Alpha-synuclein activates BV2 microglia dependent on its aggregation state

Biochemical and Biophysical Research Communications

Volumn 479, Issue 4, 2016, Pages 881-886

  Hoffmann, Alana ^a   Ettle, Benjamin ^a   Bruno, Ariane ^a   Kulinich, Anna ^b   Hoffmann, Anna Carin ^c   von Wittgenstein, Julia ^a,c   Winkler, Jürgen ^a   Xiang, Wei ^c   Schlachetzki, Johannes C M ^a,d  

^a UNIVERSITY HOSPITAL ERLANGEN   (Germany)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c UNIVERSITY OF ERLANGEN NUREMBERG   (Germany)

^d UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Alpha synuclein; Fibrils; Inflammation; Microglia; Synucleinopathies

Indexed keywords

ALPHA SYNUCLEIN; INTERLEUKIN 1BETA; TUMOR NECROSIS FACTOR; AUTACOID; CYTOKINE; MULTIPROTEIN COMPLEX; PROTEIN AGGREGATE; RECOMBINANT PROTEIN; SNCA PROTEIN, HUMAN;

ANALYSIS OF VARIANCE; ARTICLE; CELL ACTIVATION; CELL VIABILITY; CONTROLLED STUDY; CYTOKINE PRODUCTION; HUMAN; HUMAN CELL; IMMUNE RESPONSE; IMMUNOCYTOCHEMISTRY; IMMUNOREACTIVITY; INTERNALIZATION; MICROGLIA; OLIGOMERIZATION; PHAGOCYTOSIS; PHYSICAL CHEMISTRY; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN CROSS LINKING; QUANTITATIVE ANALYSIS; REAL TIME POLYMERASE CHAIN REACTION; SIZE EXCLUSION CHROMATOGRAPHY; UPREGULATION; ANIMAL; BIOSYNTHESIS; CELL LINE; CHEMISTRY; DRUG EFFECTS; METABOLISM; MOUSE; PROTEIN QUATERNARY STRUCTURE;

ALPHA-SYNUCLEIN; ANIMALS; CELL LINE; CYTOKINES; HUMANS; INFLAMMATION MEDIATORS; INTERLEUKIN-1BETA; MICE; MICROGLIA; MULTIPROTEIN COMPLEXES; PROTEIN AGGREGATES; PROTEIN STRUCTURE, QUATERNARY; RECOMBINANT PROTEINS; TUMOR NECROSIS FACTOR-ALPHA;

EID: 84991721659     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2016.09.109     Document Type: Article

References (36)

1. [1] Iwai, A., Masliah, E., Yoshimoto, M., et al. The precursor protein of non-ap component of Alzheimer's disease amyloid is a presynaptic protein of the central nervous system. Neuron, 14, 1995, 9.
2. [2] Fauvet, B., Mbefo, M.K., Fares, M.-B., et al. α-Synuclein in central nervous system and from erythrocytes, mammalian cells, and Escherichia coli exists predominantly as disordered monomer. J. Biol. Chem. 287 (2012), 15345–15364.
3. [3] Burré, J., Sharma, M., Tsetsenis, T., et al. α-Synuclein promotes SNARE-complex assembly in vivo and in vitro. Science 329 (2010), 1663–1667.
4. [4] Ramakrishnan, M., Jensen, P.H., Marsh, D., α-Synuclein association with phosphatidylglycerol probed by lipid spin labels†. Biochemistry 42 (2003), 12919–12926.
5. [5] Eliezer, D., Kutluay, E., Bussell, R. Jr., et al. Conformational properties of α-synuclein in its free and lipid-associated states1. J. Mol. Biol. 307 (2001), 1061–1073.
6. [6] Nuber, S., Selkoe, D.J., Caspase-1 clipping causes complications for alpha-synuclein. Proc. Natl. Acad. Sci. U. S. A., 22, 2016, 201610993.
7. [7] Caughey, B., Lansbury, P.T., Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annu. Rev. Neurosci. 26 (2003), 267–298.
8. [8] Oueslati, A., Fournier, M., Lashuel, H.A., Role of post-translational modifications in modulating the structure, function and toxicity of alpha-synuclein: implications for Parkinson's disease pathogenesis and therapies. Prog. Brain Res., 183, 2010.
9. [9] Cremades, N., Cohen, S.I., Deas, E., et al. Direct observation of the interconversion of normal and toxic forms of α-synuclein. Cell 149 (2012), 1048–1059.
10. [10] Braak, H., Braak, E., Pathoanatomy of Parkinson's disease. J. Neurol. Sci., 247, 2000, 8.
11. [11] Papp, M., Kahn, J., Lantos, P., Glial cytoplasmic inclusions in the CNS of patients with multiple system atrophy (striatonigral degeneration, olivopontocerebellar atrophy and Shy-Drager syndrome). J. Neurol. Sci., 94, 1989, 22.
12. [12] Uchihara, T., Giasson, B.I., Paulus, W., Propagation of Abeta, tau and alpha-synuclein pathology between experimental models and human reality: prions, propagons and propaganda. Acta Neuropathol. 131:1 (2016 Jan), 1–3, 10.1007/s00401-015-1517-x.
13. [13] McGeer, P.L., Itagaki, S., Boyes, B.E., et al. Reactive microglia are positive for HLA-DR in the substantia nigra of Parkinson's and Alzheimer's disease brains. Neurology, 38, 1988.
14. [14] Paolicelli, R.C., Bolasco, G., Pagani, F., et al. Synaptic pruning by microglia is necessary for normal brain development. Science 333 (2011), 1456–1458.
15. [15] Boche, D., Perry, V.H., Nicoll, J.A., Review: activation patterns of microglia and their identification in the human brain. Neuropathol. Appl. Neurobiol. 39 (2013), 3–18.
16. [16] Croisier, E., Graeber, M.B., Glial degeneration and reactive gliosis in alpha-synucleinopathies: the emerging concept of primary gliodegeneration. Acta Neuropathol. 112 (2006), 517–530.
17. [17] Salvesen, L., Ullerup, B.H., Sunay, F.B., et al. Changes in total cell numbers of the basal ganglia in patients with multiple system atrophy - a stereological study. Neurobiol. Dis. 74 (2015), 104–113.
18. [18] Xiang, W., Schlachetzki, J.C.M., Helling, S., et al. Oxidative stress-induced posttranslational modifications of alpha-synuclein: specific modification of alpha-synuclein by 4-hydroxy-2-nonenal increases dopaminergic toxicity. Mol. Cell. Neurosci. 54 (2013), 71–83.
19. [19] Blasi, E., Barluzzi, R., Bocchini, V., et al. Immortalization of murine microglial cells by a v-raf/v-myc carrying retrovirus. J. Neuroimmunol. 27 (1990), 229–237.
20. [20] Ettle, B., Reiprich, S., Deusser, J., et al. Intracellular alpha-synuclein affects early maturation of primary oligodendrocyte progenitor cells. Mol. Cell Neurosci. 62 (2014), 68–78.
21. [21] Klucken, J., Poehler, A.M., Ebrahimi-Fakhari, D., et al. Alpha-synuclein aggregation involves a bafilomycin A 1-sensitive autophagy pathway. Autophagy, 8, 2012.
22. [22] Das, A., Chai, J.C., Kim, S.H., et al. Dual RNA sequencing reveals the expression of unique transcriptomic signatures in lipopolysaccharide-induced BV-2 microglial cells. PLoS One, 10, 2015.
23. [23] Das, A., Kim, S.H., Arifuzzaman, S., et al. Transcriptome sequencing reveals that LPS-triggered transcriptional responses in established microglia BV2 cell lines are poorly representative of primary microglia. J. Neuroinflamm. 13 (2016), 1–18.
24. [24] Ricciardi-Castagnoli, P., Pirami, L., Righi, M., et al. Cellular Sources and Effects of Tumor Necrosis Factor a on Pituitary Cells and in the Central Nervous System, Neuropeptides and Immunopeptides: Messengers in a Neuroimmune Axis. 1990, NY Acad. Sci, New York, 156–168.
25. [25] Giulian, D., Baker, T.J., Shih, L.C., et al. Interleukin 1 of the central nervous system is produced by ameboid microglia. J. Exp. Med. 164 (1986), 594–604.
26. [26] Plata-Salamán, C.R., Immunoregulators in the nervous system. Neurosci. Biobehav. Rev. 15 (1991), 185–215.
27. [27] Merrill, J.E., Koyanagi, Y., Zack, J., et al. Induction of interleukin-1 and tumor necrosis factor alpha in brain cultures by human immunodeficiency virus type 1. J. Virol. 66 (1992), 2217–2225.
28. [28] Hausler, K.G., Prinz, M., Nolte, C., et al. Interferon-gamma differentially modulates the release of cytokines and chemokines in lipopolysaccharide- and pneumococcal cell wall-stimulated mouse microglia and macrophages. Eur. J. Neurosci. 16 (2002), 2113–2122.
29. [29] Henn, A., Lund, S., Hedtjarn, M., et al. The suitability of BV2 cells as alternative model system for primary microglia cultures or for animal experiments examining brain inflammation. Altex 26 (2009), 83–94.
30. [30] Su, X., Maguire-Zeiss, K.A., Giuliano, R., et al. Synuclein activates microglia in a model of Parkinson's Disease. Neurobiol. Aging 29 (2008), 1690–1701.
31. [31] Yin, J., Han, J., Zhang, C., et al. C-terminal part of α-synuclein mediates its activity in promoting proliferation of dopaminergic cells. J. Neural Transm. 118 (2011), 1155–1164.
32. [32] Bliederhaeuser, C., Grozdanov, V., Speidel, A., et al. Age-dependent defects of alpha-synuclein oligomer uptake in microglia and monocytes. Acta Neuropathol. 131 (2016), 379–391.
33. [33] Fellner, L., Irschick, R., Schanda, K., et al. Toll-like receptor 4 is required for alpha-synuclein dependent activation of microglia and astroglia. Glia 61 (2013), 349–360.
34. [34] Zhang, W., Wang, T., Pei, Z., et al. Aggregated α-synuclein activates microglia: a process leading to disease progression in Parkinson's disease. FASEB J. 19 (2005), 533–542.
35. [35] Kim, C., Ho, D.H., Suk, J.E., et al. Neuron-released oligomeric alpha-synuclein is an endogenous agonist of TLR2 for paracrine activation of microglia. Nat. Commun., 4, 2013, 1562.
36. [36] Stefanova, N., Fellner, L., Reindl, M., et al. Toll-like receptor 4 promotes α-synuclein clearance and survival of nigral dopaminergic neurons. Am. J. Pathol. 179 (2011), 954–963.