ArticleBiochemical and biophysical research communications2020
Cathepsin K is a potent disaggregase of α-synuclein fibrils.
Article in Biochemical and biophysical research communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed, 18 citations in OpenAlex.
- Article
- Mutations in α-synuclein, TDP-43 and tau prolong protein half-life through diminished degradation by lysosomal proteases.Molecular neurodegeneration · 2023Article
- Proteome profiling of cerebrospinal fluid reveals biomarker candidates for Parkinson's disease.Cell reports. Medicine · 2022Article
- The Role of Extracellular Matrix Components in the Spreading of Pathological Protein Aggregates.Frontiers in cellular neuroscience · 2022Review
- Targeted proteolytic products of τ and α-synuclein in neurodegeneration.Essays in biochemistry · 2021Article
- Current Evidence for a Bidirectional Loop Between the Lysosome and Alpha-Synuclein Proteoforms.Frontiers in cell and developmental biology · 2020Review
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The intracellular accumulation of α-synuclein (α-syn) amyloid fibrils is a hallmark of Parkinson's disease. Because lysosomes are responsible for degrading aggregated species, enhancing lysosomal function could alleviate the overburden of α-syn. Previously, we showed that cysteine cathepsins (Cts) is the main class of lysosomal proteases that degrade α-syn, and in particular, CtsL was found to be capable of digesting α-syn fibrils. Here, we report that CtsK is a more potent protease for degrading α-syn amyloids. Using peptide mapping by liquid chromatography with mass spectrometry, critical cleavage sites involved in destabilizing fibril structure are identified. CtsK is only able to devour the internal regions after the removal of both N- and C-termini, indicating their protective role of the amyloid core from proteolytic attack. Our results suggest that if overexpressed in lysosomes, CtsK has the potential to ameliorate α-syn pathology.
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Registered trials
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