Let’s make microglia great again in neurodegenerative disorders

Aguzzi A, Rajendran L (2009) The transcellular spread of cytosolic amyloids, prions, and prionoids. Neuron 64:783–790. doi:10.1016/j.neuron.2009.12.016 PubMedCrossRef

Alais S, Simoes S, Baas D et al (2008) Mouse neuroblastoma cells release prion infectivity associated with exosomal vesicles. Biol Cell 100:603–615. doi:10.1042/BC20080025 PubMedCrossRef

Alam Q, Alam MZ, Mushtaq G et al (2016) Inflammatory process in Alzheimer’s and Parkinson’s Diseases: central role of cytokines. Curr Pharm Des 22:541–548PubMedCrossRef

Alvarez-Erviti L, Couch Y, Richardson J et al (2011a) Alpha-synuclein release by neurons activates the inflammatory response in a microglial cell line. Neurosci Res 69:337–342. doi:10.1016/j.neures.2010.12.020 PubMedCrossRef

Alvarez-Erviti L, Seow Y, Schapira AH et al (2011b) Lysosomal dysfunction increases exosome-mediated alpha-synuclein release and transmission. Neurobiol Disease 42:360–367. doi:10.1016/j.nbd.2011.01.029 CrossRef

Alvarez-Erviti L, Seow Y, Yin H et al (2011c) Delivery of siRNA to the mouse brain by systemic injection of targeted exosomes. Nat Biotechnol 29:341–345. doi:10.1038/nbt.1807 PubMedCrossRef

Anand PK, Anand E, Bleck CKE et al (2010) Exosomal Hsp70 induces a pro-inflammatory response to foreign particles including mycobacteria. PLoS One 5:e10136. doi:10.1371/journal.pone.0010136 PubMedPubMedCentralCrossRef

Andreasson KI, Bachstetter AD, Colonna M et al (2016) Targeting innate immunity for neurodegenerative disorders of the central nervous system. J Neurochem 138(5):653–693. doi:10.1111/jnc.13667 PubMedPubMedCentralCrossRef

Angelopoulos P, Agouridaki H, Vaiopoulos H et al (2008) Cytokines in Alzheimer’s disease and vascular dementia. Int J Neurosci 118:1659–1672. doi:10.1080/00207450701392068 PubMedCrossRef

Annunziata P, Volpi N (1985) High levels of C3c in the cerebrospinal fluid from amyotrophic lateral sclerosis patients. Acta Neurol Scand 72(1):61–64PubMedCrossRef

Antonucci F, Turola E, Riganti L et al (2012) Microvesicles released from microglia stimulate synaptic activity via enhanced sphingolipid metabolism. EMBO J 31:1231–1240. doi:10.1038/emboj.2011.489 PubMedPubMedCentralCrossRef

Apelt J, Schliebs R (2001) Beta-amyloid-induced glial expression of both pro- and anti-inflammatory cytokines in cerebral cortex of aged transgenic Tg2576 mice with Alzheimer plaque pathology. Brain Res 894:21–30. doi:10.1016/S0006-8993(00)03176-0 PubMedCrossRef

Arends YM, Duyckaerts C, Rozemuller JM et al (2000) Microglia, amyloid and dementia in alzheimer disease. A correlative study. Neurobiology 21:39–47. doi:10.1016/S0197-4580(00)00094-4 CrossRef

Arimoto T, Choi D-Y, Lu X et al (2007) Interleukin-10 protects against inflammation-mediated degeneration of dopaminergic neurons in substantia nigra. Neurobiology 28:894–906. doi:10.1016/j.neurobiolaging.2006.04.011 CrossRef

Arnold JE, Tipler C, Laszlo L et al (1995) The abnormal isoform of the prion protein accumulates in late-endosome-like organelles in scrapie-infected mouse brain. J Pathol 176:403–411. doi:10.1002/path.1711760412 PubMedCrossRef

Arosio B, Trabattoni D, Galimberti L et al (2004) Interleukin-10 and interleukin-6 gene polymorphisms as risk factors for Alzheimer’s disease. Neurobiology 25:1009–1015. doi:10.1016/j.neurobiolaging.2003.10.009 CrossRef

Asai H, Ikezu S, Tsunoda S et al (2015) Depletion of microglia and inhibition of exosome synthesis halt tau propagation. Nat Neurosci 18:1584–1593. doi:10.1038/nn.4132 PubMedPubMedCentralCrossRef

Asselineau D, Benlhassan K, Arosio B et al (2015) Interleukin-10 production in response to amyloid-β differs between slow and fast decliners in patients with Alzheimer’s Disease. J Alzheimer’s Disease 46:837–842. doi:10.3233/JAD-142832 CrossRef

Bahia El Idrissi N, Bosch S, Ramaglia V et al (2016) Complement activation at the motor end-plates in amyotrophic lateral sclerosis. J Neuroinflammation 13(1):72. doi:10.1186/s12974-016-0538-2 PubMedPubMedCentralCrossRef

Balducci C, Frasca A, Zotti M et al (2017) Toll-like receptor 4-dependent glial cell activation mediates the impairment in memory establishment induced by β-amyloid oligomers in an acute mouse model of Alzheimer’s disease. Brain Behav Immun 60:188–197. doi:10.1016/j.bbi.2016.10.012 PubMedCrossRef

Banati RB, Daniel SE, Blunt SB (1998) Glial pathology but absence of apoptotic nigral neurons in long-standing Parkinson’s disease. Mov Disord 13:221–227. doi:10.1002/mds.870130205 PubMedCrossRef

Bellingham SA, Coleman BM, Hill AF (2012) Small RNA deep sequencing reveals a distinct miRNA signature released in exosomes from prion-infected neuronal cells. Nucleic Acids Res 40:10937–10949. doi:10.1093/nar/gks832 PubMedPubMedCentralCrossRef

Benitez BA, Jin SC, Guerreiro R et al (2014) Missense variant in TREML2 protects against Alzheimer’s disease. Neurobiology 35(1510):e19–e26. doi:10.1016/j.neurobiolaging.2013.12.010 CrossRef

Berjaoui S, Povedano M, Garcia-Esparcia P et al (2015) Complex inflammation mRNA-related response in ALS Is region dependent. Neural Plast 2015:573784. doi:10.1155/2015/573784 PubMedPubMedCentralCrossRef

Betmouni S, Perry VH (1999) The acute inflammatory response in CNS following injection of prion brain homogenate or normal brain homogenate. Neuropathol Appl Neurobiol 25:20–28. doi:10.1046/j.1365-2990.1999.00153.x PubMedCrossRef

Betmouni S, Perry VH, Gordon JL (1996) Evidence for an early inflammatory response in the central nervous system of mice with scrapie. Neuroscience 74:1–5. doi:10.1016/0306-4522(96)00212-6 PubMedCrossRef

Béraud D, Maguire-Zeiss KA (2012) Misfolded α-synuclein and Toll-like receptors: therapeutic targets for Parkinson’s disease. Parkinsonism Relat Disord 18(Suppl 1):S17–S20. doi:10.1016/S1353-8020(11)70008-6 PubMedPubMedCentralCrossRef

Béraud D, Twomey M, Bloom B et al (2011) α-Synuclein alters toll-like receptor expression. Front Neurosci 5:80. doi:10.3389/fnins.2011.00080 PubMedPubMedCentralCrossRef

Bialecka M, Klodowska-Duda G, Kurzawski M et al (2008) Interleukin-10 (IL10) and tumor necrosis factor alpha (TNF) gene polymorphisms in Parkinson’s disease patients. Parkinsonism Relat Disord 14:636–640. doi:10.1016/j.parkreldis.2008.02.001 PubMedCrossRef

Bialecka M, Klodowska-Duda G, Kurzawski M et al (2007) Interleukin-10 gene polymorphism in Parkinson’s disease patients. Arch Med Res 38:858–863. doi:10.1016/j.arcmed.2007.06.006 PubMedCrossRef

Bliederhaeuser C, Grozdanov V, Speidel A et al (2016) Age-dependent defects of alpha-synuclein oligomer uptake in microglia and monocytes. Acta Neuropathol 131:379–391. doi:10.1007/s00401-015-1504-2 PubMedCrossRef

Bobrie A, Colombo M, Raposo G, Théry C (2011) Exosome secretion: molecular mechanisms and roles in immune responses. Traffic 12:1659–1668. doi:10.1111/j.1600-0854.2011.01225.x PubMedCrossRef

Boillée S, Yamanaka K, Lobsiger CS et al (2006) Onset and progression in inherited ALS determined by motor neurons and microglia. Science 312:1389–1392. doi:10.1126/science.1123511 PubMedCrossRef

Bolmont T, Haiss F, Eicke D et al (2008) Dynamics of the microglial/amyloid interaction indicate a role in plaque maintenance. J Neurosci 28:4283–4292. doi:10.1523/JNEUROSCI.4814-07.2008 PubMedPubMedCentralCrossRef

Bornemann KD, Wiederhold KH, Pauli C et al (2001) Abeta-induced inflammatory processes in microglia cells of APP23 transgenic mice. Am J Pathol 158:63–73. doi:10.1016/S0002-9440(10)63945-4 PubMedPubMedCentralCrossRef

Braak H, Del Tredici K (2016) Potential Pathways of Abnormal Tau and α-Synuclein Dissemination in Sporadic Alzheimer“s and Parkinson”s Diseases. Cold Spring Harb Perspect Biol. doi:10.1101/cshperspect.a023630 PubMedCrossRef

Bradshaw EM, Chibnik LB, Keenan BT et al (2013) CD33 Alzheimer’s disease locus: altered monocyte function and amyloid biology. Nat Neurosci 16:848–850. doi:10.1038/nn.3435 PubMedPubMedCentralCrossRef

Bradt BM, Kolb WP, Cooper NR (1998) Complement-dependent proinflammatory properties of the Alzheimer’s disease beta-peptide. J Exp Med 188:431–438. doi:10.1084/jem.188.3.431 PubMedPubMedCentralCrossRef

Brochard V, Combadière B, Prigent A et al (2009) Infiltration of CD4+ lymphocytes into the brain contributes to neurodegeneration in a mouse model of Parkinson disease. J Clin Investig 119:182–192. doi:10.1172/JCI36470 PubMedCrossRef

Brodacki B, Staszewski J, Toczyłowska B et al (2008) Serum interleukin (IL-2, IL-10, IL-6, IL-4), TNFalpha, and INFgamma concentrations are elevated in patients with atypical and idiopathic parkinsonism. Neurosci Lett 441:158–162. doi:10.1016/j.neulet.2008.06.040 PubMedCrossRef

Brubaker WD, Crane A, Johansson JU et al (2017) Peripheral complement interactions with amyloid β peptide: erythrocyte clearance mechanisms. Alzheimers Dement S1552–5260(17):30149–30158. doi:10.1016/j.jalz.2017.03.010 CrossRef

Bulloj A, Leal MC, Xu H et al (2010) Insulin-degrading enzyme sorting in exosomes: a secretory pathway for a key brain amyloid-beta degrading protease. J Alzheimers Disease 19:79–95. doi:10.3233/JAD-2010-1206 CrossRef

Butovsky O, Jedrychowski MP, Cialic R et al (2015) Targeting miR-155 restores abnormal microglia and attenuates disease in SOD1 mice. Ann Neurol 77:75–99. doi:10.1002/ana.24304 PubMedCrossRef

Cady J, Koval ED, Benitez BA et al (2014) TREM2 variant p. R47H as a risk factor for sporadic amyotrophic lateral sclerosis. JAMA Neurol 71:449–453. doi:10.1001/jamaneurol.2013.6237 PubMedPubMedCentralCrossRef

Cagnin A, Kassiou M, Meikle SR, Banati RB (2006) In vivo evidence for microglial activation in neurodegenerative dementia. Acta Neurol Scand Suppl 185:107–114. doi:10.1111/j.1600-0404.2006.00694.x PubMedCrossRef

Cameron B, Tse W, Lamb R et al (2012) Loss of interleukin receptor-associated kinase 4 signaling suppresses amyloid pathology and alters microglial phenotype in a mouse model of Alzheimer’s disease. J Neurosci 32:15112–15123. doi:10.1523/JNEUROSCI.1729-12.2012 PubMedPubMedCentralCrossRef

Carbutt S, Duff J, Yarnall A et al (2015) Variation in complement protein C1q is not a major contributor to cognitive impairment in Parkinson’s disease. Neurosci Lett 6(594):66–69. doi:10.1016/j.neulet.2015.03.048 CrossRef

Casula M, Iyer AM, Spliet WGM et al (2011) Toll-like receptor signaling in amyotrophic lateral sclerosis spinal cord tissue. Neuroscience 179:233–243. doi:10.1016/j.neuroscience.2011.02.001 PubMedCrossRef

Chakrabarty P, Li A, Ceballos-Diaz C et al (2015) IL-10 alters immunoproteostasis in APP mice, increasing plaque burden and worsening cognitive behavior. Neuron 85:519–533. doi:10.1016/j.neuron.2014.11.020 PubMedPubMedCentralCrossRef

Chan G, White CC, Winn PA et al (2015) CD33 modulates TREM2: convergence of Alzheimer loci. Nat Neurosci 18:1556–1558. doi:10.1038/nn.4126 PubMedPubMedCentralCrossRef

Chan G, White CC, Winn PA et al (2016) Trans-pQTL study identifies immune crosstalk between Parkinson and Alzheimer loci. Neurol Genet 2:e90. doi:10.1212/NXG.0000000000000090 PubMedPubMedCentralCrossRef

Chang C, Lang H, Geng N et al (2013) Exosomes of BV-2 cells induced by alpha-synuclein: important mediator of neurodegeneration in PD. Neurosci Lett 548:190–195. doi:10.1016/j.neulet.2013.06.009 PubMedCrossRef

Chao CC, Ala TA, Hu S et al (1994a) Serum cytokine levels in patients with Alzheimer’s disease. Clin Diagn Lab Immunol 1:433–436PubMedPubMedCentral

Chao CC, Hu S, Frey WH et al (1994b) Transforming growth factor beta in Alzheimer’s disease. Clin Diagn Lab Immunol 1:109–110PubMedPubMedCentral

Chen W, Abud EA, Yeung ST et al (2016) Increased tauopathy drives microglia-mediated clearance of beta-amyloid. Acta Neuropathol Commun 4:63. doi:10.1186/s40478-016-0336-1 PubMedPubMedCentralCrossRef

Chen X, Chen Y, Wei Q et al (2015) Assessment of TREM2 rs75932628 association with amyotrophic lateral sclerosis in a Chinese population. J Neurol Sci 355:193–195. doi:10.1016/j.jns.2015.05.010 PubMedCrossRef

Cheng L, Sharples RA, Scicluna BJ, Hill AF (2014a) Exosomes provide a protective and enriched source of miRNA for biomarker profiling compared to intracellular and cell-free blood. J Extracell Vesicles. doi:10.3402/jev.v3.23743 PubMedPubMedCentralCrossRef

Cheng L, Sun X, Scicluna BJ et al (2014b) Characterization and deep sequencing analysis of exosomal and non-exosomal miRNA in human urine. Kidney Int 86:433–444. doi:10.1038/ki.2013.502 PubMedCrossRef

Cho HJ, Liu G, Jin SM et al (2013) MicroRNA-205 regulates the expression of Parkinson’s disease-related leucine-rich repeat kinase 2 protein. Hum Mol Genet 22:608–620. doi:10.1093/hmg/dds470 PubMedCrossRef

Cogswell JP, Ward J, Taylor IA et al (2008) Identification of miRNA changes in Alzheimer’s disease brain and CSF yields putative biomarkers and insights into disease pathways. J Alzheimer’s Disease 14:27–41. doi:10.3233/JAD-2008-14103 CrossRef

Colangelo AM, Alberghina L, Papa M (2014) Astrogliosis as a therapeutic target for neurodegenerative diseases. Neurosci Lett 565:59–64. doi:10.1016/j.neulet.2014.01.014 PubMedCrossRef

Coleman BM, Hanssen E, Lawson VA, Hill AF (2012) Prion-infected cells regulate the release of exosomes with distinct ultrastructural features. FASEB J 26:4160–4173. doi:10.1096/fj.11-202077 PubMedCrossRef

Concannon RM, Okine BN, Finn DP et al (2015) Differential upregulation of the cannabinoid CB(2) receptor in neurotoxic and inflammation-driven rat models of Parkinson’s disease. Exp Neurol 269:133–141. doi:10.1016/j.expneurol.2015.04.007 PubMedCrossRef

Constam DB, Philipp J, Malipiero UV et al (1992) Differential expression of transforming growth factor-beta 1, -beta 2, and -beta 3 by glioblastoma cells, astrocytes, and microglia. J Immunol 148:1404–1410PubMed

Cookson MR (2009) α-Synuclein and neuronal cell death. Mol Neurodegener 4:9. doi:10.1186/1750-1326-4-9 PubMedPubMedCentralCrossRef

Couch Y, Alvarez-Erviti L, Sibson NR et al (2011) The acute inflammatory response to intranigral α-synuclein differs significantly from intranigral lipopolysaccharide and is exacerbated by peripheral inflammation. J Neuroinflammation 8:166. doi:10.1186/1742-2094-8-166 PubMedPubMedCentralCrossRef

Crane A, Brubaker WD, Johansson JU et al (2017) Peripheral complement interactions with amyloid β peptide in Alzheimer’s disease: 2. Relationship to Aβ immunotherapy. Alzheimers Dement S1552–5260(17):32898–32904. doi:10.1016/j.jalz.2017.04.015 CrossRef

Crehan H, Holton P, Wray S et al (2012) Complement receptor 1 (CR1) and Alzheimer's disease. Immunobiology 217(2):244–250. doi:10.1016/j.imbio.2011.07.017 PubMedCrossRef

Cunningham C, Boche D, Perry VH (2002) Transforming growth factor beta1, the dominant cytokine in murine prion disease: influence on inflammatory cytokine synthesis and alteration of vascular extracellular matrix. Neuropathol Appl Neurobiol 28(2):107–119. doi:10.1046/j.1365-2990.2002.00383.x PubMedCrossRef

Daniele SG, Béraud D, Davenport C et al (2015) Activation of MyD88-dependent TLR1/2 signaling by misfolded α-synuclein, a protein linked to neurodegenerative disorders. Sci Signal 8:ra45. doi:10.1126/scisignal.2005965 PubMedPubMedCentralCrossRef

Danzer KM, Kranich LR, Ruf WP et al (2012) Exosomal cell-to-cell transmission of alpha synuclein oligomers. Mol Neurodegener 7:42. doi:10.1186/1750-1326-7-42 PubMedPubMedCentralCrossRef

De Lucia C, Rinchon A, Olmos-Alonso A et al (2016) Microglia regulate hippocampal neurogenesis during chronic neurodegeneration. Brain Behav Immun 55:179–190. doi:10.1016/j.bbi.2015.11.001 PubMedPubMedCentralCrossRef

De Paola M, Sestito SE, Mariani A et al (2016) Synthetic and natural small molecule TLR4 antagonists inhibit motoneuron death in cultures from ALS mouse model. Pharmacol Res 103:180–187. doi:10.1016/j.phrs.2015.11.020 PubMedCrossRef

Deleidi M, Gasser T (2013) The role of inflammation in sporadic and familial Parkinson’s disease. Cell Mol Life Sci 70:4259–4273. doi:10.1007/s00018-013-1352-y PubMedCrossRef

Depboylu C, Du Y, Muller U et al (2003) Lack of association of interleukin-10 promoter region polymorphisms with Alzheimer’s disease. Neurosci Lett 342:132–134. doi:10.1016/S0304-3940(03)00231-3 PubMedCrossRef

Depboylu C, Schäfer MK, Arias-Carrión O et al (2011) Possible involvement of complement factor C1q in the clearance of extracellular neuromelanin from the substantia nigra in Parkinson disease. J Neuropathol Exp Neurol 70(2):125–132. doi:10.1097/NEN.0b013e31820805b9 PubMedCrossRef

Depboylu C, Stricker S, Ghobril J-P et al (2012) 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 238:183–191. doi:10.1016/j.expneurol.2012.08.020 PubMedCrossRef

Desplats P, Lee H-J, Bae E-J et al (2009) Inclusion formation and neuronal cell death through neuron-to-neuron transmission of alpha-synuclein. Proc Natl Acad Sci USA 106:13010–13015. doi:10.1073/pnas.0903691106 PubMedPubMedCentralCrossRef

Ding X, Ma M, Teng J et al (2015) Exposure to ALS-FTD-CSF generates TDP-43 aggregates in glioblastoma cells through exosomes and TNTs-like structure. Oncotarget 6:24178–24191. doi:10.18632/oncotarget.4680 PubMedPubMedCentralCrossRef

Doorn KJ, Moors T, Drukarch B et al (2014) Microglial phenotypes and toll-like receptor 2 in the substantia nigra and hippocampus of incidental Lewy body disease cases and Parkinson’s disease patients. Acta Neuropathol Commun 2:90. doi:10.1186/s40478-014-0090-1 PubMedPubMedCentralCrossRef

Doty KR, Guillot-Sestier M-V, Town T (2014) The role of the immune system in neurodegenerative disorders: adaptive or maladaptive? Brain Res. doi:10.1016/j.brainres.2014.09.008 PubMedPubMedCentralCrossRef

Drouin-Ouellet J, St-Amour I, Saint-Pierre M et al (2014) Toll-like receptor expression in the blood and brain of patients and a mouse model of Parkinson’s disease. Int J Neuropsychopharmacol. doi:10.1093/ijnp/pyu103 PubMedCrossRef

Dumestre-Perard C, Osmundson J, Lemaire-Vieille C et al (2007) Activation of classical pathway of complement cascade by soluble oligomers of prion. Cell Microbiol 9(12):2870–2879. doi:10.1111/j.1462-5822.2007.01002.x CrossRef

Dzamko N, Gysbers A, Perera G et al (2016) Toll-like receptor 2 is increased in neurons in Parkinson’s disease brain and may contribute to alpha-synuclein pathology. Acta Neuropathol. doi:10.1007/s00401-016-1648-8 PubMedPubMedCentralCrossRef

Edison P, Archer HA, Gerhard A et al (2008) Microglia, amyloid, and cognition in Alzheimer’s disease: an [11C](R)PK11195-PET and [11C]PIB-PET study. Neurobiol Disease 32:412–419. doi:10.1016/j.nbd.2008.08.001 CrossRef

Emmanouilidou E, Melachroinou K, Roumeliotis T et al (2010) Cell-produced alpha-synuclein is secreted in a calcium-dependent manner by exosomes and impacts neuronal survival. J Neurosci 30:6838–6851. doi:10.1523/JNEUROSCI.5699-09.2010 PubMedPubMedCentralCrossRef

Endo F, Komine O, Fujimori-Tonou N et al (2015) Astrocyte-derived TGF-β1 accelerates disease progression in ALS mice by interfering with the neuroprotective functions of microglia and T cells. Cell Rep 11:592–604. doi:10.1016/j.celrep.2015.03.053 PubMedCrossRef

Endo F, Yamanaka K (2015) Astrocytic TGF-β1: detrimental factor in ALS. Oncotarget 6:15728–15729. doi:10.18632/oncotarget.4786 PubMedPubMedCentralCrossRef

Escrevente C, Keller S, Altevogt P, Costa J (2011) Interaction and uptake of exosomes by ovarian cancer cells. BMC Cancer 11:108. doi:10.1186/1471-2407-11-108 PubMedPubMedCentralCrossRef

Espejo EF, Gonzalez-Albo MC, Moraes JP et al (2001) Functional regeneration in a rat Parkinson’s model after intrastriatal grafts of glial cell line-derived neurotrophic factor and transforming growth factor beta1-expressing extra-adrenal chromaffin cells of the Zuckerkandl’s organ. J Neurosci 21:9888–9895PubMedCrossRef

Fan R, Tenner AJ (2004) Complement C1q expression induced by Abeta in rat hippocampal organotypic slice cultures. Exp Neurol 185:241–253. doi:10.1016/j.expneurol.2003.09.023 PubMedCrossRef

Fassbender K, Walter S, Kuhl S et al (2004) The LPS receptor (CD14) links innate immunity with Alzheimer’s disease. FASEB J 18:203–205. doi:10.1096/fj.03-0364fje PubMedCrossRef

Fellner L, Irschick R, Schanda K et al (2013) Toll-like receptor 4 is required for α-synuclein dependent activation of microglia and astroglia. Glia 61:349–360. doi:10.1002/glia.22437 PubMedPubMedCentralCrossRef

Feng D, Zhao W-L, Ye Y-Y et al (2010) Cellular internalization of exosomes occurs through phagocytosis. Traffic 11:675–687. doi:10.1111/j.1600-0854.2010.01041.x PubMedCrossRef

Feng S-J, Nie K, Gan R et al (2014) Triggering receptor expressed on myeloid cells 2 variants are rare in Parkinson’s disease in a Han Chinese cohort. Neurobiology 35(1780):e11–e12. doi:10.1016/j.neurobiolaging.2014.01.142 CrossRef

Fernandez-Espejo E, Armengol JA, Flores JA et al (2005) Cells of the sympathoadrenal lineage: biological properties as donor tissue for cell-replacement therapies for Parkinson’s disease. Brain Res Brain Res Rev 49:343–354. doi:10.1016/j.brainresrev.2005.01.004 PubMedCrossRef

Fevrier B, Vilette D, Archer F et al (2004) Cells release prions in association with exosomes. Proc Natl Acad Sci USA 101:9683–9688. doi:10.1073/pnas.0308413101 PubMedPubMedCentralCrossRef

Finch CE, Laping NJ, Morgan TE et al (1993) TGF-beta 1 is an organizer of responses to neurodegeneration. J Cell Biochem 53:314–322. doi:10.1002/jcb.240530408 PubMedCrossRef

Finehout EJ, Franck Z, Lee KH (2005) Complement protein isoforms in CSF as possible biomarkers for neurodegenerative disease. Dis Markers 21(2005):93–101. doi:10.1155/2005/806573 PubMedPubMedCentralCrossRef

Fitzner D, Schnaars M, van Rossum D et al (2011) Selective transfer of exosomes from oligodendrocytes to microglia by macropinocytosis. J Cell Sci 124:447–458. doi:10.1242/jcs.074088 PubMedCrossRef

Frank S, Burbach GJ, Bonin M et al (2008) TREM2 is upregulated in amyloid plaque-associated microglia in aged APP23 transgenic mice. Glia 56:1438–1447. doi:10.1002/glia.20710 PubMedCrossRef

Frank S, Copanaki E, Burbach GJ et al (2009) Differential regulation of toll-like receptor mRNAs in amyloid plaque-associated brain tissue of aged APP23 transgenic mice. Neurosci Lett 453:41–44. doi:10.1016/j.neulet.2009.01.075 PubMedCrossRef

Frost B, Jacks RL, Diamond MI (2009) Propagation of tau misfolding from the outside to the inside of a cell. J Biol Chem 284:12845–12852. doi:10.1074/jbc.M808759200 PubMedPubMedCentralCrossRef

Fröhlich D, Kuo WP, Frühbeis C et al (2014) Multifaceted effects of oligodendroglial exosomes on neurons: impact on neuronal firing rate, signal transduction and gene regulation. Philos Trans R Soc Lond B Biol Sci. doi:10.1098/rstb.2013.0510 PubMedPubMedCentralCrossRef

Frühbeis C, Fröhlich D, Kuo WP et al (2013a) Neurotransmitter-triggered transfer of exosomes mediates oligodendrocyte-neuron communication. PLoS Biol 11:e1001604. doi:10.1371/journal.pbio.1001604 PubMedPubMedCentralCrossRef

Frühbeis C, Fröhlich D, Kuo WP, Krämer-Albers E-M (2013b) Extracellular vesicles as mediators of neuron-glia communication. Front Cell Neurosci 7:182. doi:10.3389/fncel.2013.00182 PubMedPubMedCentralCrossRef

Galan-Rodriguez B, del-Marco A, Flores JA et al (2008) Grafts of extra-adrenal chromaffin cells as aggregates show better survival rate and regenerative effects on parkinsonian rats than dispersed cell grafts. Neurobiol Disease 29:529–542. doi:10.1016/j.nbd.2007.11.009 CrossRef

Gate D, Rezai-Zadeh K, Jodry D et al (2010) Macrophages in Alzheimer’s disease: the blood-borne identity. J Neural Transm 117:961–970. doi:10.1007/s00702-010-0422-7 PubMedPubMedCentralCrossRef

Gezen-Ak D, Dursun E, Hanağası H et al (2013) BDNF, TNFα, HSP90, CFH, and IL-10 serum levels in patients with early or late onset Alzheimer’s disease or mild cognitive impairment. J Alzheimer’s Disease 37:185–195. doi:10.3233/JAD-130497 CrossRef

Ghaisas S, Maher J, Kanthasamy A (2016) Gut microbiome in health and disease: linking the microbiome-gut-brain axis and environmental factors in the pathogenesis of systemic and neurodegenerative diseases. Pharmacol Ther 158:52–62. doi:10.1016/j.pharmthera.2015.11.012 PubMedCrossRef

Giese A, Brown DR, Groschup MH et al (1998) Role of microglia in neuronal cell death in prion disease. Brain Pathol 8:449–457PubMedCrossRef

Glass CK, Saijo K, Winner B et al (2010) Mechanisms underlying inflammation in neurodegeneration. Cell 140:918–934. doi:10.1016/j.cell.2010.02.016 PubMedPubMedCentralCrossRef

Goedert M, Masuda-Suzukake M, Falcon B (2016) Like prions: the propagation of aggregated tau and α-synuclein in neurodegeneration. Brain. doi:10.1093/brain/aww230 PubMedCrossRef

Gomes C, Keller S, Altevogt P, Costa J (2007) Evidence for secretion of Cu, Zn superoxide dismutase via exosomes from a cell model of amyotrophic lateral sclerosis. Neurosci Lett 428:43–46. doi:10.1016/j.neulet.2007.09.024 PubMedCrossRef

Gonzalez-Aparicio R, Flores JA, Fernandez-Espejo E (2010) Antiparkinsonian trophic action of glial cell line-derived neurotrophic factor and transforming growth factor β1 is enhanced after co-infusion in rats. Exp Neurol 226:136–147. doi:10.1016/j.expneurol.2010.08.016 PubMedCrossRef

Grad LI, Pokrishevsky E, Silverman JM, Cashman NR (2014) Exosome-dependent and independent mechanisms are involved in prion-like transmission of propagated Cu/Zn superoxide dismutase misfolding. Prion 8:331–335. doi:10.4161/19336896.2014.983398 PubMedPubMedCentralCrossRef

Grasso M, Piscopo P, Confaloni A, Denti MA (2014) Circulating miRNAs as biomarkers for neurodegenerative disorders. Molecules 19:6891–6910. doi:10.3390/molecules19056891 PubMedCrossRef

Gravel M, Béland L-C, Soucy G et al (2016) IL-10 controls early microglial phenotypes and disease onset in ALS caused by misfolded superoxide dismutase 1. J Neurosci 36:1031–1048. doi:10.1523/JNEUROSCI.0854-15.2016 PubMedCrossRef

Graves MC, Fiala M, Dinglasan LAV et al (2004) Inflammation in amyotrophic lateral sclerosis spinal cord and brain is mediated by activated macrophages, mast cells and T cells. Amyotroph Lateral Scler Other Motor Neuron Disord 5:213–219PubMedCrossRef

Grey M, Dunning CJ, Gaspar R et al (2015) Acceleration of α-synuclein aggregation by exosomes. J Biol Chem 290:2969–2982. doi:10.1074/jbc.M114.585703 PubMedCrossRef

Griciuc A, Serrano-Pozo A, Parrado AR et al (2013) Alzheimer’s disease risk gene CD33 inhibits microglial uptake of amyloid beta. Neuron. doi:10.1016/j.neuron.2013.04.014 PubMedPubMedCentralCrossRef

Guerreiro R, Wojtas A, Bras J et al (2013) TREM2 variants in Alzheimer’s disease. N Engl J Med 368:117–127. doi:10.1056/NEJMoa1211851 PubMedCrossRef

Gui Y, Liu H, Zhang L et al (2015) Altered microRNA profiles in cerebrospinal fluid exosome in Parkinson disease and Alzheimer disease. Oncotarget 6:37043–37053. doi:10.18632/oncotarget.6158 PubMedPubMedCentralCrossRef

Guillot-Sestier M-V, Doty KR, Gate D et al (2015a) IL10 deficiency rebalances innate immunity to mitigate Alzheimer-like pathology. Neuron 85:534–548. doi:10.1016/j.neuron.2014.12.068 PubMedPubMedCentralCrossRef

Guillot-Sestier M-V, Doty KR, Town T (2015b) Innate immunity fights Alzheimer’s disease. Trends Neurosci 38:674–681. doi:10.1016/j.tins.2015.08.008 PubMedPubMedCentralCrossRef

Hannafon BN, Ding W-Q (2013) Intercellular communication by exosome-derived microRNAs in cancer. Int J Mol Sci 14:14240–14269. doi:10.3390/ijms140714240 PubMedPubMedCentralCrossRef

Harold D, Abraham R, Hollingworth P et al (2009) Genome-wide association study identifies variants at CLU and PICALM associated with Alzheimer’s disease. Nat Genet 41:1088–1093. doi:10.1038/ng.440 PubMedPubMedCentralCrossRef

Håkansson A, Westberg L, Nilsson S et al (2005) Investigation of genes coding for inflammatory components in Parkinson’s disease. Mov Disord 20:569–573. doi:10.1002/mds.20378 PubMedCrossRef

He X, Jing Z, Cheng G (2014) MicroRNAs: new regulators of Toll-like receptor signalling pathways. Biomed Res Int 2014:945169. doi:10.1155/2014/945169 PubMedPubMedCentralCrossRef

Hébert SS, Horré K, Nicolaï L et al (2008) Loss of microRNA cluster miR-29a/b-1 in sporadic Alzheimer’s disease correlates with increased BACE1/beta-secretase expression. Proc Natl Acad Sci USA 105:6415–6420. doi:10.1073/pnas.0710263105 PubMedPubMedCentralCrossRef

Heneka MT, Nadrigny F, Regen T et al (2010) Locus ceruleus controls Alzheimer’s disease pathology by modulating microglial functions through norepinephrine. Proc Natl Acad Sci USA 107:6058–6063. doi:10.1073/pnas.0909586107 PubMedPubMedCentralCrossRef

Heneka MT, Carson MJ, Khoury JE et al (2015) Neuroinflammation in Alzheimer’s disease. Lancet Neurol 14:388–405. doi:10.1016/S1474-4422(15)70016-5 PubMedCrossRefPubMedCentral

Henry CJ, Huang Y, Wynne AM, Godbout JP (2009) Peripheral lipopolysaccharide (LPS) challenge promotes microglial hyperactivity in aged mice that is associated with exaggerated induction of both pro-inflammatory IL-1beta and anti-inflammatory IL-10 cytokines. Brain Behav Immun 23:309–317. doi:10.1016/j.bbi.2008.09.002 PubMedCrossRef

Heppner FL, Prinz M, Aguzzi A (2001) Pathogenesis of prion diseases: possible implications of microglial cells. Prog Brain Res 132:737–750. doi:10.1016/S0079-6123(01)32114-3 PubMedCrossRef

Heppner FL, Ransohoff RM, Becher B (2015) Immune attack: the role of inflammation in Alzheimer disease. Nat Rev Neurosci 16:358–372. doi:10.1038/nrn3880 PubMedCrossRef

Heurich B, El Idrissi NB, Donev RM et al (2011) Complement upregulation and activation on motor neurons and neuromuscular junction in the SOD1 G93A mouse model of familial amyotrophic lateral sclerosis. J Neuroimmunol 235(1–2):104–109. doi:10.1016/j.jneuroim.2011.03.011 PubMedCrossRef

Hickman SE, Allison EK, El Khoury J (2008) Microglial dysfunction and defective beta-amyloid clearance pathways in aging Alzheimer’s disease mice. J Neurosci 28:8354–8360. doi:10.1523/JNEUROSCI.0616-08.2008 PubMedPubMedCentralCrossRef

Hirsch EC, Hunot S (2009) Neuroinflammation in Parkinson’s disease: a target for neuroprotection? Lancet Neurol 8:382–397. doi:10.1016/S1474-4422(09)70062-6 PubMedCrossRef

Hock E-M, Polymenidou M (2016) Prion-like propagation as a pathogenic principle in frontotemporal dementia. J Neurochem 138(Suppl 1):163–183. doi:10.1111/jnc.13668 PubMedCrossRef

Hollingworth P, Harold D, Sims R et al (2011) Common variants at ABCA7, MS4A6A/MS4A4E, EPHA1, CD33 and CD2AP are associated with Alzheimer’s disease. Nat Genet 43:429–435. doi:10.1038/ng.803 PubMedPubMedCentralCrossRef

Hondius DC, van Nierop P, Li KW et al (2016) Profiling the human hippocampal proteome at all pathologic stages of Alzheimer’s disease. Alzheimers Dement 12:654–668. doi:10.1016/j.jalz.2015.11.002 PubMedCrossRef

Hong S, Beja-Glasser VF, Nfonoyim BM et al (2016) Complement and microglia mediate early synapse loss in Alzheimer mouse models. Science 352:712–716. doi:10.1126/science.aad8373 PubMedPubMedCentralCrossRef

Hooten KG, Beers DR, Zhao W, Appel SH (2015) Protective and toxic neuroinflammation in amyotrophic lateral sclerosis. Neurotherapeutics 12:364–375. doi:10.1007/s13311-014-0329-3 PubMedPubMedCentralCrossRef

Houi K, Kobayashi T, Kato S et al (2002) Increased plasma TGF-beta1 in patients with amyotrophic lateral sclerosis. Acta Neurol Scand 106:299–301PubMedCrossRef

Iero M, Valenti R, Huber V et al (2008) Tumour-released exosomes and their implications in cancer immunity. Cell Death Differ 15:80–88. doi:10.1038/sj.cdd.4402237 PubMedCrossRef

Imamura K, Hishikawa N, Sawada M et al (2003) Distribution of major histocompatibility complex class II-positive microglia and cytokine profile of Parkinson’s disease brains. Acta Neuropathol 106:518–526. doi:10.1007/s00401-003-0766-2 PubMedCrossRef

Infante J, Garcia-Gorostiaga I, Sanchez-Juan P et al (2008) Inflammation-related genes and the risk of Parkinson’s disease: a multilocus approach. Eur J Neurol 15:431–433. doi:10.1111/j.1468-1331.2008.02092.x PubMedCrossRef

International Parkinson Disease Genomics Consortium, Nalls MA, Plagnol V et al (2011) Imputation of sequence variants for identification of genetic risks for Parkinson’s disease: a meta-analysis of genome-wide association studies. Lancet 377:641–649. doi: 10.1016/S0140-6736(10)62345-8

Ishii T, Haga S, Yagishita S, Tateishi J (1984) The presence of complements in amyloid plaques of Creutzfeldt–Jakob disease and Gerstmann–Straussler-Scheinker disease. Appl Pathol 2(6):370–379PubMed

Iwasaki Y, Ichikawa Y, Igarashi O et al (2003) Plasma TGFbeta1 in ALS patients. Acta Neurol Scand 108:221. doi:10.1034/j.1600-0404.2003.00164.x PubMedCrossRef

Iyer SS, Cheng G (2012) Role of interleukin 10 transcriptional regulation in inflammation and autoimmune disease. Crit Rev Immunol 32:23–63PubMedPubMedCentralCrossRef

Iłzecka J, Stelmasiak Z, Dobosz B (2002) Transforming growth factor-Beta 1 (tgf-Beta 1) in patients with amyotrophic lateral sclerosis. Cytokine 20:239–243. doi:10.1006/cyto.2002.2005 PubMedCrossRef

Jay TR, Hirsch AM, Broihier ML et al (2016) Disease progression-dependent effects of TREM2 deficiency in a mouse model of Alzheimer’s disease. J Neurosci. doi:10.1523/JNEUROSCI.2110-16.2016 CrossRef

Jay TR, Miller CM, Cheng PJ et al (2015) TREM2 deficiency eliminates TREM2+ inflammatory macrophages and ameliorates pathology in Alzheimer’s disease mouse models. J Exp Med 212:287–295. doi:10.1084/jem.20142322 PubMedPubMedCentralCrossRef

Jeffrey M, Halliday WG, Bell J et al (2000) Synapse loss associated with abnormal PrP precedes neuronal degeneration in the scrapie-infected murine hippocampus. Neuropathol Appl Neurobiol 26:41–54. doi:10.1046/j.1365-2990.2000.00216.x PubMedCrossRef

Jin J, Wu P, Li W et al (2014) Interleukin-10-1082A/G and -592C/A polymorphisms with risk of Parkinson’s disease: a meta-analysis. Int J Neurosci 124:852–858. doi:10.3109/00207454.2014.880910 PubMedCrossRef

Johnston H, Boutin H, Allan SM (2011) Assessing the contribution of inflammation in models of Alzheimer’s disease. Biochem Soc Trans 39:886–890. doi:10.1042/BST0390886 PubMedCrossRef

Johnston LC, Su X, Maguire-Zeiss K et al (2008) Human interleukin-10 gene transfer is protective in a rat model of Parkinson’s disease. Mol Ther 16:1392–1399. doi:10.1038/mt.2008.113 PubMedPubMedCentralCrossRef

Joniec-Maciejak I, Ciesielska A, Wawer A et al (2014) The influence of AAV2-mediated gene transfer of human IL-10 on neurodegeneration and immune response in a murine model of Parkinson’s disease. Pharmacol Rep 66:660–669. doi:10.1016/j.pharep.2014.03.008 PubMedCrossRef

Jonsson T, Stefansson H, Steinberg S et al (2013) Variant of TREM2 associated with the risk of Alzheimer’s disease. N Engl J Med 368:107–116. doi:10.1056/NEJMoa1211103 PubMedCrossRef

Junn E, Lee K-W, Jeong BS et al (2009) Repression of alpha-synuclein expression and toxicity by microRNA-7. Proc Natl Acad Sci USA 106:13052–13057. doi:10.1073/pnas.0906277106 PubMedPubMedCentralCrossRef

Kang S-G, Kim C, Cortez LM et al (2016) Toll-like receptor-mediated immune response inhibits prion propagation. Glia 64:937–951. doi:10.1002/glia.22973 PubMedCrossRef

Kim C, Ho D-H, Suk J-E et al (2013) Neuron-released oligomeric α-synuclein is an endogenous agonist of TLR2 for paracrine activation of microglia. Nat Commun 4:1562. doi:10.1038/ncomms2534 PubMedPubMedCentralCrossRef

Kim C, Lee H-J, Masliah E, Lee S-J (2016) Non-cell-autonomous neurotoxicity of α-synuclein Through microglial Toll-like receptor 2. Exp Neurobiol 25:113–119. doi:10.5607/en.2016.25.3.113 PubMedPubMedCentralCrossRef

Kingery ND, Ohsumi TK, Borowsky ML et al (2013) The microglial sensome revealed by direct RNA sequencing. Nat Neurosci. doi:10.1038/nn.3554 PubMedPubMedCentralCrossRef

Kinsella S, König H-G, Prehn JHM (2016) Bid promotes K63-linked polyubiquitination of tumor necrosis factor receptor associated factor 6 (TRAF6) and sensitizes to mutant SOD1-induced proinflammatory signaling in microglia. eNeuro. doi:10.1523/ENEURO.0099-15.2016 PubMedPubMedCentralCrossRef

Klein MA, Kaeser PS, Schwarz P et al (2001) Complement facilitates early prion pathogenesis. Nat Med 7(4):488–492. doi:10.1038/86567 PubMedCrossRef

Knöferle J, Ramljak S, Koch JC et al (2010) TGF-beta 1 enhances neurite outgrowth via regulation of proteasome function and EFABP. Neurobiol Disease 38:395–404. doi:10.1016/j.nbd.2010.02.011 CrossRef

Kokubo H, Saido TC, Iwata N et al (2005) Part of membrane-bound Abeta exists in rafts within senile plaques in Tg2576 mouse brain. Neurobiology 26:409–418. doi:10.1016/j.neurobiolaging.2004.04.008 CrossRef

Kong SMY, Chan BKK, Park J-S et al (2014) Parkinson’s disease-linked human PARK9/ATP13A2 maintains zinc homeostasis and promotes α-synuclein externalization via exosomes. Hum Mol Genet 23:2816–2833. doi:10.1093/hmg/ddu099 PubMedCrossRef

Kovacs GG, Gasque P, Ströbel T et al (2004) Complement activation in human prion disease. Neurobiol Dis 15(1):21–28. doi:10.1016/j.nbd.2003.09.010 PubMedCrossRef

Krieglstein K, Suter-Crazzolara C, Fischer WH, Unsicker K (1995) TGF-beta superfamily members promote survival of midbrain dopaminergic neurons and protect them against MPP+ toxicity. EMBO J 14:736–742PubMedPubMedCentralCrossRef

Kumar P, Dezso Z, MacKenzie C et al (2013) Circulating miRNA biomarkers for Alzheimer’s disease. PLoS One 8:e69807. doi:10.1371/journal.pone.0069807 PubMedPubMedCentralCrossRef

Lambert JC, Heath S, Even G et al (2009) Genome-wide association study identifies variants at CLU and CR1 associated with Alzheimer's disease. Nat Genet 41(10):1094–1099. doi:10.1038/ng.439 PubMedCrossRef

Lambert JC, Ibrahim-Verbaas CA, Harold D et al (2013) Meta-analysis of 74,046 individuals identifies 11 new susceptibility loci for Alzheimer’s disease. Nat Genet 45:1452–1458. doi:10.1038/ng.2802 PubMedPubMedCentralCrossRef

Lattante S, Le Ber I, Camuzat A et al (2013) TREM2 mutations are rare in a French cohort of patients with frontotemporal dementia. Neurobiology 34(2443):e1–e2. doi:10.1016/j.neurobiolaging.2013.04.030 CrossRef

Lee H-J, Suk J-E, Bae E-J et al (2008) Assembly-dependent endocytosis and clearance of extracellular alpha-synuclein. Int J Biochem Cell Biol 40:1835–1849. doi:10.1016/j.biocel.2008.01.017 PubMedCrossRef

Lee H-J, Suk J-E, Patrick C et al (2010) Direct transfer of alpha-synuclein from neuron to astroglia causes inflammatory responses in synucleinopathies. J Biol Chem 285:9262–9272. doi:10.1074/jbc.M109.081125 PubMedPubMedCentralCrossRef

Lee JY, Lee JD, Phipps S et al (2015) Absence of toll-like receptor 4 (TLR4) extends survival in the hSOD1 G93A mouse model of amyotrophic lateral sclerosis. J Neuroinflammation 12:90. doi:10.1186/s12974-015-0310-z PubMedPubMedCentralCrossRef

Lee S, Kim H-J (2015) Prion-like mechanism in amyotrophic lateral sclerosis: are protein aggregates the key? Exp Neurobiol 24:1–7. doi:10.5607/en.2015.24.1.1 PubMedCrossRef

Lee JD, Kumar V, Fung JN et al (2017) Pharmacological inhibition of complement C5a-C5a 1 receptor signalling ameliorates disease pathology in the hSOD1 G93A mouse model of amyotrophic lateral sclerosis. Br J Pharmacol 174(8):689–699. doi:10.1111/bph.13730 PubMedPubMedCentralCrossRef

Lehmann SM, Krüger C, Park B et al (2012) An unconventional role for miRNA: let-7 activates Toll-like receptor 7 and causes neurodegeneration. Nat Neurosci 15:827–835. doi:10.1038/nn.3113 PubMedCrossRef

Letiembre M, Liu Y, Walter S et al (2009) Screening of innate immune receptors in neurodegenerative diseases: a similar pattern. Neurobiology 30:759–768. doi:10.1016/j.neurobiolaging.2007.08.018 CrossRef

Lewis C-A, Manning J, Rossi F, Krieger C (2012) The neuroinflammatory response in ALS: the roles of microglia and T Cells. Neurol Res Int 2012:803701. doi:10.1155/2012/803701 PubMedPubMedCentralCrossRef

Li D, He Q, Li R et al (2012) Interleukin-10 promoter polymorphisms in Chinese patients with Parkinson’s disease. Neurosci Lett 513:183–186. doi:10.1016/j.neulet.2012.02.033 PubMedCrossRef

Li MO, Flavell RA (2008) Contextual regulation of inflammation: a duet by transforming growth factor-beta and interleukin-10. Immunity 28(4):468–476. doi:10.1016/j.immuni.2008.03.003 PubMedCrossRef

Li X, Long J, He T et al (2015a) Integrated genomic approaches identify major pathways and upstream regulators in late onset Alzheimer’s disease. Sci Rep 5:12393. doi:10.1038/srep12393 PubMedPubMedCentralCrossRef

Li X, Shen N, Zhang S et al (2015b) CD33 rs3865444 polymorphism contributes to Alzheimer’s disease susceptibility in Chinese, European, and North American populations. Mol Neurobiol 52:414–421. doi:10.1007/s12035-014-8880-9 PubMedCrossRef

Lian H, Litvinchuck A, Chiang ACA et al (2016) Astrocyte-microglia cross talk through complement activation modulates amyloid pathology in mouse models of Alzheimer’s disease. J Neurosci 36(2):577–589. doi:10.1523/JNEUROSCI.2117-15.2016 PubMedPubMedCentralCrossRef

Lill CM, Rengmark A, Pihlstrøm L et al (2015) The role of TREM2 R47H as a risk factor for Alzheimer’s disease, frontotemporal lobar degeneration, amyotrophic lateral sclerosis, and Parkinson’s disease. Alzheimers Dement 11:1407–1416. doi:10.1016/j.jalz.2014.12.009 PubMedPubMedCentralCrossRef

Lio D, Licastro F, Scola L et al (2003) Interleukin-10 promoter polymorphism in sporadic Alzheimer’s disease. Genes Immun 4:234–238. doi:10.1038/sj.gene.6363964 PubMedCrossRef

Lippa CF, Fujiwara H, Mann DM et al (1998) Lewy bodies contain altered alpha-synuclein in brains of many familial Alzheimer’s disease patients with mutations in presenilin and amyloid precursor protein genes. Am J Pathol 153:1365–1370PubMedPubMedCentralCrossRef

Liu H, Leak RK, Hu X (2016) Neurotransmitter receptors on microglia. Stroke Vasc Neurol 1(2):52–58. doi:10.1136/svn-2016-000012 PubMedPubMedCentralCrossRef

Liu Y, Hao W, Dawson A et al (2009) Expression of amyotrophic lateral sclerosis-linked SOD1 mutant increases the neurotoxic potential of microglia via TLR2. J Biol Chem 284:3691–3699. doi:10.1074/jbc.M804446200 PubMedCrossRef

Liu Y, Walter S, Stagi M et al (2005) LPS receptor (CD14): a receptor for phagocytosis of Alzheimer’s amyloid peptide. Brain 128:1778–1789. doi:10.1093/brain/awh531 PubMedCrossRef

Lobo-Silva D, Carriche GM, Castro AG et al (2016) Balancing the immune response in the brain: IL-10 and its regulation. J Neuroinflammation 13:297. doi:10.1186/s12974-016-0763-8 PubMedPubMedCentralCrossRef

Lobsiger CS, Boillée S, Cleveland DW (2007) Toxicity from different SOD1 mutants dysregulates the complement system and the neuronal regenerative response in ALS motor neurons. Proc Natl Acad Sci USA 104(18):7319–7326. doi:10.1073/pnas.0702230104 PubMedPubMedCentralCrossRef

Lobsiger CS, Boillée S, Pozniak C et al (2013) C1q induction and global complement pathway activation do not contribute to ALS toxicity in mutant SOD1 mice. Proc Natl Acad Sci USA 110(46):E4385–E4392. doi:10.1073/pnas.1318309110 PubMedPubMedCentralCrossRef

Loeffler DA, Camp DM, Bennett DA (2008) Plaque complement activation and cognitive loss in Alzheimer’s disease. J Neuroinflammation 5:9. doi:10.1186/1742-2094-5-9 PubMedPubMedCentralCrossRef

Loewenbrueck KF, Tigno-Aranjuez JT, Boehm BO et al (2010) Th1 responses to beta-amyloid in young humans convert to regulatory IL-10 responses in down syndrome and Alzheimer’s disease. Neurobiology 31:1732–1742. doi:10.1016/j.neurobiolaging.2008.09.007 CrossRef

Long-Smith CM, Sullivan AM, Nolan YM (2009) The influence of microglia on the pathogenesis of Parkinson’s disease. Prog Neurobiol 89:277–287. doi:10.1016/j.pneurobio.2009.08.001 PubMedCrossRef

López González I, Garcia-Esparcia P, Llorens F, Ferrer I (2016) Genetic and transcriptomic profiles of inflammation in neurodegenerative diseases: Alzheimer, Parkinson, Creutzfeldt-Jakob and Tauopathies. Int J Mol Sci 17:206. doi:10.3390/ijms17020206 PubMedPubMedCentralCrossRef

Luo H-T, Zhang J-P, Miao F (2016) Effects of pramipexole treatment on the α-synuclein content in serum exosomes of Parkinson’s disease patients. Exp Ther Med 12:1373–1376. doi:10.3892/etm.2016.3471 PubMedPubMedCentralCrossRef

Lv Y, Chen C, Zhang BY et al (2015) Remarkable activation of the complement system and aberrant neuronal localization of the membrane attack complex in the brain tissues of scrapie-infected rodents. Mol Neurobiol 52(3):1165–1179. doi:10.1007/s12035-014-8915-2 PubMedCrossRef

Ma SL, Tang NL, Lam LC, Chiu HF (2005) The association between promoter polymorphism of the interleukin-10 gene and Alzheimer’s disease. Neurobiology 26:1005–1010. doi:10.1016/j.neurobiolaging.2004.08.010 CrossRef

Maciotta S, Meregalli M, Torrente Y (2013) The involvement of microRNAs in neurodegenerative diseases. Front Cell Neurosci 7:265. doi:10.3389/fncel.2013.00265 PubMedPubMedCentralCrossRef

Malik M, Simpson JF, Parikh I et al (2013) CD33 Alzheimer’s risk-altering polymorphism, CD33 expression, and exon 2 splicing. J Neurosci 33:13320–13325. doi:10.1523/JNEUROSCI.1224-13.2013 PubMedPubMedCentralCrossRef

Mantovani S, Gordon R, Macmaw JK et al (2014) Elevation of the terminal complement activation products C5a and C5b-9 in ALS patient blood. J Neuroimmunol 276(1–2):213–218PubMedCrossRef

Mawuenyega KG, Sigurdson W, Ovod V et al (2010) Decreased clearance of CNS beta-amyloid in Alzheimer’s disease. Science 330:1774. doi:10.1126/science.1197623 PubMedPubMedCentralCrossRef

McDonald CL, Hennessy E, Rubio-Araiz A et al (2016) Inhibiting TLR2 activation attenuates amyloid accumulation and glial activation in a mouse model of Alzheimer’s disease. Brain Behav Immun 58:191–200. doi:10.1016/j.bbi.2016.07.143 PubMedCrossRef

McGeer PL, Itagaki S, Boyes BE, McGeer EG (1988) Reactive microglia are positive for HLA-DR in the substantia nigra of Parkinson’s and Alzheimer’s disease brains. Neurology 38:1285–1291PubMedCrossRef

McGeer PL, Itagaki S, Tago H, McGeer EG (1987) Reactive microglia in patients with senile dementia of the Alzheimer type are positive for the histocompatibility glycoprotein HLA-DR. Neurosci Lett 79:195–200PubMedCrossRef

McGeer PL, McGeer EG (2004) Inflammation and neurodegeneration in Parkinson’s disease. Parkinsonism Relat Disord 10(Suppl 1):S3–S7. doi:10.1016/j.parkreldis.2004.01.005 PubMedCrossRef

Melchior B, Garcia AE, Hsiung BK et al (2010) Dual induction of TREM2 and tolerance-related transcript, Tmem176b, in amyloid transgenic mice: implications for vaccine-based therapies for Alzheimer’s disease. ASN Neuro 2:e00037. doi:10.1042/AN20100010 PubMedPubMedCentralCrossRef

Mengel D, Thelen M, Balzer-Geldsetzer M et al (2016) TREM2 rare variant p.R47H is not associated with Parkinson’s disease. Parkinsonism Relat Disord 23:109–111. doi:10.1016/j.parkreldis.2015.11.026 PubMedCrossRef

Michaud J-P, Hallé M, Lampron A et al (2013) Toll-like receptor 4 stimulation with the detoxified ligand monophosphoryl lipid A improves Alzheimer’s disease-related pathology. Proc Natl Acad Sci USA 110:1941–1946. doi:10.1073/pnas.1215165110 PubMedPubMedCentralCrossRef

Michaud J-P, Rivest S (2015) Anti-inflammatory signaling in microglia exacerbates Alzheimer’s disease-related pathology. Neuron 85:450–452. doi:10.1016/j.neuron.2015.01.021 PubMedCrossRef

Michel B, Ferguson A, Johnson T et al (2012) Genetic depletion of complement receptors CD21/35 prevents terminal prion disease in a mouse model of chronic wasting disease. J Immunol 189(9):4520–4527. doi:10.4049/jimmunol.1201579 PubMedPubMedCentralCrossRef

Michel B, Ferguson A, Johnson T et al (2013) Complement protein C3 exacerbates prion disease in a mouse model of chronic wasting disease. Int Immunol 25(12):697–702. doi:10.1093/intimm/dxt034 PubMedPubMedCentralCrossRef

Miguel-Álvarez M, Santos-Lozano A, Sanchis-Gomar F et al (2015) Non-steroidal anti-inflammatory drugs as a treatment for Alzheimer’s disease: a systematic review and meta-analysis of treatment effect. Drugs Aging 32:139–147. doi:10.1007/s40266-015-0239-z PubMedCrossRef

Minoretti P, Gazzaruso C, Vito CD et al (2006) Effect of the functional toll-like receptor 4 Asp299Gly polymorphism on susceptibility to late-onset Alzheimer’s disease. Neurosci Lett 391:147–149. doi:10.1016/j.neulet.2005.08.047 PubMedCrossRef

Mirza B, Hadberg H, Thomsen P, Moos T (2000) The absence of reactive astrocytosis is indicative of a unique inflammatory process in Parkinson’s disease. Neuroscience 95:425–432. doi:10.1016/S0306-4522(99)00455-8 PubMedCrossRef

Mogi M, Harada M, Kondo T et al (1995) Transforming growth factor-beta 1 levels are elevated in the striatum and in ventricular cerebrospinal fluid in Parkinson’s disease. Neurosci Lett 193:129–132PubMedCrossRef

Montag J, Hitt R, Opitz L et al (2009) Upregulation of miRNA hsa-miR-342-3p in experimental and idiopathic prion disease. Mol Neurodegener 4:36. doi:10.1186/1750-1326-4-36 PubMedPubMedCentralCrossRef

Morelli AE, Larregina AT, Shufesky WJ et al (2004) Endocytosis, intracellular sorting, and processing of exosomes by dendritic cells. Blood 104:3257–3266. doi:10.1182/blood-2004-03-0824 PubMedCrossRef

Münch C, Bertolotti A (2011) Self-propagation and transmission of misfolded mutant SOD1: prion or prion-like phenomenon? Cell Cycle 10:1711. doi:10.4161/cc.10.11.15560 PubMedCrossRef

Münch C, O’Brien J, Bertolotti A (2011) Prion-like propagation of mutant superoxide dismutase-1 misfolding in neuronal cells. Proc Natl Acad Sci USA 108:3548–3553. doi:10.1073/pnas.1017275108 PubMedPubMedCentralCrossRef

Nagai M, Re DB, Nagata T et al (2007) Astrocytes expressing ALS-linked mutated SOD1 release factors selectively toxic to motor neurons. Nat Neurosci 10:615–622. doi:10.1038/nn1876 PubMedPubMedCentralCrossRef

Nagatsu T, Mogi M, Ichinose H, Togari A (2000) Cytokines in Parkinson’s disease. J Neural Transm Suppl 58:143–151

Naj AC, Jun G, Beecham GW et al (2011) Common variants at MS4A4/MS4A6E, CD2AP, CD33 and EPHA1 are associated with late-onset Alzheimer’s disease. Nat Genet 43:436–441. doi:10.1038/ng.801 PubMedPubMedCentralCrossRef

Nakamura M, Ito H, Wate R et al (2008) Phosphorylated Smad2/3 immunoreactivity in sporadic and familial amyotrophic lateral sclerosis and its mouse model. Acta Neuropathol 115:327–334. doi:10.1007/s00401-007-0337-z PubMedCrossRef

Nakamura M, Kaneko S, Ito H et al (2013) Activation of transforming growth factor-β/Smad signaling reduces aggregate formation of mislocalized TAR DNA-binding protein-43. Neurodegener Dis 11:182–193. doi:10.1159/000338151 PubMedCrossRef

Nawrocka-Kunecka A, Papierz W, Liberski PP (2005) Complement factors C1q and C3b in brains with Creutzfeldt-Jakob disease. Pol J Pathol 56(3):127–129PubMed

Nie K, Zhang Y, Gan R et al (2013) Polymorphisms in immune/inflammatory cytokine genes are related to Parkinson’s disease with cognitive impairment in the Han Chinese population. Neurosci Lett 541:111–115. doi:10.1016/j.neulet.2013.02.024 PubMedCrossRef

Noelker C, Morel L, Lescot T et al (2013) Toll like receptor 4 mediates cell death in a mouse MPTP model of Parkinson disease. Sci Rep 3:1393. doi:10.1038/srep01393 PubMedPubMedCentralCrossRef

Nonaka T, Masuda-Suzukake M, Arai T et al (2013) Prion-like properties of pathological TDP-43 aggregates from diseased brains. Cell Rep 4:124–134. doi:10.1016/j.celrep.2013.06.007 PubMedCrossRef

Okello A, Edison P, Archer HA et al (2009) Microglial activation and amyloid deposition in mild cognitive impairment: a PET study. Neurology 72:56–62. doi:10.1212/01.wnl.0000338622.27876.0d PubMedPubMedCentralCrossRef

Orr CF, Rowe DB, Mizuno Y et al (2005) A possible role for humoral immunity in the pathogenesis of Parkinson’s disease. Brain 128:2665–2674. doi:10.1093/brain/awh625 PubMedCrossRef

Pascale E, Passarelli E, Purcaro C et al (2011) Lack of association between IL-1β, TNF-α, and IL-10 gene polymorphisms and sporadic Parkinson’s disease in an Italian cohort. Acta Neurol Scand 124:176–181. doi:10.1111/j.1600-0404.2010.01441.x PubMedCrossRef

Peyrin JM, Lasmézas CI, Haïk S et al (1999) Microglial cells respond to amyloidogenic PrP peptide by the production of inflammatory cytokines. Neuroreport 10:723–729PubMedCrossRef

Phatnani HP, Guarnieri P, Friedman BA et al (2013) Intricate interplay between astrocytes and motor neurons in ALS. Proc Natl Acad Sci USA 110:E756–E765. doi:10.1073/pnas.1222361110 PubMedPubMedCentralCrossRef

Polanco JC, Scicluna BJ, Hill AF, Götz J (2016) Extracellular vesicles isolated from the brains of rTg4510 mice seed tau protein aggregation in a threshold-dependent manner. J Biol Chem 291:12445–12466. doi:10.1074/jbc.M115.709485 PubMedPubMedCentralCrossRef

Price DA, Martinez AA, Seillier A et al (2009) WIN55,212-2, a cannabinoid receptor agonist, protects against nigrostriatal cell loss in the 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine mouse model of Parkinson’s disease. Eur J Neurosci 29:2177–2186. doi:10.1111/j.1460-9568.2009.06764.x PubMedPubMedCentralCrossRef

Prinz M, Priller J (2017) The role of peripheral immune cells in the CNS in steady state and disease. Nat Neurosci. doi:10.1038/nn.4475 CrossRefPubMed

Prokop S, Miller KR, Heppner FL (2013) Microglia actions in Alzheimer’s disease. Acta Neuropathol 126:461–477. doi:10.1007/s00401-013-1182-x PubMedCrossRef

Qin Y, Liu Y, Hao W et al (2016) Stimulation of TLR4 attenuates Alzheimer’s disease-related symptoms and pathology in tau-transgenic mice. J Immunol 197:3281–3292. doi:10.4049/jimmunol.1600873 PubMedCrossRef

Rajendran L, Bali J, Barr MM et al (2014) Emerging roles of extracellular vesicles in the nervous system. J Neurosci 34:15482–15489. doi:10.1523/JNEUROSCI.3258-14.2014 PubMedPubMedCentralCrossRef

Rajendran L, Honsho M, Zahn TR et al (2006) Alzheimer’s disease beta-amyloid peptides are released in association with exosomes. Proc Natl Acad Sci USA 103:11172–11177. doi:10.1073/pnas.0603838103 PubMedPubMedCentralCrossRef

Ramirez BG, Blazquez C, Gomez del Pulgar T et al (2005) Prevention of Alzheimer’s disease pathology by cannabinoids: neuroprotection mediated by blockade of microglial activation. J Neurosci 25:1904–1913. doi:10.1523/JNEUROSCI.4540-04.2005 PubMedCrossRef

Ramos EM, Lin MT, Larson EB et al (2006) Tumor necrosis factor alpha and interleukin 10 promoter region polymorphisms and risk of late-onset Alzheimer disease. Arch Neurol 63:1165–1169. doi:10.1001/archneur.63.8.1165 PubMedCrossRef

Rayaprolu S, Mullen B, Baker M et al (2013) TREM2 in neurodegeneration: evidence for association of the p. R47H variant with frontotemporal dementia and Parkinson’s disease. Mol Neurodegener 8:19. doi:10.1186/1750-1326-8-19 PubMedPubMedCentralCrossRef

Reed-Geaghan EG, Savage JC, Hise AG, Landreth GE (2009) CD14 and toll-like receptors 2 and 4 are required for fibrillar A{beta}-stimulated microglial activation. J Neurosci 29:11982–11992. doi:10.1523/JNEUROSCI.3158-09.2009 PubMedPubMedCentralCrossRef

Rentzos M, Nikolaou C, Andreadou E et al (2009) Circulating interleukin-10 and interleukin-12 in Parkinson’s disease. Acta Neurol Scand 119:332–337. doi:10.1111/j.1600-0404.2008.01103.x PubMedCrossRef

Rezai-Zadeh K, Gate D, Town T (2009) CNS infiltration of peripheral immune cells: D-Day for neurodegenerative disease? J Neuroimmune Pharmacol 4:462–475. doi:10.1007/s11481-009-9166-2 PubMedPubMedCentralCrossRef

Rivest S (2015) TREM2 enables amyloid β clearance by microglia. Cell Res 25:535–536. doi:10.1038/cr.2015.37 PubMedPubMedCentralCrossRef

Roberts K, Zeineddine R, Corcoran L et al (2013) Extracellular aggregated Cu/Zn superoxide dismutase activates microglia to give a cytotoxic phenotype. Glia 61:409–419. doi:10.1002/glia.22444 PubMedCrossRef

Saba R, Goodman CD, Huzarewich RLCH et al (2008) A miRNA signature of prion induced neurodegeneration. PLoS One 3:e3652. doi:10.1371/journal.pone.0003652 PubMedPubMedCentralCrossRef

Saba R, Gushue S, Huzarewich RLCH et al (2012) MicroRNA 146a (miR-146a) is over-expressed during prion disease and modulates the innate immune response and the microglial activation state. PLoS One 7:e30832. doi:10.1371/journal.pone.0030832 PubMedPubMedCentralCrossRef

Salins P, He Y, Olson K et al (2008) TGF-beta1 is increased in a transgenic mouse model of familial Alzheimer’s disease and causes neuronal apoptosis. Neurosci Lett 430:81–86. doi:10.1016/j.neulet.2007.10.025 PubMedCrossRef

Saman S, Kim W, Raya M et al (2012) Exosome-associated tau is secreted in tauopathy models and is selectively phosphorylated in cerebrospinal fluid in early Alzheimer disease. J Biol Chem 287:3842–3849. doi:10.1074/jbc.M111.277061 PubMedCrossRef

Sanchez-Mejias E, Navarro V, Jimenez S et al (2016) Soluble phospho-tau from Alzheimer’s disease hippocampus drives microglial degeneration. Acta Neuropathol 132:897–916. doi:10.1007/s00401-016-1630-5 PubMedPubMedCentralCrossRef

Sargsyan SA, Monk PN, Shaw PJ (2005) Microglia as potential contributors to motor neuron injury in amyotrophic lateral sclerosis. Glia 51:241–253. doi:10.1002/glia.20210 PubMedCrossRef

Sarkar S, Jun S, Rellick S et al (2016) Expression of microRNA-34a in Alzheimer’s disease brain targets genes linked to synaptic plasticity, energy metabolism, and resting state network activity. Brain Res 1646:139–151. doi:10.1016/j.brainres.2016.05.026 PubMedPubMedCentralCrossRef

Scassellati C, Zanardini R, Squitti R et al (2004) Promoter haplotypes of interleukin-10 gene and sporadic Alzheimer’s disease. Neurosci Lett 356:119–122. doi:10.1016/j.neulet.2003.11.033 PubMedCrossRef

Sharples RA, Vella LJ, Nisbet RM et al (2008) Inhibition of gamma-secretase causes increased secretion of amyloid precursor protein C-terminal fragments in association with exosomes. FASEB J 22:1469–1478. doi:10.1096/fj.07-9357 PubMedCrossRef

Sherwin E, Dinan TG, Cryan JF (2017) Recent developments in understanding the role of the gut microbiota in brain health and disease. Ann N Y Acad Sci. doi:10.1111/nyas.13416 PubMedCrossRef

Sierra A, Gottfried-Blackmore AC, McEwen BS, Bulloch K (2007) Microglia derived from aging mice exhibit an altered inflammatory profile. Glia 55:412–424. doi:10.1002/glia.20468 PubMedCrossRef

Sim RB, Kishore U, Villiers CL et al (2007) C1q binding and complement activation by prions and amyloids. Immunobiology 212(4–5):355–362. doi:10.1016/j.imbio.2007.04.001 PubMedCrossRef

Sisková Z, Page A, O’Connor V, Perry VH (2009) Degenerating synaptic boutons in prion disease: microglia activation without synaptic stripping. Am J Pathol 175:1610–1621. doi:10.2353/ajpath.2009.090372 PubMedPubMedCentralCrossRef

Slattery CF, Beck JA, Harper L et al (2014) R47H TREM2 variant increases risk of typical early-onset Alzheimer’s disease but not of prion or frontotemporal dementia. Alzheimers Dement 10(602–608):e4. doi:10.1016/j.jalz.2014.05.1751 CrossRef

Spinner DS, Cho IS, Park SY et al (2008) Accelerated prion disease pathogenesis in Toll-like receptor 4 signaling-mutant mice. J Virol 82:10701–10708. doi:10.1128/JVI.00522-08 PubMedPubMedCentralCrossRef

Stefanova N, Fellner L, Reindl M et al (2011) Toll-like receptor 4 promotes α-synuclein clearance and survival of nigral dopaminergic neurons. Am J Pathol 179:954–963. doi:10.1016/j.ajpath.2011.04.013 PubMedPubMedCentralCrossRef

Stoeck K, Bodemer M, Ciesielczyk B et al (2005) Interleukin 4 and interleukin 10 levels are elevated in the cerebrospinal fluid of patients with Creutzfeldt-Jakob disease. Arch Neurol 62:1591–1594. doi:10.1001/archneur.62.10.1591 PubMedCrossRef

Street JM, Barran PE, Mackay CL et al (2012) Identification and proteomic profiling of exosomes in human cerebrospinal fluid. J Transl Med 10:5. doi:10.1186/1479-5876-10-5 PubMedPubMedCentralCrossRef

Stuendl A, Kunadt M, Kruse N et al (2016) Induction of α-synuclein aggregate formation by CSF exosomes from patients with Parkinson’s disease and dementia with Lewy bodies. Brain 139:481–494. doi:10.1093/brain/awv346 PubMedCrossRef

Svensson KJ, Christianson HC, Wittrup A et al (2013) Exosome uptake depends on ERK1/2-heat shock protein 27 signaling and lipid Raft-mediated endocytosis negatively regulated by caveolin-1. J Biol Chem 288:17713–17724. doi:10.1074/jbc.M112.445403 PubMedPubMedCentralCrossRef

Szekely CA, Zandi PP (2010) Non-steroidal anti-inflammatory drugs and Alzheimer’s disease: the epidemiological evidence. CNS Neurol Disord Drug Targets 9:132–139PubMedCrossRef

Sznejder-Pachołek A, Joniec-Maciejak I, Wawer A et al (2017) The effect of α-synuclein on gliosis and IL-1α, TNFα, IFNγ, TGFβ expression in murine brain. Pharmacol Rep 69(2):242–251. doi:10.1016/j.pharep.2016.11.003 PubMedCrossRef

Tacnet-Delorme P, Chevallier S, Arlaud GJ (2001) Beta-amyloid fibrils activate the C1 complex of complement under physiological conditions: evidence for a binding site for A beta on the C1q globular regions. J Immunol 167:6374–6381. doi:10.4049/jimmunol.167.11.6374 PubMedCrossRef

Tahara K, Kim HD, Jin JJ et al (2006) Role of toll-like receptor signalling in Abeta uptake and clearance. Brain 129:3006–3019. doi:10.1093/brain/awl249 PubMedPubMedCentralCrossRef

Tamboli IY, Barth E, Christian L et al (2010) Statins promote the degradation of extracellular amyloid {beta}-peptide by microglia via stimulation of exosome-associated insulin-degrading enzyme (IDE) secretion. J Biol Chem 285:37405–37414. doi:10.1074/jbc.M110.149468 PubMedPubMedCentralCrossRef

Tan J, Town T, Mullan M (2002) CD40-CD40L interaction in Alzheimer's disease. Curr Opin Pharmacol 2(4):445–451. doi:10.1016/S1471-4892(02)00180-7 PubMedCrossRef

Taylor DL, Diemel LT, Cuzner ML et al (2002) Activation of group II metabotropic glutamate receptors underlies microglial reactivity and neurotoxicity following stimulation with chromogranin A, a peptide up-regulated in Alzheimer’s disease. J Neurochem 82:1179–1191. doi:10.1046/j.1471-4159.2002.01062.x PubMedCrossRef

Taylor DL, Diemel LT, Pocock JM (2003) Activation of microglial group III metabotropic glutamate receptors protects neurons against microglial neurotoxicity. J Neurosci 23:2150–2160PubMedCrossRef

Ternianov A, Perez-Ortiz JM, Solesio ME et al (2012) Overexpression of CB2 cannabinoid receptors results in neuroprotection against behavioral and neurochemical alterations induced by intracaudate administration of 6-hydroxydopamine. Neurobiol Aging 33(421):e1–e16. doi:10.1016/j.neurobiolaging.2010.09.012 CrossRef

Tesseur I, Nguyen A, Chang B et al (2017) Deficiency in Neuronal TGF-beta Signaling Leads to Nigrostriatal Degeneration and Activation of TGF-beta Signaling Protects against MPTP Neurotoxicity in Mice. J Neurosci 37(17):4584–4592. doi:10.1523/JNEUROSCI.2952-16.2017 PubMedPubMedCentralCrossRef

Tesseur I, Zou K, Esposito L et al (2006) Deficiency in neuronal TGF-beta signaling promotes neurodegeneration and Alzheimer’s pathology. J Clin Investig 116:3060–3069. doi:10.1172/JCI27341 PubMedPubMedCentralCrossRef

Théry C, Ostrowski M, Segura E (2009) Membrane vesicles as conveyors of immune responses. Nat Rev Immunol 9:581–593. doi:10.1038/nri2567 PubMedCrossRef

Togo T, Akiyama H, Iseki E, Kondo H, Ikeda K, Kato M, Oda T, Tsuchiya K, Kosaka K (2002) Occurrence of T cells in the brain of Alzheimer’s disease and other neurological diseases. J Neuroimmunol. 124(1–2):83–92. doi:10.1016/S0165-5728(01)00496-9 PubMedCrossRef

Town T (2009) Alternative Abeta immunotherapy approaches for Alzheimer’s disease. CNS Neurol Disord Drug Targets 8:114–127. doi:10.2174/187152709787847306 PubMedPubMedCentralCrossRef

Town T (2010) Alzheimer’s Disease Beyond Abeta. Expert Rev Neurother 10:671–675PubMedPubMedCentralCrossRef

Town T, Laouar Y, Pittenger C et al (2008) Blocking TGF-beta-Smad2/3 innate immune signaling mitigates Alzheimer-like pathology. Nat Med 14:681–687. doi:10.1038/nm1781 PubMedPubMedCentralCrossRef

Town T, Tan J, Mullan M (2001) CD40 signaling and Alzheimer's disease pathogenesis. Neurochem Int 39(5–6):371–380PubMedCrossRef

Tran TA, Nguyen AD, Chang J et al (2011) Lipopolysaccharide and tumor necrosis factor regulate Parkin expression via nuclear factor-kappa B. PLoS One 6:e23660. doi:10.1371/journal.pone.0023660 PubMedPubMedCentralCrossRef

Trias E, Ibarburu S, Barreto-Núñez R, Barbeito L (2017) Significance of aberrant glial cell phenotypes in pathophysiology of amyotrophic lateral sclerosis. Neurosci Lett 636:27–31. doi:10.1016/j.neulet.2016.07.052 PubMedCrossRef

Tsuboi Y, Yamada T (1994) Increased concentration of C4d complement protein in CSF in amyotrophic lateral sclerosis. J Neurol Neurosurg Psychiatry 57(7):859–861PubMedPubMedCentralCrossRef

Tsunemi T, Hamada K, Krainc D (2014) ATP13A2/PARK9 regulates secretion of exosomes and α-synuclein. J Neurosci 34:15281–15287. doi:10.1523/JNEUROSCI.1629-14.2014 PubMedPubMedCentralCrossRef

Tu J, Chen B, Yang L et al (2015) Amyloid-β activates microglia and regulates protein expression in a manner similar to prions. J Mol Neurosci 56:509–518. doi:10.1007/s12031-015-0553-2 PubMedCrossRef

Unsicker K, Suter-Crazzalora C, Krieglstein K (1996) Growth factor function in the development and maintenance of midbrain dopaminergic neurons: concepts, facts and prospects for TGF-beta. Ciba Found Symp 196:70–80 (discussion 80–4) PubMed

Valadi H, Ekström K, Bossios A et al (2007) Exosome-mediated transfer of mRNAs and microRNAs is a novel mechanism of genetic exchange between cells. Nat Cell Biol 9:654–659. doi:10.1038/ncb1596 PubMedCrossRef

van der Wal EA, Gómez-Pinilla F, Cotman CW (1993) Transforming growth factor-beta 1 is in plaques in Alzheimer and down pathologies. Neuroreport 4:69–72PubMedCrossRef

Vawter MP, Dillon-Carter O, Tourtellotte WW et al (1996) TGFbeta1 and TGFbeta2 concentrations are elevated in Parkinson’s disease in ventricular cerebrospinal fluid. Exp Neurol 142:313–322. doi:10.1006/exnr.1996.0200 PubMedCrossRef

Veerhuis R, Hoozemans JJM, Janssen I et al (2002) Adult human microglia secrete cytokines when exposed to neurotoxic prion protein peptide: no intermediary role for prostaglandin E2. Brain Res 925:195–203PubMedCrossRef

Vehmas AK, Kawas CH, Stewart WF, Troncoso JC (2003) Immune reactive cells in senile plaques and cognitive decline in Alzheimer’s disease. Neurobiology 24:321–331. doi:10.1016/S0197-4580(02)00090-8 CrossRef

Vekrellis K, Xilouri M, Emmanouilidou E et al (2011) Pathological roles of α-synuclein in neurological disorders. Lancet Neurol 10:1015–1025. doi:10.1016/S1474-4422(11)70213-7 PubMedCrossRef

Vella LJ, Sharples RA, Lawson VA et al (2007) Packaging of prions into exosomes is associated with a novel pathway of PrP processing. J Pathol 211:582–590. doi:10.1002/path.2145 PubMedCrossRef

Vella LJ, Sharples RA, Nisbet RM et al (2008) The role of exosomes in the processing of proteins associated with neurodegenerative diseases. Eur Biophys J 37:323–332. doi:10.1007/s00249-007-0246-z PubMedCrossRef

Vincent B, Cisse MA, Sunyach C et al (2008) Regulation of betaAPP and PrPc cleavage by alpha-secretase: mechanistic and therapeutic perspectives. Curr Alzheimer Res 5:202–211PubMedCrossRef

Vural P, Değirmencioğlu S, Parildar-Karpuzoğlu H et al (2009) The combinations of TNFalpha-308 and IL-6 -174 or IL-10 -1082 genes polymorphisms suggest an association with susceptibility to sporadic late-onset Alzheimer’s disease. Acta Neurol Scand 120:396–401. doi:10.1111/j.1600-0404.2009.01230.x PubMedCrossRef

Wahner AD, Sinsheimer JS, Bronstein JM, Ritz B (2007) Inflammatory cytokine gene polymorphisms and increased risk of Parkinson disease. Arch Neurol 64:836–840. doi:10.1001/archneur.64.6.836 PubMedCrossRef

Walker DG, Whetzel AM, Serrano G et al (2015) Association of CD33 polymorphism rs3865444 with Alzheimer’s disease pathology and CD33 expression in human cerebral cortex. Neurobiology 36:571–582. doi:10.1016/j.neurobiolaging.2014.09.023 CrossRef

Walter S, Letiembre M, Liu Y et al (2007) Role of the toll-like receptor 4 in neuroinflammation in Alzheimer’s disease. Cell Physiol Biochem 20:947–956. doi:10.1159/000110455 PubMedCrossRef

Wang J, Zhao D, Pan B et al (2015a) Toll-like receptor 2 deficiency shifts PrP106-126-induced microglial activation from a neurotoxic to a neuroprotective phenotype. J Mol Neurosci 55:880–890. doi:10.1007/s12031-014-0442-0 PubMedCrossRef

Wang L-Z, Yu J-T, Miao D et al (2011a) Genetic association of TLR4/11367 polymorphism with late-onset Alzheimer’s disease in a Han Chinese population. Brain Res 1381:202–207. doi:10.1016/j.brainres.2011.01.007 PubMedCrossRef

Wang Y, Hancock AM, Bradner J et al (2011b) Complement 3 and factor h in human cerebrospinal fluid in Parkinson’s disease, Alzheimer’s disease, and multiple-system atrophy. Am J Pathol 178:1509–1516. doi:10.1016/j.ajpath.2011.01.006 PubMedPubMedCentralCrossRef

Wang Y, Cella M, Mallinson K et al (2015b) TREM2 lipid sensing sustains the microglial response in an Alzheimer’s disease model. Cell 160:1061–1071. doi:10.1016/j.cell.2015.01.049 PubMedPubMedCentralCrossRef

Wang Y, Duan W, Wang W et al (2016a) scAAV9-VEGF prolongs the survival of transgenic ALS mice by promoting activation of M2 microglia and the PI3K/Akt pathway. Brain Res 1648:1–10. doi:10.1016/j.brainres.2016.06.043 PubMedCrossRef

Wang Y, Ulland TK, Ulrich JD et al (2016b) TREM2-mediated early microglial response limits diffusion and toxicity of amyloid plaques. J Exp Med 213:667–675. doi:10.1084/jem.20151948 PubMedPubMedCentralCrossRef

Wang HA, Lee JD, Lee KM et al (2017) Complement C5a-C5aR1 signalling drives skeletal muscle macrophage recruitment in the hSOD1 G93A mouse model of amyotrophic lateral sclerosis. Skelet Muscle 7(1):10. doi:10.1186/s13395-017-0128-8 PubMedPubMedCentralCrossRef

Weitz TM, Town T (2012) Microglia in Alzheimer“s disease: it’s all about context. Int j Alzheimer’s Disease 2012:314185. doi:10.1155/2012/314185 CrossRef

Weitz TM, Town T (2016) Amyloid cascade into clarity. Immunity 45:717–718. doi:10.1016/j.immuni.2016.10.006 PubMedCrossRef

Westergard T, Jensen BK, Wen X et al (2016) Cell-to-cell transmission of dipeptide repeat proteins linked to C9orf72-ALS/FTD. Cell Rep 17:645–652. doi:10.1016/j.celrep.2016.09.032 PubMedPubMedCentralCrossRef

Williams A, Lucassen PJ, Ritchie D, Bruce M (1997) PrP deposition, microglial activation, and neuronal apoptosis in murine scrapie. Exp Neurol 144:433–438. doi:10.1006/exnr.1997.6424 PubMedCrossRef

Williams AE, Lawson LJ, Perry VH, Fraser H (1994a) Characterization of the microglial response in murine scrapie. Neuropathol Appl Neurobiol 20:47–55PubMedCrossRef

Williams AE, van Dam AM, Man-A-Hing WK et al (1994b) Cytokines, prostaglandins and lipocortin-1 are present in the brains of scrapie-infected mice. Brain Res 654:200–206PubMedCrossRef

Wisniewski HM, Barcikowska M, Kida E (1991) Phagocytosis of beta/A4 amyloid fibrils of the neuritic neocortical plaques. Acta Neuropathol 81:588–590PubMedCrossRef

Wolfers J, Lozier A, Raposo G et al (2001) Tumor-derived exosomes are a source of shared tumor rejection antigens for CTL cross-priming. Nat Med 7:297–303. doi:10.1038/85438 PubMedCrossRef

Woodruff TM, Costantini KJ, Crane JW et al (2008) The complement factor C5a contributes to pathology in a rat model of amyotrophic lateral sclerosis. J Immunol 181(12):8727–8734PubMedCrossRef

Wyss-Coray T, Lin C, Sanan DA et al (2000) Chronic overproduction of transforming growth factor-beta1 by astrocytes promotes Alzheimer’s disease-like microvascular degeneration in transgenic mice. Am J Pathol 156:139–150. doi:10.1016/S0002-9440(10)64713-X PubMedPubMedCentralCrossRef

Wyss-Coray T, Lin C, Yan F et al (2001) TGF-beta1 promotes microglial amyloid-beta clearance and reduces plaque burden in transgenic mice. Nat Med 7:612–618. doi:10.1038/87945 PubMedCrossRef

Wyss-Coray T, Masliah E, Mallory M et al (1997) Amyloidogenic role of cytokine TGF-beta1 in transgenic mice and in Alzheimer’s disease. Nature 389:603–606. doi:10.1038/39321 PubMedCrossRef

Wyss-Coray T, Mucke L (2002) Inflammation in neurodegenerative disease—a double-edged sword. Neuron 35:419–432. doi:10.1016/S0896-6273(02)00794-8 PubMedCrossRef

Yamada T, McGeer PL, McGeer EG (1992) Lewy bodies in Parkinson’s-disease are recognized by antibodies to complement proteins. Acta Neuropathol 84:100–104PubMedCrossRef

Yamanaka K, Chun SJ, Boillée S et al (2008) Astrocytes as determinants of disease progression in inherited amyotrophic lateral sclerosis. Nat Neurosci 11:251–253. doi:10.1038/nn2047 PubMedPubMedCentralCrossRef

Yang Y, Keene CD, Peskind ER et al (2015) Cerebrospinal fluid particles in Alzheimer disease and Parkinson disease. J Neuropathol Exp Neurol 74:672–687. doi:10.1097/NEN.0000000000000207 PubMedPubMedCentralCrossRef

Yu Y, Ye RD (2015) Microglial Aβ receptors in Alzheimer’s disease. Cell Mol Neurobiol 35:71–83. doi:10.1007/s10571-014-0101-6 PubMedCrossRef

Yuyama K, Sun H, Mitsutake S, Igarashi Y (2012) Sphingolipid-modulated exosome secretion promotes clearance of amyloid-beta by microglia. J Biol Chem 287:10977–10989. doi:10.1074/jbc.M111.324616 PubMedPubMedCentralCrossRef

Zabel MD, Heikenwalder M, Prinz M et al (2007) Stromal complement receptor CD21/35 facilitates lymphoid prion colonization and pathogenesis. J Immunol 179(9):6144–6152. doi:10.4049/jimmunol.179.9.6144 PubMedCrossRef

Zhang B, Gaiteri C, Bodea L-G et al (2013) Integrated systems approach identifies genetic nodes and networks in late-onset Alzheimer’s disease. Cell 153:707–720. doi:10.1016/j.cell.2013.03.030 PubMedPubMedCentralCrossRef

Zhang W, Wang T, Pei Z et al (2005) Aggregated alpha-synuclein activates microglia: a process leading to disease progression in Parkinson’s disease. FASEB J 19:533–542. doi:10.1096/fj.04-2751com PubMedCrossRef

Zhao W, Beers DR, Henkel JS et al (2010) Extracellular mutant SOD1 induces microglial-mediated motoneuron injury. Glia 58:231–243. doi:10.1002/glia.20919 PubMedPubMedCentralCrossRef

Zheng C, Zhou X-W, Wang J-Z (2016) The dual roles of cytokines in Alzheimer’s disease: update on interleukins, TNF-α, TGF-β and IFN-γ. Transl Neurodegener 5:7. doi:10.1186/s40035-016-0054-4 PubMedPubMedCentralCrossRef

Zhou F, Guan Y, Chen Y et al (2013) miRNA-9 expression is upregulated in the spinal cord of G93A-SOD1 transgenic mice. Int J Clin Exp Pathol 6:1826–1838PubMedPubMedCentral

Zhu C, Herrmann US, Li B et al (2015) Triggering receptor expressed on myeloid cells-2 is involved in prion-induced microglial activation but does not contribute to prion pathogenesis in mouse brains. Neurobiology 36:1994–2003. doi:10.1016/j.neurobiolaging.2015.02.019 CrossRef

Zitvogel L, Regnault A, Lozier A et al (1998) Eradication of established murine tumors using a novel cell-free vaccine: dendritic cell-derived exosomes. Nat Med 4:594–600PubMedCrossRef

Springer Medizin

Let’s make microglia great again in neurodegenerative disorders

Abstract

Leitlinien kompakt für die Neurologie

Neu im Fachgebiet Neurologie

Niedriger diastolischer Blutdruck erhöht Risiko für schwere kardiovaskuläre Komplikationen

Demenzkranke durch Antipsychotika vielfach gefährdet

Parkinson-Therapie im Wandel – aktuelle Leitlinie im Fokus

Auf diese Krankheiten bei Geflüchteten sollten Sie vorbereitet sein

Update Neurologie

Springer Medizin

Abstract

Bitte loggen Sie sich ein, um Zugang zu diesem Inhalt zu erhalten

Weitere Artikel der Ausgabe 5/2018

Neuroinflammation in neurodegeneration: role in pathophysiology, therapeutic opportunities and clinical perspectives

Interleukin 6 and complement serum level study in Parkinson’s disease

Neuroinflammatory responses in Alzheimer’s disease

Differential contribution of microglia and monocytes in neurodegenerative diseases

The IL-1β phenomena in neuroinflammatory diseases