bee23fd446c101e7fd6e6daa5b955aa1 pmc_33147750.pdf b6e318e5a8b193abc8d84f2c985e36081f39ae23 pmc_33147750.pdf 59572c8b470b3ebbb62ec66676bd13a71d8b831ffd9de95792855b7f8f0f9bea pmc_33147750.pdf Title: The Emerging Role of the Lysosome in Parkinson’s Disease Subject: Lysosomal function has a central role in maintaining neuronal homeostasis, and, accordingly, lysosomal dysfunction has been linked to neurodegeneration and particularly to Parkinson’s disease (PD). Lysosomes are the converging step where the substrates delivered by autophagy and endocytosis are degraded in order to recycle their primary components to rebuild new macromolecules. Genetic studies have revealed the important link between the lysosomal function and PD; several of the autosomal dominant and recessive genes associated with PD as well as several genetic risk factors encode for lysosomal, autophagic, and endosomal proteins. Mutations in these PD-associated genes can cause lysosomal dysfunction, and since -synuclein degradation is mostly lysosomal-dependent, among other consequences, lysosomal impairment can affect -synuclein turnover, contributing to increase its intracellular levels and therefore promoting its accumulation and aggregation. Recent studies have also highlighted the bidirectional link between Parkinson’s disease and lysosomal storage diseases (LSD); evidence includes the presence of -synuclein inclusions in the brain regions of patients with LSD and the identification of several lysosomal genes involved in LSD as genetic risk factors to develop PD. Keywords: Parkinson’s disease; lysosomes; autophagy; lysosomal storage diseases; endocytosis; glucocerebrosidase; -synuclein Author: Alba Navarro-Romero, Marta Montpeyó and Marta Martinez-Vicente Creator: LaTeX with hyperref package Producer: pdfTeX-1.40.18 CreationDate: Wed Nov 4 09:41:04 2020 CET ModDate: Wed Nov 4 09:50:12 2020 CET Tagged: no UserProperties: no Suspects: no Form: none JavaScript: no Pages: 25 Encrypted: no Page size: 595.276 x 841.89 pts (A4) Page rot: 0 File size: 885181 bytes Optimized: no PDF version: 1.7 name type encoding emb sub uni object ID ------------------------------------ ----------------- ---------------- --- --- --- --------- SOZKOC+VnURWPalladioL-Bold Type 1 Custom yes yes no 10 0 IVLPVJ+URWPalladioL-Ital Type 1 Custom yes yes no 15 0 XWFSWS+URWPalladioL-Bold Type 1 Custom yes yes no 20 0 CVZNDX+URWPalladioL-Roma Type 1 Custom yes yes no 24 0 MHAHCD+Rpxr Type 1 Builtin yes yes no 28 0 QDCWHF+EURM10 Type 1 Builtin yes yes no 32 0 PFKOHU+TimesNewRomanPS-BoldItalicMT Type 1C WinAnsi yes yes no 40 0 MCBCCI+SourceSansRoman-Regular Type 1C Custom yes yes no 57 0 MCBCCM+SourceSansRoman.613wght Type 1C Custom yes yes no 61 0 MCBCCO+SourceSansRoman-Bold Type 1C Custom yes yes no 65 0 NOOBKN+PalatinoLinotype TrueType WinAnsi yes yes no 79 0 NOOBON+PalatinoLinotype,Italic TrueType WinAnsi yes yes no 82 0 NOOBPP+PalatinoLinotype,Bold TrueType WinAnsi yes yes no 85 0 NOODAK+TimesNewRoman CID TrueType Identity-H yes yes yes 88 0 IESWRA+URWPalladioL-BoldItal Type 1 Custom yes yes no 110 0 KNZVOU+Rpxsc Type 1 Builtin yes yes no 114 0 RWSFOK+VnURWPalladioL Type 1 Custom yes yes no 140 0 VSHNAE+Rpcxr Type 1 Builtin yes yes no 178 0 Jhove (Rel. 1.22.1, 2019-04-17) Date: 2023-05-27 03:49:05 CEST RepresentationInformation: pmc_33147750.pdf ReportingModule: PDF-hul, Rel. 1.12.1 (2019-04-17) LastModified: 2023-03-31 11:43:32 CEST Size: 885181 Format: PDF Version: 1.7 Status: Well-Formed and valid SignatureMatches: PDF-hul MIMEtype: application/pdf PDFMetadata: Objects: 817 FreeObjects: 1 IncrementalUpdates: 0 DocumentCatalog: PageLayout: SinglePage PageMode: UseNone Outlines: Item: Title: Introduction Destination: edu.harvard.hul.ois.jhove.module.pdf.PdfSimpleObject@44c8afef Item: Title: The Autophagy Lysosomal Endosomal System Destination: edu.harvard.hul.ois.jhove.module.pdf.PdfSimpleObject@7b69c6ba Children: Item: Title: Autophagy Destination: edu.harvard.hul.ois.jhove.module.pdf.PdfSimpleObject@46daef40 Item: Title: Endocytosis Destination: edu.harvard.hul.ois.jhove.module.pdf.PdfSimpleObject@12f41634 Item: Title: Parkinson’s Disease and Alpha-Synuclein Destination: edu.harvard.hul.ois.jhove.module.pdf.PdfSimpleObject@13c27452 Item: Title: Lysosomal-Dependent Degradation of Synuclein Destination: edu.harvard.hul.ois.jhove.module.pdf.PdfSimpleObject@262b2c86 Item: Title: Lysosomal Dysfunction in Parkinson’s Disease Destination: edu.harvard.hul.ois.jhove.module.pdf.PdfSimpleObject@371a67ec Item: Title: Lysosomal Storage Disorders and Parkinson’s Disease Destination: edu.harvard.hul.ois.jhove.module.pdf.PdfSimpleObject@5ed828d Item: Title: Autophagy Dysfunction in Parkinson’s Disease Destination: edu.harvard.hul.ois.jhove.module.pdf.PdfSimpleObject@50d0686 Item: Title: Endocytosis Dysfunction in Parkinson’s Disease Destination: edu.harvard.hul.ois.jhove.module.pdf.PdfSimpleObject@7a3d45bd Item: Title: Role of Glial Cells in PD Destination: edu.harvard.hul.ois.jhove.module.pdf.PdfSimpleObject@1e7c7811 Item: Title: Conclusions Destination: edu.harvard.hul.ois.jhove.module.pdf.PdfSimpleObject@77ec78b9 Item: Title: References Destination: edu.harvard.hul.ois.jhove.module.pdf.PdfSimpleObject@1a3869f4 Info: Title: The Emerging Role of the Lysosome in Parkinson’s Disease Author: Alba Navarro-Romero, Marta Montpeyó and Marta Martinez-Vicente Subject: Lysosomal function has a central role in maintaining neuronal homeostasis, and, accordingly, lysosomal dysfunction has been linked to neurodegeneration and particularly to Parkinson’s disease (PD). Lysosomes are the converging step where the substrates delivered by autophagy and endocytosis are degraded in order to recycle their primary components to rebuild new macromolecules. Genetic studies have revealed the important link between the lysosomal function and PD; several of the autosomal dominant and recessive genes associated with PD as well as several genetic risk factors encode for lysosomal, autophagic, and endosomal proteins. Mutations in these PD-associated genes can cause lysosomal dysfunction, and since -synuclein degradation is mostly lysosomal-dependent, among other consequences, lysosomal impairment can affect -synuclein turnover, contributing to increase its intracellular levels and therefore promoting its accumulation and aggregation. Recent studies have also highlighted the bidirectional link between Parkinson’s disease and lysosomal storage diseases (LSD); evidence includes the presence of -synuclein inclusions in the brain regions of patients with LSD and the identification of several lysosomal genes involved in LSD as genetic risk factors to develop PD. 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