Parkinson's disease (PD) is a neurodegenerative disease with characteristics and symptoms that are well defined. Nevertheless, its aetiology remains unknown. PD is characterized by the presence of Lewy bodies inside neurons. α-Synuclein (α-syn) is a soluble protein present in the pre-synaptic terminal of neurons. Evidence suggests that α-syn has a fundamental role in PD pathogenesis, given that it is an important component of Lewy bodies localized in the dopaminergic neurons of PD patients. In the present study, we investigated the influence of wild type (WT) and A30P α-syn overexpression on neuroblastoma SH-SY5Y toxicity induced by the conditioned medium (CM) from primary cultures of glia challenged with lipopolysaccharide (LPS) from Escherichia coli. We observed that SH-SY5Y cells transduced with α-syn (WT or A30P) and treated with CM from LPS-activated glia cells show evidence of cell death, which is not reverted by NF-κB inhibition by sodium salicylate or by blockage of P50 (NF-κB subunit). Furthermore, the expression of A30P α-syn in neuroblastoma SH-SY5Y decreases the cell death triggered by the CM of activated glia versus WT α-syn or control group. This effect of A30P α-syn may be due to the low MAPK42/44 phosphorylation. This finding is substantiated by MEK1 inhibition by PD98059, decreasing LDH release by CM in SH-SY5Y cells. Our results suggest that SH-SY5Y cells transduced with α-syn (WT or A30P) and treated with CM from LPS-activated glia cells show cell death, which is not reverted by NF-κB blockage. Additionally, the expression of A30P α-syn on neuroblastoma SH-SY5Y leads to decreased cell death triggered by the CM of activated glia, when compared to WT α-syn or control group. The mechanism underlying this process remains to be completely elucidated, but the present data suggest that MAPK42/44 phosphorylation plays an important role in this process. CRD42015020829.
Parkinson 's disease ( PD ) is a neurodegenerative disease with characteristics and symptoms that are well defined . Nevertheless , its aetiology remains unknown . PD is characterized by the presence of Lewy bodies inside neurons . α - Synuclein ( α - syn ) is a soluble protein present in the pre - synaptic terminal of neurons . Evidence suggests that α - syn has a fundamental role in PD pathogenesis , given that it is an important component of Lewy bodies localized in the dopaminergic neurons of PD patients . In the present study , we investigated the influence of wild type ( WT ) and A30P α - syn overexpression on neuroblastoma SH - SY5Y toxicity induced by the conditioned medium ( CM ) from primary cultures of glia challenged with lipopolysaccharide ( LPS ) from Escherichia coli . We observed that SH - SY5Y cells transduced with α - syn ( WT or A30P ) and treated with CM from LPS - activated glia cells show evidence of cell death , which is not reverted by NF - κB inhibition by sodium salicylate or by blockage of P50 ( NF - κB subunit ) . Furthermore , the expression of A30P α - syn in neuroblastoma SH - SY5Y decreases the cell death triggered by the CM of activated glia versus WT α - syn or control group . This effect of A30P α - syn may be due to the low MAPK42/44 phosphorylation . This finding is substantiated by MEK1 inhibition by PD98059 , decreasing LDH release by CM in SH - SY5Y cells . Our results suggest that SH - SY5Y cells transduced with α - syn ( WT or A30P ) and treated with CM from LPS - activated glia cells show cell death , which is not reverted by NF - κB blockage . Additionally , the expression of A30P α - syn on neuroblastoma SH - SY5Y leads to decreased cell death triggered by the CM of activated glia , when compared to WT α - syn or control group . The mechanism underlying this process remains to be completely elucidated , but the present data suggest that MAPK42/44 phosphorylation plays an important role in this process . CRD42015020829 .
Which is the primary protein component of Lewy bodies?
Which is the primary protein component of Lewy bodies ?
α-synuclein
alpha-synuclein α-synuclein αSyn