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- W1562877184 abstract "A cellular feature of Parkinson's disease is cytosolic accumulation and amyloid formation of α-synuclein (α-syn), implicating a misregulation or impairment of protein degradation pathways that involve the proteasome and lysosome. Within lysosomes, Cathepsin (Cat) D, an aspartyl protease is suggested to be responsible for α-syn clearance; however, the protease alone only generates amyloidogenic C-terminal truncated species (e.g. 1–94 and 5–94), arguing that other proteases and/or environmental factors within the lysosome are needed to facilitate degradation and to avoid α-syn aggregation. Here, we show that in addition to aspartyl cathepsin activity, purified mouse brain and liver lysosomes harbor cysteine cathepsin activity identified as Cat B and L by using liquid chromatography mass spectrometry and peptide mapping. In contrast to Cat D, both Cat B and L cleave α-syn within its amyloidogenic region (residues 20–100) generating short peptides that are not aggregation prone. Surprisingly, we discovered that Cat L is efficient in degrading α-syn amyloid fibrils, which by definition are resistant to broad spectrum proteases. Based on these results, stimulating Cat L activity or increasing its level is a potential strategy for clearance of aggregated α-syn in lysosomes." @default.
- W1562877184 created "2016-06-24" @default.
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- W1562877184 date "2015-04-01" @default.
- W1562877184 modified "2023-09-27" @default.
- W1562877184 title "Cysteine Cathepsins Are Essential in Lysosomal Degradation of α‐Synuclein" @default.
- W1562877184 doi "https://doi.org/10.1096/fasebj.29.1_supplement.564.8" @default.
- W1562877184 hasPublicationYear "2015" @default.
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