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The Correlation Research of the Lysosomal Degradation Pathway and the Proteasomal Degradation Pathway for α-synuclein Protein

Author: ZhaoJie
Tutor: CaoXueBing；SunShengGang
School: Huazhong University of Science and Technology
Course: Neurology
Keywords: Lysosomal Proteasome α-synuclein Parkinson's disease Autophagy
CLC: R742.5
Type: Master's thesis
Year: 2008
Downloads: 140
Quote: 0
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Abstract


Objective To investigate the mechanism of lysosome and proteasome dysfunction in the pathogenesis of Parkinson's disease. Method with nerve growth factor (Nerve growth factor, NGF)-induced differentiation of PC12 cells as study dopaminergic neurons carrier, respectively, and the combination lysosomal inhibitor and proteasome inhibitor lactacystin E64 (the Trans-Epoxysuccinyl-L- leucylam) Thioflavin processing neuron-like differentiation of PC12 cells, the four MTT assay (MTT) cell activity and the metabolic state, cell apoptosis were detected by flow cytometry, immunofluorescence double labeling method observed in PC12 cells S, α-synuclein protein expression aggregation formation of inclusion bodies; Hoechst33258 double-labeled cells observed α-synuclein protein, thioflavine S apoptosis. Decline (in a concentration-dependent) cell activity in the application of these inhibitors and apoptosis rate; drug treatment, the percentage of α-synuclein protein aggregation and inclusion body formation in PC12 cells: E64 group, 7.94 ± 0.97%, lactacystin. Groups 20.33 ± 2.4%, the combination group 36.77 ± 3.5%, compared with the control group and the group between the differences were statistically significant (P lt; 0.05); inclusion bodies of α-synuclein protein-positive cells significantly apoptosis (17.29 ± 1.54 %). Conclusion lysosome and proteasome dysfunction by abnormal aggregation induced by α-synuclein protein in dopamine neurons may play an important role in PD pathogenesis. Objective To investigate the degradation of α-synuclein protein intracellular lysosomal pathway, its aggregation mechanism. Nerve growth factor NGF-induced differentiation of PC12 cells as a research the dopaminergic neurons carrier, application of rotenone treatment of PC12 cells to establish a cellular model of α-synuclein protein. LAMP2 antibody labeled lysosomal membranes, using double immunofluorescent labeling clearly α-synuclein protein colocalization the LAMP2 between the. Use the lysosomal pathway degradation inhibitor E64 3-MA BafA1 processing neuron-like differentiation of PC12 cells, immunofluorescence double labeling was observed the thioflavin S PC12 cells, α-synuclein protein was gathered inclusion bodies formation. Comparison of the difference in each group. Α-synuclein protein in lysosomes rotenone pre-treated PC12 cells after α-synuclein protein aggregation E64 handling and more inclusion body formation 15.36 ± 0.85%, and the control group, 3-MA group and BafA1-group was statistically significant (P lt; 0.05); 3-MA, BafA1 processing fish pre-treated PC12 cells after rotenone less α-synuclein protein aggregation and only a small amount of inclusion body formation (7.65 ± 0.46% compared to 8.72 ± 0.39 %), compared with the control group was not statistically significant (P gt; 0.05). Conclusion lysosomal chaperone-mediated autophagy pathway may be in the α-synuclein protein degradation, play an important role in gathering and dopamine neuron death process.

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CLC: > Medicine, health > Neurology and psychiatry > Neurology > Brain diseases > Paralysis agitans syndrome
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