| http://purl.uniprot.org/citations/25476568 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/25476568 | http://www.w3.org/2000/01/rdf-schema#comment | "Kallikrein-6 and calpain-1 are amongst a small group of proteases that degrade α-synuclein. We have explored the possibility that reduction in the level or activity of these enzymes contributes to the accumulation of α-synuclein in Lewy body diseases. We measured calpain-1 activity by fluorogenic activity assay, kallikrein-6 level by sandwich ELISA, and levels of α-synuclein and α-synuclein phosphorylated at serine 129 (α-synuclein-P129), in post-mortem brain tissue in pure dementia with Lewy bodies (DLB, n=12), Alzheimer's disease (AD, n=20) and age-matched controls (n=19). Calpain-1 activity was significantly reduced in DLB within the cingulate and parahippocampal cortex, regions with highest α-synuclein and α-synuclein-P129 load, and correlated inversely with the levels of α-synuclein and α-synuclein-P129. Calpain-1 was unaltered in the thalamus and frontal cortex, regions with less α-synuclein pathology. Kallikrein-6 level was reduced in the cingulate cortex in the DLB cohort, and correlated inversely with α-synuclein and α-synuclein-P129. Kallikrein-6 was also reduced in DLB in the thalamus but not in relation to α-synuclein or α-synuclein-P129 load and was unaltered in the frontal and parahippocampal cortex. In SH-SY5Y cells overexpressing wild-type α-synuclein there was partial co-localisation of kallikrein-6 and calpain-1 with α-synuclein, and siRNA-mediated knock-down of kallikrein-6 and calpain-1 increased the amount of α-synuclein in cell lysates. Our results indicate that reductions in kallikrein-6 and calpain-1 may contribute to the accumulation of α-synuclein in DLB."xsd:string |
| http://purl.uniprot.org/citations/25476568 | http://purl.org/dc/terms/identifier | "doi:10.1186/s40478-014-0164-0"xsd:string |
| http://purl.uniprot.org/citations/25476568 | http://purl.uniprot.org/core/author | "Love S."xsd:string |
| http://purl.uniprot.org/citations/25476568 | http://purl.uniprot.org/core/author | "Renfrew R."xsd:string |
| http://purl.uniprot.org/citations/25476568 | http://purl.uniprot.org/core/author | "Miners J.S."xsd:string |
| http://purl.uniprot.org/citations/25476568 | http://purl.uniprot.org/core/author | "Swirski M."xsd:string |
| http://purl.uniprot.org/citations/25476568 | http://purl.uniprot.org/core/date | "2014"xsd:gYear |
| http://purl.uniprot.org/citations/25476568 | http://purl.uniprot.org/core/name | "Acta Neuropathol Commun"xsd:string |
| http://purl.uniprot.org/citations/25476568 | http://purl.uniprot.org/core/pages | "164"xsd:string |
| http://purl.uniprot.org/citations/25476568 | http://purl.uniprot.org/core/title | "Accumulation of alpha-synuclein in dementia with Lewy bodies is associated with decline in the alpha-synuclein-degrading enzymes kallikrein-6 and calpain-1."xsd:string |
| http://purl.uniprot.org/citations/25476568 | http://purl.uniprot.org/core/volume | "2"xsd:string |
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