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Glial phagocytic clearance in Parkinson’s disease

Tremblay, Marie-Eve, Cookson, Mark R., Civiero, Laura·2019·Molecular Neurodegeneration

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  • In astrocytes, LRRK2 plays a role in ciliogenesis.

    “In astrocytes, LRRK2 plays a role in ciliogenesis [15, 30, 35, 84].”

    From Cellular and subcellular localization of Rab10 and phospho-T73 Rab10 in the mouse and human brain (2023) · cites this paper as [84]

    The Background section on endolysosomal dysfunction says LRRK2 affects lysosomal function in astrocytes, but does not address ciliogenesis. Searches for astrocyte ciliogenesis and primary cilia found no passage in our copy supporting that specific role; no page number is available for the section. (LLM, conf=0.72)

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  1. Langston JW. The Parkinson’s complex: parkinsonism is just the tip of the iceberg. Ann Neurol. 2006;59:591–6 Available from: http://doi.wiley.com/10.1002/ana.20834 [cited 2018 Dec 6]. · DOI
  2. Singleton AB, Hardy JA, Gasser T. The Birth of the Modern Era of Parkinson’s Disease Genetics. J Parkinsons Dis. 2017;7:S87–93 Available from: http://www.ncbi.nlm.nih.gov/pubmed/28282818 [cited 2018 Dec 5]. · DOI
  3. Dickson DW. Parkinson’s disease and parkinsonism: neuropathology. Cold Spring Harb Perspect Med 2012;2. Available from: http://www.ncbi.nlm.nih.gov/pubmed/22908195 . [cited 2017 Jun 28] · DOI · Paper page
  4. Braak H, Del Tredici K, Rüb U, de Vos RAI, Jansen Steur ENH, Braak E. Staging of brain pathology related to sporadic Parkinson’s disease. Neurobiol Aging. 24:197–211 Available from: http://www.ncbi.nlm.nih.gov/pubmed/12498954 . [cited 2018 Dec 5]. · DOI · Paper page
  5. Wakabayashi K, Hayashi S, Yoshimoto M, Kudo H, Takahashi H. NACP/alpha-synuclein-positive filamentous inclusions in astrocytes and oligodendrocytes of Parkinson’s disease brains. Acta Neuropathol. 2000;99:14–20 Available from: http://www.ncbi.nlm.nih.gov/pubmed/10651022 . [cited 2018 Dec 5]. · DOI
  6. Croisier E, Graeber MB. Glial degeneration and reactive gliosis in alpha-synucleinopathies: the emerging concept of primary gliodegeneration. Acta Neuropathol. 2006;112:517–30 Available from: http://link.springer.com/10.1007/s00401-006-0119-z [cited 2018 Dec 5]. · DOI
  7. Reemst K, Noctor SC, Lucassen PJ, Hol EM. The Indispensable Roles of Microglia and Astrocytes during Brain Development. Front Hum Neurosci. 2016;10:566 Available from: http://journal.frontiersin.org/article/10.3389/fnhum.2016.00566/full [cited 2018 Dec 6]. · DOI · Paper page
  8. Weinhard L, di Bartolomei G, Bolasco G, Machado P, Schieber NL, Neniskyte U, et al. Microglia remodel synapses by presynaptic trogocytosis and spine head filopodia induction. Nat Commun. 2018;9:1228 Available from: http://www.nature.com/articles/s41467-018-03566-5 [cited 2018 Dec 6]. · DOI · Paper page
  9. Salter MW, Beggs S. Sublime microglia: expanding roles for the guardians of the CNS. Cell. 2014;158:15–24 Available from: https://linkinghub.elsevier.com/retrieve/pii/S0092867414007296 [cited 2018 Dec 6]. · DOI · Paper page
  10. Stevens B, Schafer DP. Roles of microglia in nervous system development, plasticity, and disease. Dev Neurobiol. 2018;78:559–60 Available from: http://doi.wiley.com/10.1002/dneu.22594 [cited 2018 Dec 6]. · DOI
  11. Bellesi M, de Vivo L, Chini M, Gilli F, Tononi G, Cirelli C. Sleep Loss Promotes Astrocytic Phagocytosis and Microglial Activation in Mouse Cerebral Cortex. J Neurosci. 2017;37:5263–73 Available from: http://www.ncbi.nlm.nih.gov/pubmed/28539349 [cited 2018 Dec 6]. · DOI
  12. Yun SP, Kam T-I, Panicker N, Kim S, Oh Y, Park J-S, et al. Block of A1 astrocyte conversion by microglia is neuroprotective in models of Parkinson’s disease. Nat Med. 2018;24:931–8 Available from: http://www.ncbi.nlm.nih.gov/pubmed/29892066 [cited 2018 Dec 6]. · DOI · Paper page
  13. Jha MK, Jo M, Kim J-H, Suk K. Microglia-Astrocyte Crosstalk: An Intimate Molecular Conversation. Neuroscientist. 2018:1073858418783959 Available from: http://journals.sagepub.com/doi/10.1177/1073858418783959 [cited 2018 Dec 6]. · DOI · Paper page
  14. Tian L, Ma L, Kaarela T, Li Z. Neuroimmune crosstalk in the central nervous system and its significance for neurological diseases. J Neuroinflammation. 2012;9:155 Available from: http://jneuroinflammation.biomedcentral.com/articles/10.1186/1742-2094-9-155 [cited 2018 Dec 6]. · DOI
  15. Chavarría C, Rodríguez-Bottero S, Quijano C, Cassina P, Souza JM. Impact of monomeric, oligomeric and fibrillar alpha-synuclein on astrocyte reactivity and toxicity to neurons. Biochem J. 2018;475:3153–69 Available from: http://www.ncbi.nlm.nih.gov/pubmed/30185433 [cited 2018 Dec 6]. · DOI
  16. Booth HDE, Hirst WD, Wade-Martins R. The Role of Astrocyte Dysfunction in Parkinson’s Disease Pathogenesis. Trends Neurosci. 2017;40:358–70 Available from: http://linkinghub.elsevier.com/retrieve/pii/S0166223617300681 [cited 2017 Jun 26]. · DOI · Paper page
  17. Bourdenx M, Dehay B. What lysosomes actually tell us about Parkinson’s disease? Ageing Res Rev. 2016;32:140–9 Available from: http://www.ncbi.nlm.nih.gov/pubmed/26947123 [cited 2017 Jun 26]. · DOI · Paper page
  18. Tofaris GK. Lysosome-dependent pathways as a unifying theme in Parkinson’s disease. Mov Disord. 2012;27:1364–9 Available from: http://www.ncbi.nlm.nih.gov/pubmed/22927213 [cited 2018 Dec 6]. · DOI
  19. Arandjelovic S, Ravichandran KS. Phagocytosis of apoptotic cells in homeostasis. Nat Immunol. 2015;16:907–17 Available from: http://www.ncbi.nlm.nih.gov/pubmed/26287597 [cited 2018 Dec 6]. · DOI · Paper page
  20. Morizawa YM, Hirayama Y, Ohno N, Shibata S, Shigetomi E, Sui Y, et al. Reactive astrocytes function as phagocytes after brain ischemia via ABCA1-mediated pathway. Nat Commun. 2017;8:28 Available from: http://www.ncbi.nlm.nih.gov/pubmed/28642575 . [cited 2018 Dec 6]. · DOI
  21. Wakida NM, Cruz GMS, Ro CC, Moncada EG, Khatibzadeh N, Flanagan LA, et al. Phagocytic response of astrocytes to damaged neighboring cells. Deli MA, editor. PLoS One. 2018;13:e0196153 Available from: https://dx.plos.org/10.1371/journal.pone.0196153 . [cited 2018 Dec 6]. · DOI
  22. Paolicelli RC, Bisht K, Tremblay M-Ã. Fractalkine regulation of microglial physiology and consequences on the brain and behavior. Front Cell Neurosci. 2014;8:129 Available from: http://www.ncbi.nlm.nih.gov/pubmed/24860431 . [cited 2018 Dec 6]. · DOI
  23. Okun E, Mattson MP, Arumugam TV. Involvement of Fc receptors in disorders of the central nervous system. Neuromolecular Med. 2010;12:164–78 Available from: http://link.springer.com/10.1007/s12017-009-8099-5 . [cited 2018 Dec 6]. · DOI
  24. Neniskyte U, Gross CT. Errant gardeners: glial-cell-dependent synaptic pruning and neurodevelopmental disorders. Nat Rev Neurosci. 2017;18:658–70 Available from: http://www.ncbi.nlm.nih.gov/pubmed/28931944 . [cited 2018 Dec 6]. · DOI
  25. Kielian T. Toll-like receptors in central nervous system glial inflammation and homeostasis. J Neurosci Res. 2006;83:711–30 Available from: http://doi.wiley.com/10.1002/jnr.20767 . [cited 2019 Mar 5]. · DOI
  26. Gurley C, Nichols J, Liu S, Phulwani NK, Esen N, Kielian T. Microglia and Astrocyte Activation by Toll-Like Receptor Ligands: Modulation by PPAR-gamma Agonists. PPAR Res. 2008;2008:453120 Available from: http://www.hindawi.com/journals/ppar/2008/453120/ . [cited 2019 Mar 5]. · DOI
  27. Marinelli C, Di Liddo R, Facci L, Bertalot T, Conconi MT, Zusso M, et al. Ligand engagement of Toll-like receptors regulates their expression in cortical microglia and astrocytes. J Neuroinflammation. 2015;12:244 Available from: http://www.jneuroinflammation.com/content/12/1/244 . [cited 2019 Mar 5]. · DOI
  28. El-Hage N, Podhaizer EM, Sturgill J, Hauser KF. Toll-like receptor expression and activation in astroglia: differential regulation by HIV-1 Tat, gp120, and morphine. Immunol Invest. 2011;40:498–522 Available from: http://www.tandfonline.com/doi/full/10.3109/08820139.2011.561904 . [cited 2019 Mar 5]. · DOI
  29. Caron E, Hall A. Identification of two distinct mechanisms of phagocytosis controlled by different Rho GTPases. Science. 1998;282:1717–21 Available from: http://www.ncbi.nlm.nih.gov/pubmed/9831565 . [cited 2018 Dec 6]. · DOI · Paper page
  30. Münz C. Autophagy Proteins in Phagocyte Endocytosis and Exocytosis. Front Immunol. 2017;8:1183 Available from: http://www.ncbi.nlm.nih.gov/pubmed/29018446 . [cited 2018 Dec 6]. · DOI
  31. Niedergang F, Grinstein S. How to build a phagosome: new concepts for an old process. Curr Opin Cell Biol. 2018;50:57–63 Available from: https://linkinghub.elsevier.com/retrieve/pii/S0955067417301540 . [cited 2018 Dec 6]. · DOI
  32. Fazeli G, Wehman AM. Safely removing cell debris with LC3-associated phagocytosis. Biol cell. 2017;109:355–63 Available from: http://doi.wiley.com/10.1111/boc.201700028 . [cited 2018 Dec 6]. · DOI
  33. Huang J, Canadien V, Lam GY, Steinberg BE, Dinauer MC, Magalhaes MAO, et al. Activation of antibacterial autophagy by NADPH oxidases. Proc Natl Acad Sci. 2009;106:6226–31 Available from: http://www.ncbi.nlm.nih.gov/pubmed/19339495 . [cited 2018 Dec 6]. · DOI · Paper page
  34. Seto S, Tsujimura K, Koide Y. Rab GTPases regulating phagosome maturation are differentially recruited to mycobacterial phagosomes. Traffic. 2011;12:407–20 Available from: http://doi.wiley.com/10.1111/j.1600-0854.2011.01165.x . [cited 2018 Dec 6]. · DOI
  35. Pauwels A-M, Trost M, Beyaert R, Hoffmann E. Patterns, Receptors, and Signals: Regulation of Phagosome Maturation. Trends Immunol. 2017;38:407–22 Available from: https://linkinghub.elsevier.com/retrieve/pii/S1471490617300571 . [cited 2018 Dec 6]. · DOI
  36. Colonna M, Wang Y. TREM2 variants: new keys to decipher Alzheimer disease pathogenesis. Nat Rev Neurosci. 2016;17:201–7 Available from: http://www.nature.com/articles/nrn.2016.7 . [cited 2018 Dec 6]. · DOI · Paper page
  37. Chan G, White CC, Winn PA, Cimpean M, Replogle JM, Glick LR, et al. Trans-pQTL study identifies immune crosstalk between Parkinson and Alzheimer loci. Neurol Genet. 2016;2:e90 Available from: http://ng.neurology.org/lookup/doi/10.1212/NXG.0000000000000090 . [cited 2018 Dec 6]. · DOI
  38. Zhang Y, Feng S, Nie K, Li Y, Gao Y, Gan R, et al. TREM2 modulates microglia phenotypes in the neuroinflammation of Parkinson’s disease. Biochem Biophys Res Commun. 2018;499:797–802 Available from: https://linkinghub.elsevier.com/retrieve/pii/S0006291X18307599 . [cited 2018 Dec 6]. · DOI
  39. Yin J, Liu X, He Q, Zhou L, Yuan Z, Zhao S. Vps35-dependent recycling of Trem2 regulates microglial function. Traffic. 2016;17:1286–96 Available from: http://doi.wiley.com/10.1111/tra.12451 . [cited 2018 Dec 6]. · DOI · Paper page
  40. Vilariño-Güell C, Wider C, Ross OA, Dachsel JC, Kachergus JM, Lincoln SJ, et al. VPS35 Mutations in Parkinson Disease. Am J Hum Genet. 2011;89:162–7 Available from: http://www.ncbi.nlm.nih.gov/pubmed/21763482 . [cited 2018 Dec 6]. · DOI · Paper page
  41. Mengel D, Thelen M, Balzer-Geldsetzer M, Söling C, Bach J-P, Schaeffer E, et al. TREM2 rare variant p.R47H is not associated with Parkinson’s disease. Parkinsonism Relat Disord. 2016;23:109–11 Available from: https://linkinghub.elsevier.com/retrieve/pii/S1353802015300493 . [cited 2018 Dec 6];. · DOI
  42. Joers V, Tansey MG, Mulas G, Carta AR. Microglial phenotypes in Parkinson’s disease and animal models of the disease. Prog Neurobiol. 2017;155:57–75 Available from: https://linkinghub.elsevier.com/retrieve/pii/S0301008215300538 . [cited 2018 Dec 6]. · DOI · Paper page
  43. Aono H, Choudhury ME, Higaki H, Miyanishi K, Kigami Y, Fujita K, et al. Microglia may compensate for dopaminergic neuron loss in experimental Parkinsonism through selective elimination of glutamatergic synapses from the subthalamic nucleus. Glia. 2017;65:1833–47 Available from: http://doi.wiley.com/10.1002/glia.23199 . [cited 2018 Dec 6]. · DOI
  44. Emmrich JV, Hornik TC, Neher JJ, Brown GC. Rotenone induces neuronal death by microglial phagocytosis of neurons. FEBS J. 2013;280:5030–8 Available from: http://doi.wiley.com/10.1111/febs.12401 . [cited 2018 Dec 6]. · DOI
  45. Depboylu C, Stricker S, Ghobril J-P, Oertel WH, Priller J, Höglinger GU. Brain-resident microglia predominate over infiltrating myeloid cells in activation, phagocytosis and interaction with T-lymphocytes in the MPTP mouse model of Parkinson disease. Exp Neurol. 2012;238:183–91 Available from: https://linkinghub.elsevier.com/retrieve/pii/S0014488612003299 . [cited 2018 Dec 6]. · DOI
  46. Barcia C, Ros CM, Ros-Bernal F, Gómez A, Annese V, Carrillo-de Sauvage MA, et al. Persistent phagocytic characteristics of microglia in the substantia nigra of long-term Parkinsonian macaques. J Neuroimmunol. 2013;261:60–6 Available from: https://linkinghub.elsevier.com/retrieve/pii/S0165572813001331 . [cited 2018 Dec 6]. · DOI
  47. Sherer TB, Betarbet R, Kim JH, Greenamyre JT. Selective microglial activation in the rat rotenone model of Parkinson’s disease. Neurosci Lett. 2003;341:87–90 Available from: http://www.ncbi.nlm.nih.gov/pubmed/12686372 . [cited 2018 Dec 6]. · DOI
  48. Loeffler DA, Camp DM, Conant SB. Complement activation in the Parkinson’s disease substantia nigra: an immunocytochemical study. J Neuroinflammation. 2006;3:29 Available from: http://jneuroinflammation.biomedcentral.com/articles/10.1186/1742-2094-3-29 . [cited 2018 Dec 6]. · DOI
  49. Bodea L-G, Wang Y, Linnartz-Gerlach B, Kopatz J, Sinkkonen L, Musgrove R, et al. Neurodegeneration by activation of the microglial complement-phagosome pathway. J Neurosci. 2014;34:8546–56 Available from: http://www.jneurosci.org/cgi/doi/10.1523/JNEUROSCI.5002-13.2014 . [cited 2018 Dec 6]. · DOI · Paper page
  50. Park J-Y, Paik SR, Jou I, Park SM. Microglial phagocytosis is enhanced by monomeric alpha-synuclein, not aggregated alpha-synuclein: implications for Parkinson’s disease. Glia. 2008;56:1215–23 Available from: http://doi.wiley.com/10.1002/glia.20691 . [cited 2018 Dec 6]. · DOI
  51. Luk KC, Kehm VM, Zhang B, O’Brien P, Trojanowski JQ, VMY L. Intracerebral inoculation of pathological α-synuclein initiates a rapidly progressive neurodegenerative α-synucleinopathy in mice. J Exp Med. 2012;209:975–86 Available from: http://www.jem.org/lookup/doi/10.1084/jem.20112457 . [cited 2018 Dec 6]. · DOI
  52. Volpicelli-Daley L, Brundin P. Prion-like propagation of pathology in Parkinson disease. Handb Clin Neurol. 2018;153:321–35 Available from: https://linkinghub.elsevier.com/retrieve/pii/B9780444639455000179 . [cited 2018 Dec 6]. · DOI
  53. Choi YR, Kang S-J, Kim J-M, Lee S-J, Jou I, Joe E-H, et al. FcγRIIB mediates the inhibitory effect of aggregated α-synuclein on microglial phagocytosis. Neurobiol Dis. 2015;83:90–9 Available from: https://linkinghub.elsevier.com/retrieve/pii/S0969996115300450 . [cited 2018 Dec 6]. · DOI
  54. Haenseler W, Zambon F, Lee H, Vowles J, Rinaldi F, Duggal G, et al. Excess α-synuclein compromises phagocytosis in iPSC-derived macrophages. Sci Rep. 2017;7:9003 Available from: http://www.nature.com/articles/s41598-017-09362-3 . [cited 2018 Dec 6]. · DOI
  55. Härtlova A, Herbst S, Peltier J, Rodgers A, Bilkei-Gorzo O, Fearns A, et al. LRRK2 is a negative regulator of Mycobacterium tuberculosis phagosome maturation in macrophages. EMBO J. 2018;37:e98694 Available from: http://emboj.embopress.org/lookup/doi/10.15252/embj.201798694 . [cited 2018 Dec 6]. · DOI
  56. Ma B, Xu L, Pan X, Sun L, Ding J, Xie C, et al. LRRK2 modulates microglial activity through regulation of chemokine (C-X3-C) receptor 1 -mediated signalling pathways. Hum Mol Genet. 2016;25:3515–23 Available from: https://academic.oup.com/hmg/article-lookup/doi/10.1093/hmg/ddw194 . [cited 2018 Dec 6]. · DOI
  57. Milior G, Lecours C, Samson L, Bisht K, Poggini S, Pagani F, et al. Fractalkine receptor deficiency impairs microglial and neuronal responsiveness to chronic stress. Brain Behav Immun. 2016;55:114–25 Available from: https://linkinghub.elsevier.com/retrieve/pii/S0889159115004195 . [cited 2018 Dec 6]. · DOI
  58. Bonifati V, Rizzu P, van Baren MJ, Schaap O, Breedveld GJ, Krieger E, et al. Mutations in the DJ-1 Gene Associated with Autosomal Recessive Early-Onset Parkinsonism. Science. 2003;299:256–9 Available from: http://www.ncbi.nlm.nih.gov/pubmed/12446870 . [cited 2019 Mar 5]. · DOI
  59. Trudler D, Weinreb O, Mandel SA, Youdim MBH, Frenkel D. DJ-1 deficiency triggers microglia sensitivity to dopamine toward a pro-inflammatory phenotype that is attenuated by rasagiline. J Neurochem. 2014;129:434–47 Available from: http://doi.wiley.com/10.1111/jnc.12633 . [cited 2019 Mar 5]. · DOI
  60. Nash Y, Schmukler E, Trudler D, Pinkas-Kramarski R, Frenkel D. DJ-1 deficiency impairs autophagy and reduces alpha-synuclein phagocytosis by microglia. J Neurochem. 2017;143:584–94 Available from: http://doi.wiley.com/10.1111/jnc.14222 . [cited 2019 Mar 5]. · DOI · Paper page
  61. Du C, Wang Y, Zhang F, Yan S, Guan Y, Gong X, et al. Synaptotagmin-11 inhibits cytokine secretion and phagocytosis in microglia. Glia. 2017;65:1656–67 Available from: http://doi.wiley.com/10.1002/glia.23186 . [cited 2018 Dec 6]. · DOI
  62. Colombo E, Farina C. Astrocytes: Key Regulators of Neuroinflammation. Trends Immunol. 2016;37:608–20 Available from: https://linkinghub.elsevier.com/retrieve/pii/S1471490616300722 . [cited 2019 Mar 5]. · DOI
  63. Berbel P, Innocenti GM. The development of the corpus callosum in cats: A light- and electron- microscopic study. J Comp Neurol. 1988;276:132–56 Available from: http://www.ncbi.nlm.nih.gov/pubmed/3192762 . [cited 2018 Dec 6]. · DOI
  64. Jung Y-J, Chung W-S. Phagocytic Roles of Glial Cells in Healthy and Diseased Brains. Biomol Ther (Seoul). 2018;26:350–7 Available from: http://www.ncbi.nlm.nih.gov/pubmed/29316776 . [cited 2018 Dec 6]. · DOI · Paper page
  65. Wu H-H, Bellmunt E, Scheib JL, Venegas V, Burkert C, Reichardt LF, et al. Glial precursors clear sensory neuron corpses during development via Jedi-1, an engulfment receptor. Nat Neurosci. 2009;12:1534–41 Available from: http://www.ncbi.nlm.nih.gov/pubmed/19915564 . [cited 2018 Dec 6]. · DOI
  66. Iram T, Ramirez-Ortiz Z, Byrne MH, Coleman UA, Kingery ND, Means TK, et al. Megf10 Is a Receptor for C1Q That Mediates Clearance of Apoptotic Cells by Astrocytes. J Neurosci. 2016;36:5185–92 Available from: http://www.jneurosci.org/lookup/doi/10.1523/JNEUROSCI.3850-15.2016 . [cited 2018 Dec 6]. · DOI
  67. MacDonald JM, Beach MG, Porpiglia E, Sheehan AE, Watts RJ, Freeman MR. The Drosophila Cell Corpse Engulfment Receptor Draper Mediates Glial Clearance of Severed Axons. Neuron. 2006;50:869–81 Available from: http://www.ncbi.nlm.nih.gov/pubmed/16772169 . [cited 2018 Dec 6]. · DOI · Paper page
  68. Awasaki T, Tatsumi R, Takahashi K, Arai K, Nakanishi Y, Ueda R, et al. Essential role of the apoptotic cell engulfment genes draper and ced-6 in programmed axon pruning during Drosophila metamorphosis. Neuron. 2006;50:855–67 Available from: http://linkinghub.elsevier.com/retrieve/pii/S0896627306003187 . [cited 2018 Dec 6]. · DOI
  69. Ray A, Speese SD, Logan MA. Glial Draper Rescues Aβ Toxicity in a Drosophila Model of Alzheimer’s Disease. J Neurosci. 2017;37:11881–93 Available from: http://www.jneurosci.org/lookup/doi/10.1523/JNEUROSCI.0862-17.2017 . [cited 2018 Dec 6]. · DOI
  70. Bellesi M, de Vivo L, Tononi G, Cirelli C. Transcriptome profiling of sleeping, waking, and sleep deprived adult heterozygous Aldh1L1–eGFP-L10a mice. Genomics Data. 2015;6:114–7 Available from: http://www.ncbi.nlm.nih.gov/pubmed/26413480 . [cited 2018 Dec 6]. · DOI
  71. Zamanian JL, Xu L, Foo LC, Nouri N, Zhou L, Giffard RG, et al. Genomic analysis of reactive astrogliosis. J Neurosci. 2012;32:6391–410 Available from: http://www.jneurosci.org/cgi/doi/10.1523/JNEUROSCI.6221-11.2012 . [cited 2018 Dec 6]. · DOI · Paper page
  72. Clark DPQ, Perreau VM, Shultz SR, Brady RD, Lei E, Dixit S, et al. Inflammation in Traumatic Brain Injury: Roles for Toxic A1 Astrocytes and Microglial-Astrocytic Crosstalk. Neurochem Res. 2019; Available from: http://link.springer.com/10.1007/s11064-019-02721-8 . [cited 2019 Mar 5]. · DOI
  73. Morales I, Sanchez A, Rodriguez-Sabate C, Rodriguez M. Striatal astrocytes engulf dopaminergic debris in Parkinson’s disease: A study in an animal model. PLoS One. 2017;12:e0185989 Available from: http://www.ncbi.nlm.nih.gov/pubmed/29028815 . [cited 2018 Dec 6]. · DOI
  74. Loria F, Vargas JY, Bousset L, Syan S, Salles A, Melki R, et al. α-Synuclein transfer between neurons and astrocytes indicates that astrocytes play a role in degradation rather than in spreading. Acta Neuropathol. 2017;134:789–808 Available from: http://link.springer.com/10.1007/s00401-017-1746-2 . [cited 2017 Dec 20]. · DOI
  75. Mori F, Tanji K, Yoshimoto M, Takahashi H, Wakabayashi K. Demonstration of alpha-synuclein immunoreactivity in neuronal and glial cytoplasm in normal human brain tissue using proteinase K and formic acid pretreatment. Exp Neurol. 2002;176:98–104 Available from: http://www.ncbi.nlm.nih.gov/pubmed/12093086 . [cited 2017 Jun 27]. · DOI
  76. Gustafsson G, Lööv C, Persson E, Lázaro DF, Takeda S, Bergström J, et al. Secretion and Uptake of α-Synuclein Via Extracellular Vesicles in Cultured Cells. Cell Mol Neurobiol. 2018;38:1539–50 Available from: http://link.springer.com/10.1007/s10571-018-0622-5 . [cited 2019 Mar 5]. · DOI
  77. Terada S, Ishizu H, Yokota O, Tsuchiya K, Nakashima H, Ishihara T, et al. Glial involvement in diffuse Lewy body disease. Acta Neuropathol. 2003;105:163–9 Available from: http://www.ncbi.nlm.nih.gov/pubmed/12536227 . [cited 2019 Mar 5]. · DOI
  78. Braak H, Sastre M, Del Tredici K. Development of α-synuclein immunoreactive astrocytes in the forebrain parallels stages of intraneuronal pathology in sporadic Parkinson’s disease. Acta Neuropathol. 2007;114:231–41 Available from: http://www.ncbi.nlm.nih.gov/pubmed/17576580 . [cited 2018 Dec 5]. · DOI · Paper page
  79. Vargas JY, Grudina C, Zurzolo C. The prion-like spreading of α-synuclein: From in vitro to in vivo models of Parkinson’s disease. Ageing Res Rev. 2019;50:89–101 Available from: https://linkinghub.elsevier.com/retrieve/pii/S1568163718302617 . [cited 2019 Mar 5]. · DOI
  80. Singleton AB, Farrer MJ, Bonifati V. The genetics of Parkinson’s disease: Progress and therapeutic implications. Mov Disord. 2013;28:14–23 Available from: http://www.ncbi.nlm.nih.gov/pubmed/23389780 . [cited 2017 Jun 26]. · DOI
  81. Schreij AMA, Fon EA, McPherson PS. Endocytic membrane trafficking and neurodegenerative disease. Cell Mol Life Sci. 2016;73:1529–45 Available from: http://link.springer.com/10.1007/s00018-015-2105-x . [cited 2018 Dec 6]. · DOI
  82. Di Fonzo A, Chien HF, Socal M, Giraudo S, Tassorelli C, Iliceto G, et al. ATP13A2 missense mutations in juvenile parkinsonism and young onset Parkinson disease. Neurology. 2007;68:1557–62 Available from: http://www.neurology.org/cgi/doi/10.1212/01.wnl.0000260963.08711.08 . [cited 2018 Dec 6]. · DOI
  83. Ramirez A, Heimbach A, Gründemann J, Stiller B, Hampshire D, Cid LP, et al. Hereditary parkinsonism with dementia is caused by mutations in ATP13A2, encoding a lysosomal type 5 P-type ATPase. Nat Genet. 2006;38:1184–91 Available from: http://www.nature.com/articles/ng1884 . [cited 2018 Dec 6]. · DOI · Paper page
  84. Murphy KE, Cottle L, Gysbers AM, Cooper AA, Halliday GM. ATP13A2 (PARK9) protein levels are reduced in brain tissue of cases with Lewy bodies. Acta Neuropathol Commun. 2013;1:11 Available from: http://actaneurocomms.biomedcentral.com/articles/10.1186/2051-5960-1-11 . [cited 2018 Dec 6]. · DOI
  85. Dehay B, Ramirez A, Martinez-Vicente M, Perier C, Canron M-H, Doudnikoff E, et al. Loss of P-type ATPase ATP13A2/PARK9 function induces general lysosomal deficiency and leads to Parkinson disease neurodegeneration. Proc Natl Acad Sci U S A. 2012;109:9611–6 Available from: http://www.pnas.org/cgi/doi/10.1073/pnas.1112368109 . [cited 2018 Dec 6]. · DOI
  86. Usenovic M, Knight AL, Ray A, Wong V, Brown KR, Caldwell GA, et al. Identification of novel ATP13A2 interactors and their role in α-synuclein misfolding and toxicity. Hum Mol Genet. 2012;21:3785–94 Available from: https://academic.oup.com/hmg/article-lookup/doi/10.1093/hmg/dds206 . [cited 2018 Dec 6]. · DOI
  87. Kong SMY, Chan BKK, Park J-S, Hill KJ, Aitken JB, Cottle L, et al. Parkinson’s disease-linked human PARK9/ATP13A2 maintains zinc homeostasis and promotes α-Synuclein externalization via exosomes. Hum Mol Genet. 2014;23:2816–33 Available from: https://academic.oup.com/hmg/article-lookup/doi/10.1093/hmg/ddu099 . [cited 2018 Dec 6]. · DOI
  88. Grünewald A, Arns B, Seibler P, Rakovic A, Münchau A, Ramirez A, et al. ATP13A2 mutations impair mitochondrial function in fibroblasts from patients with Kufor-Rakeb syndrome. Neurobiol Aging. 2012;33:1843.e1–7 Available from: https://linkinghub.elsevier.com/retrieve/pii/S019745801100580X . [cited 2018 Dec 6]. · DOI
  89. Ramonet D, Podhajska A, Stafa K, Sonnay S, Trancikova A, Tsika E, et al. PARK9-associated ATP13A2 localizes to intracellular acidic vesicles and regulates cation homeostasis and neuronal integrity. Hum Mol Genet. 2012;21:1725–43 Available from: https://academic.oup.com/hmg/article-lookup/doi/10.1093/hmg/ddr606 . [cited 2018 Dec 6]. · DOI
  90. Lopes da Fonseca T, Pinho R, Outeiro TF. A familial ATP13A2 mutation enhances alpha-synuclein aggregation and promotes cell death. Hum Mol Genet. 2016;25:2959–71 Available from: https://academic.oup.com/hmg/article-lookup/doi/10.1093/hmg/ddw147 . [cited 2018 Dec 7]. · DOI
  91. Kett LR, Stiller B, Bernath MM, Tasset I, Blesa J, Jackson-Lewis V, et al. α-Synuclein-independent histopathological and motor deficits in mice lacking the endolysosomal Parkinsonism protein Atp13a2. J Neurosci. 2015;35:5724–42 Available from: http://www.jneurosci.org/cgi/doi/10.1523/JNEUROSCI.0632-14.2015 . [cited 2018 Dec 6]. · DOI
  92. Qiao C, Yin N, Gu H-Y, Zhu J-L, Ding J-H, Lu M, et al. Atp13a2 Deficiency Aggravates Astrocyte-Mediated Neuroinflammation via NLRP3 Inflammasome Activation. CNS Neurosci Ther. 2016;22:451–60 Available from: http://doi.wiley.com/10.1111/cns.12514 . [cited 2018 Dec 6]. · DOI
  93. Magalhaes J, Gegg ME, Migdalska-Richards A, Doherty MK, Whitfield PD, Schapira AHV. Autophagic lysosome reformation dysfunction in glucocerebrosidase deficient cells: relevance to Parkinson disease. Hum Mol Genet. 2016;25:3432–45 Available from: https://academic.oup.com/hmg/article-lookup/doi/10.1093/hmg/ddw185 . [cited 2018 Dec 6]. · DOI
  94. Papadopoulos VE, Nikolopoulou G, Antoniadou I, Karachaliou A, Arianoglou G, Emmanouilidou E, et al. Modulation of β-glucocerebrosidase increases α-synuclein secretion and exosome release in mouse models of Parkinson’s disease. Hum Mol Genet. 2018;27:1696–710 Available from: https://academic.oup.com/hmg/advance-article/doi/10.1093/hmg/ddy075/4935073 . [cited 2018 Dec 6]. · DOI
  95. Wong K, Sidransky E, Verma A, Mixon T, Sandberg GD, Wakefield LK, et al. Neuropathology provides clues to the pathophysiology of Gaucher disease. Mol Genet Metab. 2004;82:192–207 Available from: http://linkinghub.elsevier.com/retrieve/pii/S1096719204001179 . [cited 2018 Dec 6]. · DOI
  96. Ginns EI, Mak SK-K, Ko N, Karlgren J, Akbarian S, Chou VP, et al. Neuroinflammation and α-synuclein accumulation in response to glucocerebrosidase deficiency are accompanied by synaptic dysfunction. Mol Genet Metab. 2014;111:152–62 Available from: https://linkinghub.elsevier.com/retrieve/pii/S1096719213004150 . [cited 2018 Dec 6]. · DOI
  97. Aflaki E, Borger DK, Grey RJ, Kirby M, Anderson S, Lopez G, et al. Efferocytosis is impaired in Gaucher macrophages. Haematologica. 2017;102:656–65 Available from: http://www.haematologica.org/lookup/doi/10.3324/haematol.2016.155093 . [cited 2018 Dec 6]. · DOI
  98. Osellame LD, Rahim AA, Hargreaves IP, Gegg ME, Richard-Londt A, Brandner S, et al. Mitochondria and quality control defects in a mouse model of Gaucher disease--links to Parkinson’s disease. Cell Metab. 2013;17:941–53 Available from: https://linkinghub.elsevier.com/retrieve/pii/S1550413113001575 . [cited 2018 Dec 6]. · DOI
  99. Zimprich A, Biskup S, Leitner P, Lichtner P, Farrer M, Lincoln S, et al. Mutations in LRRK2 cause autosomal-dominant parkinsonism with pleomorphic pathology. Neuron. 2004;44:601–7 Available from: http://linkinghub.elsevier.com/retrieve/pii/S0896627304007202 . [cited 2017 Jun 29]. · DOI
  100. Paisán-Ruiz C, Lewis PA, Singleton AB. LRRK2: cause, risk, and mechanism. J Parkinsons Dis. 2013;3:85–103 Available from: http://www.ncbi.nlm.nih.gov/pubmed/23938341 . [cited 2017 Jun 29]. · DOI
  101. Lesage S, Dürr A, Tazir M, Lohmann E, Leutenegger A-L, Janin S, et al. LRRK2 G2019S as a cause of Parkinson’s disease in North African Arabs. N Engl J Med. 2006;354:422–3 Available from: http://www.nejm.org/doi/abs/10.1056/NEJMc055540 . [cited 2017 Jun 29]. · DOI · Paper page
  102. Roosen DA, Cookson MR. LRRK2 at the interface of autophagosomes, endosomes and lysosomes. Mol Neurodegener. 2016;11:73 Available from: http://www.ncbi.nlm.nih.gov/pubmed/27927216 . [cited 2017 Jun 26]. · DOI
  103. Steger M, Diez F, Dhekne HS, Lis P, Nirujogi RS, Karayel O, et al. Systematic proteomic analysis of LRRK2-mediated Rab GTPase phosphorylation establishes a connection to ciliogenesis. Elife. 2017;6 Available from: https://elifesciences.org/articles/31012 . [cited 2018 Dec 6]. · DOI · Paper page
  104. Steger M, Tonelli F, Ito G, Davies P, Trost M, Vetter M, Wachter S, Lorentzen E, Duddy G, Wilson S, Baptista MA, Fiske BK, Fell MJ, Morrow JA, Reith AD, Alessi DR, Mann M. Phosphoproteomics reveals that Parkinson's disease kinase LRRK2 regulates a subset of Rab GTPases. Elife. 2016;29(5):e12813. https://doi.org/10.7554/eLife.12813 . · DOI · Paper page
  105. Herzig MC, Kolly C, Persohn E, Theil D, Schweizer T, Hafner T, et al. LRRK2 protein levels are determined by kinase function and are crucial for kidney and lung homeostasis in mice. Hum Mol Genet. 2011;20:4209–23 Available from: https://academic.oup.com/hmg/article-lookup/doi/10.1093/hmg/ddr348 . [cited 2017 May 15]. · DOI
  106. Tong Y, Giaime E, Yamaguchi H, Ichimura T, Liu Y, Si H, et al. Loss of leucine-rich repeat kinase 2 causes age-dependent bi-phasic alterations of the autophagy pathway. Mol Neurodegener. 2012;7:2 Available from: http://www.ncbi.nlm.nih.gov/pubmed/22230652 . [cited 2017 Jun 26]. · DOI
  107. Miklavc P, Ehinger K, Thompson KE, Hobi N, Shimshek DR, Frick M. Surfactant secretion in LRRK2 knock-out rats: changes in lamellar body morphology and rate of exocytosis. PLoS One. 2014;9:e84926 Available from: http://www.ncbi.nlm.nih.gov/pubmed/24465451 . · DOI
  108. Fuji RN, Flagella M, Baca MS, Baptista MA, Brodbeck J, Chan BK, et al. Effect of selective LRRK2 kinase inhibition on nonhuman primate lung. Sci Transl Med. 2015;7:273ra15 Available from: http://www.ncbi.nlm.nih.gov/pubmed/25653221 . [cited 2017 Jun 26]. · DOI
  109. Pellegrini L, Hauser DN, Li Y, Mamais A, Beilina A, Kumaran R, et al. Proteomic analysis reveals co-ordinated alterations in protein synthesis and degradation pathways in LRRK2 knockout mice. Hum Mol Genet. 2018;27:3257–71 Available from: https://academic.oup.com/hmg/article/27/18/3257/5039882 . [cited 2018 Dec 6]. · DOI
  110. Sánchez-Danás A, Richaud-Patin Y, Carballo-Carbajal I, Jimánez-Delgado S, Caig C, Mora S, et al. Disease-specific phenotypes in dopamine neurons from human iPS-based models of genetic and sporadic Parkinson’s disease. EMBO Mol Med. 2012;4:380–95 Available from: http://www.ncbi.nlm.nih.gov/pubmed/22407749 . [cited 2017 Jun 26]. · DOI
  111. Schapansky J, Khasnavis S, DeAndrade MP, Nardozzi JD, Falkson SR, Boyd JD, et al. Familial knockin mutation of LRRK2 causes lysosomal dysfunction and accumulation of endogenous insoluble α-synuclein in neurons. Neurobiol Dis. 2018;111:26–35 Available from: http://www.ncbi.nlm.nih.gov/pubmed/29246723 . [cited 2018 Dec 6]. · DOI
  112. Sharma S, Bandopadhyay R, Lashley T, Renton AEM, Kingsbury AE, Kumaran R, et al. LRRK2 expression in idiopathic and G2019S positive Parkinson’s disease subjects: a morphological and quantitative study. Neuropathol Appl Neurobiol. 2011;37:777–90 Available from: http://doi.wiley.com/10.1111/j.1365-2990.2011.01187.x . [cited 2017 Jun 26]. · DOI
  113. MacLeod DA, Rhinn H, Kuwahara T, Zolin A, Di Paolo G, McCabe BD, et al. RAB7L1 interacts with LRRK2 to modify intraneuronal protein sorting and Parkinson’s disease risk. Neuron. 2013;77:425–39 Available from: https://linkinghub.elsevier.com/retrieve/pii/S0896627312011208 . [cited 2018 Dec 6]. · DOI · Paper page
  114. Beilina A, Rudenko IN, Kaganovich A, Civiero L, Chau H, Kalia SK, et al. Unbiased screen for interactors of leucine-rich repeat kinase 2 supports a common pathway for sporadic and familial Parkinson disease. Proc Natl Acad Sci U S A. 2014;111:2626–31 Available from: http://www.pnas.org/cgi/doi/10.1073/pnas.1318306111 . [cited 2018 Jun 25]. · DOI · Paper page
  115. Liu Z, Bryant N, Kumaran R, Beilina A, Abeliovich A, Cookson MR, et al. LRRK2 phosphorylates membrane-bound Rabs and is activated by GTP-bound Rab7L1 to promote recruitment to the trans-Golgi network. Hum Mol Genet. 2018;27:385–95 Available from: https://academic.oup.com/hmg/article/27/2/385/4644526 . [cited 2018 Dec 6]. · DOI · Paper page
  116. Gómez-Suaga P, Rivero-Ríos P, Fdez E, Blanca Ramírez M, Ferrer I, Aiastui A, et al. LRRK2 delays degradative receptor trafficking by impeding late endosomal budding through decreasing Rab7 activity. Hum Mol Genet. 2014;23:6779–96 Available from: https://academic.oup.com/hmg/article-lookup/doi/10.1093/hmg/ddu395 . [cited 2018 Dec 6]. · DOI · Paper page
  117. Mir R, Tonelli F, Lis P, Macartney T, Polinski NK, Martinez TN, et al. The Parkinson’s disease VPS35[D620N] mutation enhances LRRK2-mediated Rab protein phosphorylation in mouse and human. Biochem J. 2018;475:1861–83 Available from: http://www.ncbi.nlm.nih.gov/pubmed/29743203 . [cited 2018 Dec 6]. · DOI · Paper page
  118. Zhao Y, Perera G, Takahashi-Fujigasaki J, Mash DC, Vonsattel JPG, Uchino A, et al. Reduced LRRK2 in association with retromer dysfunction in post-mortem brain tissue from LRRK2 mutation carriers. Brain. 2018;141:486–95 Available from: http://www.ncbi.nlm.nih.gov/pubmed/29253086 . [cited 2018 Dec 6]. · DOI · Paper page
  119. Williams ET, Chen X, Moore DJ. VPS35, the Retromer Complex and Parkinson’s Disease. J Parkinsons Dis. 2017;7:219–33 Available from: http://www.ncbi.nlm.nih.gov/pubmed/28222538 . [cited 2018 Dec 6]. · DOI
  120. Kim MJ, Deng H-X, Wong YC, Siddique T, Krainc D. The Parkinson’s disease-linked protein TMEM230 is required for Rab8a-mediated secretory vesicle trafficking and retromer trafficking. Hum Mol Genet. 2017;26:729–41 Available from: https://academic.oup.com/hmg/article-lookup/doi/10.1093/hmg/ddw413 . [cited 2018 Dec 6]. · DOI
  121. Lee C, Guo J, Zeng W, Kim S, She J, Cang C, et al. The lysosomal potassium channel TMEM175 adopts a novel tetrameric architecture. Nature. 2017;547:472–5 Available from: http://www.nature.com/doifinder/10.1038/nature23269 . [cited 2018 Dec 6]. · DOI
  122. Jinn S, Drolet RE, Cramer PE, Wong AH-K, Toolan DM, Gretzula CA, et al. TMEM175 deficiency impairs lysosomal and mitochondrial function and increases α-synuclein aggregation. Proc Natl Acad Sci U S A. 2017;114:2389–94 Available from: http://www.pnas.org/lookup/doi/10.1073/pnas.1616332114 . [cited 2018 Dec 6]. · DOI
  123. Cang C, Aranda K, Seo Y, Gasnier B, Ren D. TMEM175 Is an Organelle K(+) Channel Regulating Lysosomal Function. Cell. 2015;162:1101–12 Available from: https://linkinghub.elsevier.com/retrieve/pii/S0092867415009782 . [cited 2018 Dec 6]. · DOI

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Metadata

Authors
Tremblay, M.-E., Cookson, M. R., & Civiero, L.
Venue
Molecular Neurodegeneration
Published
2019-04-05
Volume
14
Issue
1
ISSN
1750-1326
Cited by
152
References
41
Language
en
Funders
Università degli Studi di Padova (180425)

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