Proximity proteomics reveals unique and shared pathological features between multiple system atrophy and Parkinson’s disease

Artan M, Hartl M, Chen W, de Bono M (2022) Depletion of endogenously biotinylated carboxylases enhances the sensitivity of turboID-mediated proximity labeling in caenorhabditis elegans. J Biol Chem 298:102343. https://doi.org/10.1016/j.jbc.2022.102343

Article  CAS  PubMed  PubMed Central  Google Scholar 

Asi YT, Simpson JE, Heath PR, Wharton SB, Lees AJ, Revesz T, Houlden H, Holton JL (2014) Alpha-synuclein mRNA expression in oligodendrocytes in MSA. Glia 62:964–970. https://doi.org/10.1002/glia.22653

Article  PubMed  PubMed Central  Google Scholar 

Barca E, Kleiner G, Tang G, Ziosi M, Tadesse S, Masliah E, Louis ED, Faust P, Kang UJ, Torres J et al (2016) Decreased coenzyme Q10 levels in multiple system atrophy cerebellum. J Neuropathol Exp Neurol 75:663–672. https://doi.org/10.1093/jnen/nlw037

Article  CAS  PubMed  PubMed Central  Google Scholar 

Bjornsdottir A, Gudmundsson G, Blondal H, Olafsson E (2013) Incidence and prevalence of multiple system atrophy: a nationwide study in Iceland. J Neurol Neurosurg Psychiatry 84:136–140. https://doi.org/10.1136/jnnp-2012-302500

Article  PubMed  Google Scholar 

Borghi R, Marchese R, Negro A, Marinelli L, Forloni G, Zaccheo D, Abbruzzese G, Tabaton M (2000) Full length alpha-synuclein is present in cerebrospinal fluid from Parkinson’s disease and normal subjects. Neurosci Lett 287:65–67. https://doi.org/10.1016/s0304-3940(00)01153-8

Article  CAS  PubMed  Google Scholar 

Cappai R, Leck S-L, Tew DJ, Williamson NA, Smith DP, Galatis D, Sharpies RA, Curtain CC, Ali FE, Cherny RA et al (2005) Dopamine promotes α-synuclein aggregation into SDS-resistant soluble oligomers via a distinct folding pathway. FASEB J 19:1377–1379. https://doi.org/10.1096/fj.04-3437fje

Article  CAS  PubMed  Google Scholar 

Chamling X, Kallman A, Fang W, Berlinicke CA, Mertz JL, Devkota P, Pantoja IEM, Smith MD, Ji Z, Chang C et al (2021) Single-cell transcriptomic reveals molecular diversity and developmental heterogeneity of human stem cell-derived oligodendrocyte lineage cells. Nat Commun 12:652. https://doi.org/10.1038/s41467-021-20892-3

Article  CAS  PubMed  PubMed Central  Google Scholar 

Choi SG, Tittle T, Garcia-Prada D, Kordower JH, Melki R, Killinger BA (2024) Alpha-synuclein aggregates are phosphatase resistant. BioRxiv. https://doi.org/10.1101/2023.11.20.567854

Article  PubMed  PubMed Central  Google Scholar 

Chu Y, Hirst WD, Federoff HJ, Harms AS, Stoessl AJ, Kordower JH (2023) Nigrostriatal tau pathology in parkinsonism and Parkinson’s disease. Brain 147:444–457. https://doi.org/10.1093/brain/awad388

Article  PubMed Central  Google Scholar 

Chung CY, Khurana V, Yi S, Sahni N, Loh KH, Auluck PK, Baru V, Udeshi ND, Freyzon Y, Carr SA et al (2017) In situ peroxidase labeling and mass-spectrometry connects alpha-synuclein directly to endocytic trafficking and mRNA metabolism in neurons. Cell Syst 4(242–250):e244. https://doi.org/10.1016/j.cels.2017.01.002

Article  CAS  Google Scholar 

Danzer KM, Kranich LR, Ruf WP, Cagsal-Getkin O, Winslow AR, Zhu L, Vanderburg CR, McLean PJ (2012) Exosomal cell-to-cell transmission of alpha synuclein oligomers. Mol Neurodegener 7:42. https://doi.org/10.1186/1750-1326-7-42

Article  CAS  PubMed  PubMed Central  Google Scholar 

Del Campo N, Phillips O, Ory-Magne F, Brefel-Courbon C, Galitzky M, Thalamas C, Narr KL, Joshi S, Singh MK, Péran P et al (2021) Broad white matter impairment in multiple system atrophy. Hum Brain Mapp 42:357–366. https://doi.org/10.1002/hbm.25227

Article  PubMed  Google Scholar 

Djelloul M, Holmqvist S, Boza-Serrano A, Azevedo C, Yeung MS, Goldwurm S, Frisén J, Deierborg T, Roybon L (2015) Alpha-synuclein expression in the oligodendrocyte lineage: an in vitro and in vivo study using rodent and human models. Stem Cell Rep 5:174–184. https://doi.org/10.1016/j.stemcr.2015.07.002

Article  CAS  Google Scholar 

El-Agnaf OM, Salem SA, Paleologou KE, Curran MD, Gibson MJ, Court JA, Schlossmacher MG, Allsop D (2006) Detection of oligomeric forms of alpha-synuclein protein in human plasma as a potential biomarker for Parkinson’s disease. FASEB J 20:419–425. https://doi.org/10.1096/fj.03-1449com

Article  CAS  PubMed  Google Scholar 

Emmanouilidou E, Melachroinou K, Roumeliotis T, Garbis SD, Ntzouni M, Margaritis LH, Stefanis L, Vekrellis K (2010) Cell-produced alpha-synuclein is secreted in a calcium-dependent manner by exosomes and impacts neuronal survival. J Neurosci 30:6838–6851. https://doi.org/10.1523/JNEUROSCI.5699-09.2010

Article  CAS  PubMed  PubMed Central  Google Scholar 

Fil D, DeLoach A, Yadav S, Alkam D, MacNicol M, Singh A, Compadre CM, Goellner JJ, O’Brien CA, Fahmi T et al (2017) Mutant Profilin1 transgenic mice recapitulate cardinal features of motor neuron disease. Hum Mol Genet 26:686–701. https://doi.org/10.1093/hmg/ddw429

Article  CAS  PubMed  Google Scholar 

Geertsma HM, Fisk ZA, Sauline L, Prigent A, Kurgat K, Callaghan SM, Arenkiel BR, Mollenhauer B, Schlossmacher MG, Stadelmann C et al (2024) A topographical atlas of α-synuclein dosage and cell type-specific expression in adult mouse brain and peripheral organs. npj Parkinson’s Disease 10:65. https://doi.org/10.1038/s41531-024-00672-8

Article  CAS  PubMed  PubMed Central  Google Scholar 

Goedert M, Jakes R, Spillantini MG (2017) The Synucleinopathies: Twenty Years On. J Parkinsons Dis 7:S51–S69. https://doi.org/10.3233/JPD-179005

Article  PubMed  PubMed Central  Google Scholar 

Gomes DE, Witwer KW (2022) L1CAM-associated extracellular vesicles: a systematic review of nomenclature, sources, separation, and characterization. J Extracell Biol 1(3):e13. https://doi.org/10.1002/jex2.35

Article  CAS  Google Scholar 

Hallacli E, Kayatekin C, Nazeen S, Wang XH, Sheinkopf Z, Sathyakumar S, Sarkar S, Jiang X, Dong X, Di Maio R et al (2022) The Parkinson’s disease protein alpha-synuclein is a modulator of processing bodies and mRNA stability. Cell 185(2035–2056):e2033. https://doi.org/10.1016/j.cell.2022.05.008

Article  CAS  Google Scholar 

Holfeld A, Schuster D, Sesterhenn F, Gillingham AK, Stalder P, Haenseler W, Barrio-Hernandez I, Ghosh D, Vowles J, Cowley SA et al (2024) Systematic identification of structure-specific protein-protein interactions. Mol Syst Biol 20:651–675. https://doi.org/10.1038/s44320-024-00037-6

Article  PubMed  PubMed Central  Google Scholar 

Ingre C, Landers JE, Rizik N, Volk AE, Akimoto C, Birve A, Hubers A, Keagle PJ, Piotrowska K, Press R et al (2013) A novel phosphorylation site mutation in profilin 1 revealed in a large screen of US, Nordic, and German amyotrophic lateral sclerosis/frontotemporal dementia cohorts. Neurobiol Ag 34(1708):e1701-1706. https://doi.org/10.1016/j.neurobiolaging.2012.10.009

Article  CAS  Google Scholar 

Jenner P, Dexter DT, Sian J, Schapira AH, Marsden CD (1992) Oxidative stress as a cause of nigral cell death in Parkinson’s disease and incidental Lewy body disease. The royal kings and queens parkinson’s disease research group. Ann Neurol 32:S82-87. https://doi.org/10.1002/ana.410320714

Article  CAS  PubMed  Google Scholar 

Kang M-G, Rhee H-W (2022) Molecular spatiomics by proximity labeling. Acc Chem Res 55:1411–1422. https://doi.org/10.1021/acs.accounts.2c00061

Article  CAS  PubMed  PubMed Central  Google Scholar 

Kawashima Y, Kodera Y, Singh A, Matsumoto M, Matsumoto H (2014) Efficient extraction of proteins from formalin-fixed paraffin-embedded tissues requires higher concentration of tris(hydroxymethyl)aminomethane. Clin Proteom 11:4. https://doi.org/10.1186/1559-0275-11-4

Article  CAS  Google Scholar 

Killinger BA, Madaj Z, Sikora JW, Rey N, Haas AJ, Vepa Y, Lindqvist D, Chen H, Thomas PM, Brundin P et al (2018) The vermiform appendix impacts the risk of developing Parkinson’s disease. Sci Transl Med 10(465):eaar5280. https://doi.org/10.1126/scitranslmed.aar5280

Article  CAS  PubMed  PubMed Central  Google Scholar 

Killinger BA, Marshall LL, Chatterjee D, Chu Y, Bras J, Guerreiro R, Kordower JH (2022) In situ proximity labeling identifies Lewy pathology molecular interactions in the human brain. Proc Natl Acad Sci USA 119:e2114405119. https://doi.org/10.1073/pnas.2114405119

Comments (0)

No login
gif