TAU AND PARKINSON'S



Parkinson's disease (PD) is the second most common neurodegenerative disorder, whose prevalence is 2~3 % in the population over 65. α-Synuclein aggregation is the major pathological hallmark of PD. However, recent studies have demonstrated enhancing evidence of tau pathology in PD. Despite extensive considerations, thus far, the actual spreading mechanism of neurodegeneration has remained elusive in a PD brain. This study aimed to further investigate the development of α-synuclein and tau pathology. We employed various PD models, including cultured neurons treated with 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) or recombinant α-synuclein. Also, we studied dopaminergic neurons of Cytokine Interferon-β knock out. Moreover, we examined rats treated with 6-Hydroxydopamine, Rhesus monkeys administrated with MPTP neurotoxin, and finally, human post mortem brains. We found the α-synuclein phosphorylation triggers tau pathogenicity. Also, we observed more widespread phosphorylated tau than α-synuclein with prion-like nature in various brain areas. We optionally removed P-tau or P-α-synuclein from Cytokine Interferon-β knock out with respective monoclonal antibodies. We found that tau immunotherapy was more suppressive to neurodegeneration than α-synuclein elimination. Our findings indicate that the pathogenic tau could be one of the leading causes of comprehensive neurodegeneration triggered by PD.

There is a greater tau pathology distribution than that of α-synuclein in PD, human, post-mortem brains. (a) Immunohistochemical images of the substantia nigra of human, post- mortem brains showing cis P-tau was more widely distributed. Scale bar, 25 μm. (b) Quantification representation of the immunohistochemical analysis, section a. Two-way ANOVA with Tukey's multiple comparison tests, means ± SEM, ****p < .0001; n = 6, n = number of participants with duplicate experiments


Parkinson's disease (PD) is the second most common neurodegenerative disorder, whose prevalence is 2~3 % in the population over 65. α-Synuclein aggregation is the major pathological hallmark of PD. However, recent studies have demonstrated enhancing evidence of tau pathology in PD. Despite extensive considerations, thus far, the actual spreading mechanism of neurodegeneration has remained elusive in a PD brain. This study aimed to further investigate the development of α-synuclein and tau pathology. We employed various PD models, including cultured neurons treated with 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) or recombinant α-synuclein. Also, we studied dopaminergic neurons of Cytokine Interferon-β knock out. Moreover, we examined rats treated with 6-Hydroxydopamine, Rhesus monkeys administrated with MPTP neurotoxin, and finally, human post mortem brains. We found the α-synuclein phosphorylation triggers tau pathogenicity. Also, we observed more widespread phosphorylated tau than α-synuclein with prion-like nature in various brain areas. We optionally removed P-tau or P-α-synuclein from Cytokine Interferon-β knock out with respective monoclonal antibodies. We found that tau immunotherapy was more suppressive to neurodegeneration than α-synuclein elimination. Our findings indicate that the pathogenic tau could be one of the leading causes of comprehensive neurodegeneration triggered by PD.

There is a greater tau pathology distribution than that of α-synuclein in PD, human, post-mortem brains. (a) Immunohistochemical images of the substantia nigra of human, post- mortem brains showing cis P-tau was more widely distributed. Scale bar, 25 μm. (b) Quantification representation of the immunohistochemical analysis, section a. Two-way ANOVA with Tukey's multiple comparison tests, means ± SEM, ****p < .0001; n = 6, n = number of participants with duplicate experiments