![]() ![]() We also observed that the cotransfection of short hairpin RNA that targets PLK2 and α-Syn overexpression plasmid results in the endoplasmic reticulum stress of neurons. In vitro protein ubiquitination assay confirmed that SKP1 could promote the ubiquitination and subsequent protein degradation of PLK2. The co-IP experiment confirmed that SKP1 could directly interact with PLK2. Luciferase activity assay indicated that SKP1 is a target gene of miR-101-3p. However, the co-overexpression of miR-101-3p and α-Syn promoted aggregation and neuron toxicity. The overexpression of α-Syn did not result in toxicity or aggregation. ![]() The underlying role was investigated in the SH-SY5Y cell line. The result indicated that miR-101-3p was overexpressed in the substantia nigra of the postmortem brains of patients with PD. In vitro protein ubiquitination assay was used to ascertain the role of S-phase kinase-associated protein 1 (SKP1) on the ubiquitination processes of polo-like kinase 2 (PLK2). Luciferase activity assay was used to confirm the target gene of miRNA. Coimmunoprecipitation (co-IP) was used to verify the interaction between proteins. Western blot was used to investigate the underlying mechanism. Flow cytometry was used to confirm the apoptosis of neurons. Immunofluorescence was used to study the aggregation of α-Syn. In this study, bioinformatic analysis was used to confirm differentially expressed genes between patients with PD and healthy donors. The aggregation of α-synuclein ( α-Syn) plays an essential role in the progression of PD-related neuron toxicity. Parkinson’s disease (PD) is a neurodegenerative disorder characterized by progressive neuronal loss in different brain regions, including the dopaminergic (DA) neurons of the substantia nigra pars compacta (SNc). ![]()
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January 2023
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