, but decreased in LV-α-Syn shRNA cells treated with 100 μM Mn; similar results were observed in terms of the formation of SNARE complexes and FM1-43-labeled synaptic vesicle fusion. Our data suggested that Mn treatment could increase [Ca
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