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Leucine-rich repeat kinase 2 (LRRK2) regulates α-synuclein clearance in microglia

Maekawa, Tatsunori, Sasaoka, Toshikuni, Azuma, Sadahiro, Ichikawa, Takafumi, Melrose, Heather L., Farrer, Matthew J., Obata, Fumiya·2016·BMC Neuroscience
DOI 10.1186/s12868-016-0315-2PMC PMC5131420
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Fig. 1 Characterization of LRRK2-KO microglia. a Tomato lectin staining of LRRK2-KO and WT microglia. One hundred cells were counted per culture well. n = 3 culture wells per group. Scale bar 50 μm. b MTT assay for evaluating the viability of LRRK2-KO and WT microglia in the absence or presence of αSYN. The data represent percentage viability relative to culture day 0, and were assessed by ANOVA at each time point (3 h: F = 0.26, p = 0.852; 6 h: F = 1.26, p = 0.351; 10 h: F = 0.94, p = 0.465; 24 h: F = 3.61, p = 0.065; 48 h: F = 2.55, p = 0.129; and 96 h: F = 3.46, p = 0.071). n = 3 culture wells per group. c Phagocytosis assay using FITC-microbeads. Upper panel shows an image of microbead phagocytosis. Scale bar 50 μm. Lower panel shows the fluorescence intensity of microbeads taken up by microglia. Forty cells were analyzed per group. The data are expressed as mean ± SD and were assessed by Student’s t test. These experiments were carried out three times using independent primary microglia isolated from different mice, and a representative image and data are shown
Fig. 1 Characterization of LRRK2-KO microglia. a Tomato lectin staining of LRRK2-KO and WT microglia. One hundred cells were counted per culture well. n = 3 culture wells per group. Scale bar 50 μm. b MTT assay for evaluating the viability of LRRK2-KO and WT microglia in the absence or presence of αSYN. The data represent percentage viability relative to culture day 0, and were assessed by ANOVA at each time point (3 h: F = 0.26, p = 0.852; 6 h: F = 1.26, p = 0.351; 10 h: F = 0.94, p = 0.465; 24 h: F = 3.61, p = 0.065; 48 h: F = 2.55, p = 0.129; and 96 h: F = 3.46, p = 0.071). n = 3 culture wells per group. c Phagocytosis assay using FITC-microbeads. Upper panel shows an image of microbead phagocytosis. Scale bar 50 μm. Lower panel shows the fluorescence intensity of microbeads taken up by microglia. Forty cells were analyzed per group. The data are expressed as mean ± SD and were assessed by Student’s t test. These experiments were carried out three times using independent primary microglia isolated from different mice, and a representative image and data are shownCC BY · PubMed Central
Fig. 2 Increased αSYN uptake and degradation by LRRK2 KO microglia. a Western analysis of LRRK2-KO microglia treated with αSYN. Lysates were prepared from LRRK2- KO and WT microglia treated with or without αSYN and subjected to Western analysis using anti-LRRK2, β-actin, and αSYN (C-20) antibodies. b Quantified density of αSYN bands in (a) normalized by the density of β-actin. n = 4 culture wells per group. c Western analysis using anti-LRRK2, GAPDH, and αSYN (MJFR1) antibodies. d Quantified density of αSYN bands in (c) normalized by the density of GAPDH. n = 4 culture wells per group. e Residual αSYN in the culture media of WT and KO microglia. n = 8 culture wells per group. The amounts of αSYN were measured by ELISA 48 h after αSYN treatment. In all graphical representations, data are expressed as mean ± SD and were assessed by Student’s t test (KO vs. WT); *p < 0.05, **p < 0.01. All experiments were carried out three times using primary microglia isolated from independent mice, and a representative image and data are shown
Fig. 2 Increased αSYN uptake and degradation by LRRK2 KO microglia. a Western analysis of LRRK2-KO microglia treated with αSYN. Lysates were prepared from LRRK2- KO and WT microglia treated with or without αSYN and subjected to Western analysis using anti-LRRK2, β-actin, and αSYN (C-20) antibodies. b Quantified density of αSYN bands in (a) normalized by the density of β-actin. n = 4 culture wells per group. c Western analysis using anti-LRRK2, GAPDH, and αSYN (MJFR1) antibodies. d Quantified density of αSYN bands in (c) normalized by the density of GAPDH. n = 4 culture wells per group. e Residual αSYN in the culture media of WT and KO microglia. n = 8 culture wells per group. The amounts of αSYN were measured by ELISA 48 h after αSYN treatment. In all graphical representations, data are expressed as mean ± SD and were assessed by Student’s t test (KO vs. WT); *p < 0.05, **p < 0.01. All experiments were carried out three times using primary microglia isolated from independent mice, and a representative image and data are shownCC BY · PubMed Central
Fig. 3 Increment of endocytotic αSYN uptake by LRRK2-KO microglia. a Confocal immunostaining images of αSYN and Rab5 in KO and WT microglia. Scale bar 50 μm. Higher-magnification views of the boxed area show the detail of immunopositive particles. Scale bar 20 μm. b Cytofluorograms for αSYN and Rab5 immunostaining evaluated using the high magnification views of KO and WT microglia. c The αSYN/Rab5 correlation coefficient (Rcoloc) values for KO and WT microglia. Ten cells were randomly chosen per group. In all graphical representations, data are expressed as mean ± SD and were assessed by Student’s t test; *p < 0.05. The experiment was carried out three times using primary microglia isolated from independent mice, and a representative image and data are shown
Fig. 3 Increment of endocytotic αSYN uptake by LRRK2-KO microglia. a Confocal immunostaining images of αSYN and Rab5 in KO and WT microglia. Scale bar 50 μm. Higher-magnification views of the boxed area show the detail of immunopositive particles. Scale bar 20 μm. b Cytofluorograms for αSYN and Rab5 immunostaining evaluated using the high magnification views of KO and WT microglia. c The αSYN/Rab5 correlation coefficient (Rcoloc) values for KO and WT microglia. Ten cells were randomly chosen per group. In all graphical representations, data are expressed as mean ± SD and were assessed by Student’s t test; *p < 0.05. The experiment was carried out three times using primary microglia isolated from independent mice, and a representative image and data are shownCC BY · PubMed Central
Fig. 4 Increase of early endosomes, but not lysosomes, late, or recycling endosomes, in LRRK2-KO microglia. a Immunostaining for lysosomal markers in KO and WT microglia. Lysosomes and acidic lysosomes were visualized using anti-LAMP1 and pHrodo, respectively. b Immunostaining for endosomal markers in KO and WT microglia. Early endosomes, late endosomes, and recycling endosomes were visualized using antibodies against Rab5, Rab7 and Rab11, respectively. Scale bar 20 μm. Quantification of fluorescence intensity per cell showing an increase of Rab5-positive endosomes, but not Rab7- and Rab11-positive particles, in KO microglia. Twenty-five cells were analyzed per group. c Visualization of early endosomes using CellLight. Twenty-five cells were analyzed per group. In the graphical representation, data are expressed as mean ± SD and were assessed by Student’s t test; *p < 0.05. All experiments were carried out three times using primary microglia isolated from independent mice, and a representative image and data are shown
Fig. 4 Increase of early endosomes, but not lysosomes, late, or recycling endosomes, in LRRK2-KO microglia. a Immunostaining for lysosomal markers in KO and WT microglia. Lysosomes and acidic lysosomes were visualized using anti-LAMP1 and pHrodo, respectively. b Immunostaining for endosomal markers in KO and WT microglia. Early endosomes, late endosomes, and recycling endosomes were visualized using antibodies against Rab5, Rab7 and Rab11, respectively. Scale bar 20 μm. Quantification of fluorescence intensity per cell showing an increase of Rab5-positive endosomes, but not Rab7- and Rab11-positive particles, in KO microglia. Twenty-five cells were analyzed per group. c Visualization of early endosomes using CellLight. Twenty-five cells were analyzed per group. In the graphical representation, data are expressed as mean ± SD and were assessed by Student’s t test; *p < 0.05. All experiments were carried out three times using primary microglia isolated from independent mice, and a representative image and data are shownCC BY · PubMed Central
Fig. 5 Higher Rab5 protein level in KO microglia than in WT microglia. Western analysis was performed to determine the protein levels of Rab5, Rab7 and Rab11 in KO and WT microglia treated with or without αSYN. The quantified density of each Rab was normalized by the density of GAPDH. n = 4 culture wells per group. In all graphical representations, data are expressed as mean ± SD and were assessed by ANOVA (KO vs WT). Rab5: F = 4.28, p = 0.028; Rab7: F = 0.96, p = 0.443; and Rab11: F = 0.01, p = 0.999. The experiment was carried out three times using primary microglia isolated from independent mice, and a representative image and data are shown
Fig. 5 Higher Rab5 protein level in KO microglia than in WT microglia. Western analysis was performed to determine the protein levels of Rab5, Rab7 and Rab11 in KO and WT microglia treated with or without αSYN. The quantified density of each Rab was normalized by the density of GAPDH. n = 4 culture wells per group. In all graphical representations, data are expressed as mean ± SD and were assessed by ANOVA (KO vs WT). Rab5: F = 4.28, p = 0.028; Rab7: F = 0.96, p = 0.443; and Rab11: F = 0.01, p = 0.999. The experiment was carried out three times using primary microglia isolated from independent mice, and a representative image and data are shownCC BY · PubMed Central
Fig. 6 Increased co-localization between Rab5 and dynamin 1 in LRRK2-KO microglia. a Comparison of co-localization of Rab5 and dynamin 1 between KO and WT microglia. Confocal immunostaining images show LRRK2-, Rab5-, and dynamin1-immunopositive particles in the KO and WT microglia. Scale bar 10 μm. b Cytofluorograms of dynamin 1 and Rab5 immunostaining in KO and WT microglia. c The Rcoloc values of dynamin1/Rab5 in KO and WT microglia. Ten cells were analyzed per group. In the graphical representation, data are expressed as mean ± SD and were assessed by Student’s t test; ***p < 0.005. All experiments were carried out three times using primary microglia isolated from independent mice, and a representative image and data are shown
Fig. 6 Increased co-localization between Rab5 and dynamin 1 in LRRK2-KO microglia. a Comparison of co-localization of Rab5 and dynamin 1 between KO and WT microglia. Confocal immunostaining images show LRRK2-, Rab5-, and dynamin1-immunopositive particles in the KO and WT microglia. Scale bar 10 μm. b Cytofluorograms of dynamin 1 and Rab5 immunostaining in KO and WT microglia. c The Rcoloc values of dynamin1/Rab5 in KO and WT microglia. Ten cells were analyzed per group. In the graphical representation, data are expressed as mean ± SD and were assessed by Student’s t test; ***p < 0.005. All experiments were carried out three times using primary microglia isolated from independent mice, and a representative image and data are shownCC BY · PubMed Central

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Research works printed but not linked: 50

  1. Bendor JT, Logan TP, Edwards RH. The function of α-synuclein. Neuron. 2013;79:1044–66. · DOI · Paper page
  2. Goedert M, Spillantini MG, Del Tredici K, Braak H. 100 Years of Lewy pathology. Nat Rev Neurol. 2013;9:13–24. · DOI · Paper page
  3. Mullin S, Schapira A. α-Synuclein and mitochondrial dysfunction in Parkinson’s disease. Mol Neurobiol. 2013;47:587–97. · DOI
  4. Olanow CW, Brundin P. Parkinson’s disease and alpha synuclein: is Parkinson’s disease a prion-like disorder? Mov Disord. 2013;28:31–40. · DOI
  5. Goedert M. Familial Parkinson’s disease. The awakening of alpha-synuclein. Nature. 1997;388:232–3. · DOI
  6. Polymeropoulos MH, Lavedan C, Leroy E, Ide SE, Dehejia A, Dutra A, Pike B, Root H, Rubenstein J, Boyer R, Stenroos ES, Chandrasekharappa S, Athanassiadou A, Papapetropoulos T, Johnson WG, Lazzarini AM, Duvoisin RC, Di Iorio G, Golbe LI, Nussbaum RL. Mutation in the alpha-synuclein gene identified in families with Parkinson’s disease. Science. 1997;276:2045–7. · DOI · Paper page
  7. Farrer M, Kachergus J, Forno L, Lincoln S, Wang DS, Hulihan M, Maraganore D, Gwinn-Hardy K, Wszolek Z, Dickson D, Langston JW. Comparison of kindreds with parkinsonism and alpha-synuclein genomic multiplications. Ann Neurol. 2004;55:174–9. · DOI
  8. Trinh J, Guella I, Farrer MJ. Disease penetrance of late-onset parkinsonism: a meta-analysis. JAMA Neurol. 2014;71:1535–9. · DOI
  9. Jo E, McLaurin J, Yip CM, St George-Hyslop P, Fraser PE. Alpha-synuclein membrane interactions and lipid specificity. J Biol Chem. 2000;275:34328–34. · DOI
  10. Narhi L, Wood SJ, Steavenson S, Jiang Y, Wu GM, Anafi D, Kaufman SA, Martin F, Sitney K, Denis P, Louis JC, Wypych J, Biere AL, Citron M. Both familial Parkinson’s disease mutations accelerate alpha-synuclein aggregation. J Biol Chem. 1999;274:9843–6. · DOI
  11. Saha AR, Ninkina NN, Hanger DP, Anderton BH, Davies AM, Buchman VL. Induction of neuronal death by alpha-synuclein. Eur J Neurosci. 2000;12:3073–7. · DOI
  12. Zhou W, Hurlbert MS, Schaack J, Prasad KN, Freed CR. Overexpression of human alpha-synuclein causes dopamine neuron death in rat primary culture and immortalized mesencephalon-derived cells. Brain Res. 2000;66:33–43.
  13. Snead D, Eliezer D. Alpha-synuclein function and dysfunction on cellular membranes. Exp Neurobiol. 2014;23:292–313. · DOI
  14. Vargas KJ, Makani S, Davis T, Westphal CH, Castillo PE, Chandra SS. Synucleins regulate the kinetics of synaptic vesicle endocytosis. J Neurosci. 2014;34:9364–76. · DOI
  15. Pacheco C, Aguayo LG, Opazo C. An extracellular mechanism that can explain the neurotoxic effects of α-synuclein aggregates in the brain. Front Physiol. 2012;3:297. · DOI
  16. Lyman M, Lloyd DG, Ji X, Vizcaychipi MP, Ma D. Neuroinflammation: the role and consequences. Neurosci Res. 2014;79:1–12. · DOI
  17. Cunningham C. Microglia and neurodegeneration: the role of systemic inflammation. Glia. 2013;61:71–90. · DOI · Paper page
  18. Michelucci A, Heurtaux T, Grandbarbe L, Morga E, Heuschling P. Characterization of the microglial phenotype under specific pro-inflammatory and anti-inflammatory conditions: effects of oligomeric and fibrillar amyloid-beta. J Neuroimmunol. 2009;210:3–12. · DOI · Paper page
  19. Mandrekar S, Jiang Q, Lee CY, Koenigsknecht-Talboo J, Holtzman DM, Landreth GE. Microglia mediate the clearance of soluble Abeta through fluid phase macropinocytosis. J Neurosci. 2009;29:4252–62. · DOI · Paper page
  20. Pan XD, Zhu YG, Lin N, Zhang J, Ye QY, Huang HP, Chen XC. Microglial phagocytosis induced by fibrillar β-amyloid is attenuated by oligomeric β-amyloid: implications for Alzheimer’s disease. Mol Neurodegener. 2011;6:45. · DOI · Paper page
  21. Russo I, Berti G, Plotegher N, Bernardo G, Filograna R, Bubacco L, Greggio E. Leucine-rich repeat kinase 2 positively regulates inflammation and down-regulates NF-κB p50 signaling in cultured microglia cells. J Neuroinflamm. 2015;12:230. · DOI
  22. Lee HJ, Suk JE, Bae EJ, Lee SJ. Clearance and deposition of extracellular alpha-synuclein aggregates in microglia. Biochem Biophys Res Commun. 2008;372:423–8. · DOI · Paper page
  23. Bae EJ, Lee HJ, Rockenstein E, Ho DH, Park EB, Yang NY, Desplats P, Masliah E, Lee SJ. Antibody-aided clearance of extracellular α-synuclein prevents cell-to-cell aggregate transmission. J Neurosci. 2012;32:13454–69. · DOI · Paper page
  24. Al-Mansoori KM, Hasan MY, Al-Hayani A, El-Agnaf OM. The role of α-synuclein in neurodegenerative diseases: from molecular pathways in disease to therapeutic approaches. Curr Alzheimer Res. 2013;10:559–68. · DOI
  25. Schapira AH, Olanow CW, Greenamyre JT, Bezard E. Slowing of neurodegeneration in Parkinson’s disease and Huntington’s disease: future therapeutic perspectives. Lancet. 2014;384:545–55. · DOI
  26. Funayama M, Hasegawa K, Kowa H, Saito M, Tsuji S, Obata F. A new locus for Parkinson’s disease (PARK8) maps to chromosome 12p11.2-q13.1. Ann Neurol. 2002;51:296–301. · DOI
  27. Funayama M, Hasegawa K, Ohta E, Kawashima N, Komiyama M, Kowa H, Tsuji S, Obata F. An LRRK2 mutation as a cause for the parkinsonism in the original PARK8 family. Ann Neurol. 2005;57:918–21. · DOI
  28. Paisán-Ruíz C, Jain S, Evans EW, Gilks WP, Simón J, van der Brug M, López de Munain A, Aparicio S, Gil AM, Khan N, Johnson J, Martinez JR, Nicholl D, Carrera IM, Pena AS, de Silva R, Lees A, Martí-Massó JF, Pérez-Tur J, Wood NW, Singleton AB. Cloning of the gene containing mutations that cause PARK8-linked Parkinson’s disease. Neuron. 2004;44:595–600. · DOI
  29. Zimprich A, Biskup S, Leitner P, Lichtner P, Farrer M, Lincoln S, Kachergus J, Hulihan M, Uitti RJ, Calne DB, Stoessl AJ, Pfeiffer RF, Patenge N, Carbajal IC, Vieregge P, Asmus F, Müller-Myhsok B, Dickson DW, Meitinger T, Strom TM, Wszolek ZK, Gasser T. Mutations in LRRK2 cause autosomal-dominant parkinsonism with pleomorphic pathology. Neuron. 2004;44:601–7. · DOI
  30. Meylan E, Tschopp J. The RIP kinases: crucial integrators of cellular stress. Trends Biochem Sci. 2005;30:151–9. · DOI
  31. Esteves AR, Swerdlow RH, Cardoso SM. LRRK2, a puzzling protein: insights into Parkinson’s disease pathogenesis. Exp Neurol. 2014;261:206–16. · DOI
  32. Martin I, Kim JW, Dawson VL, Dawson TM. LRRK2 pathobiology in Parkinson’s disease. J Neurochem. 2014;131:554–65. · DOI
  33. Gardet A, Benita Y, Li C, Sands BE, Ballester I, Stevens C, Korzenik JR, Rioux JD, Daly MJ, Xavier RJ, Podolsky DK. LRRK2 is involved in the IFN-gamma response and host response to pathogens. J Immunol. 2010;185:5577–85. · DOI
  34. Kubo M, Kamiya Y, Nagashima R, Maekawa T, Eshima K, Azuma S, Ohta E, Obata F. LRRK2 is expressed in B-2 but not in B-1 B cells, and downregulated by cellular activation. J Neuroimmunol. 2010;229:123–8. · DOI
  35. Hakimi M, Selvanantham T, Swinton E, Padmore RF, Tong Y, Kabbach G, Venderova K, Girardin SE, Bulman DE, Scherzer CR, LaVoie MJ, Gris D, Park DS, Angel JB, Shen J, Philpott DJ, Schlossmacher MG. Parkinson’s disease-linked LRRK2 is expressed in circulating and tissue immune cells and upregulated following recognition of microbial structures. J Neural Transm. 2011;118:795–808. · DOI
  36. Liu Z, Lee J, Krummey S, Lu W, Cai H, Lenardo MJ. The kinase LRRK2 is a regulator of the transcription factor NFAT that modulates the severity of inflammatory bowel disease. Nat Immunol. 2011;12:1063–70. · DOI
  37. Kim B, Yang MS, Choi D, Kim JH, Kim HS, Seol W, Choi S, Jou I, Kim EY, Joe EH. Impaired inflammatory responses in murine Lrrk2-knockdown brain microglia. PLoS ONE. 2012;7:e34693. · DOI
  38. Moehle MS, Webber PJ, Tse T, Sukar N, Standaert DG, DeSilva TM, Cowell RM, West AB. LRRK2 inhibition attenuates microglial inflammatory responses. J Neurosci. 2012;32:1602–11. · DOI · Paper page
  39. Gillardon F, Schmid R, Draheim H. Parkinson’s disease-linked leucine-rich repeat kinase 2(R1441G) mutation increases proinflammatory cytokine release from activated primary microglial cells and resultant neurotoxicity. Neuroscience. 2012;208:41–8. · DOI
  40. Lin X, Parisiadou L, Gu XL, Wang L, Shim H, Sun L, Xie C, Long CX, Yang WJ, Ding J, Chen ZZ, Gallant PE, Tao-Cheng JH, Rudow G, Troncoso JC, Liu Z, Li Z, Cai H. Leucine-rich repeat kinase 2 regulates the progression of neuropathology induced by Parkinson’s-disease-related mutant alpha-synuclein. Neuron. 2009;64:807–27. · DOI
  41. Ni M, Aschner M. Neonatal rat primary microglia: isolation, culturing, and selected applications. Curr Protoc Toxicol 2010, 12: Unit 12.17. · DOI
  42. Lee HJ, Suk JE, Bae EJ, Lee JH, Paik SR, Lee SJ. Assembly-dependent endocytosis and clearance of extracellular alpha-synuclein. Int J Biochem Cell Biol. 2008;40:1835–49. · DOI · Paper page
  43. Shin N, Jeong H, Kwon J, Heo HY, Kwon JJ, Yun HJ, Kim CH, Han BS, Tong Y, Shen J, Hatano T, Hattori N, Kim KS, Chang S, Seol W. LRRK2 regulates synaptic vesicle endocytosis. Exp Cell Res. 2008;314:2055–65. · DOI
  44. Heo HY, Kim KS, Seol W. Coordinate regulation of neurite outgrowth by LRRK2 and its interactor, Rab5. Exp Neurobiol. 2010;19:97–105. · DOI
  45. Sung JY, Kim J, Paik SR, Park JH, Ahn YS, Chung KC. Induction of neuronal cell death by Rab5A-dependent endocytosis of alpha-synuclein. J Biol Chem. 2001;276:27441–8. · DOI
  46. Stafa K, Tsika E, Moser R, Musso A, Glauser L, Jones A, Biskup S, Xiong Y, Bandopadhyay R, Dawson VL, Dawson TM, Moore DJ. Functional interaction of Parkinson’s disease-associated LRRK2 with members of the dynamin GTPase superfamily. Hum Mol Genet. 2014;23:2055–77. · DOI
  47. Yun HJ, Kim H, Ga I, Oh H, Ho DH, Kim J, Seo H, Son I, Seol W. An early endosome regulator, Rab5b, is an LRRK2 kinase substrate. J Biochem. 2015;157:485–95. · DOI
  48. Bhattacharya M, Ojha N, Solanki S, Mukhopadhyay CK, Madan R, Patel N, Krishnamurthy G, Kumar S, Basu SK, Mukhopadhyay A. IL-6 and IL-12 specifically regulate the expression of Rab5 and Rab7 via distinct signaling pathways. EMBO J. 2006;25:2878–88. · DOI
  49. Ozansoy M, Başak AN. The central theme of Parkinson’s disease: α-synuclein. Mol Neurobiol. 2013;47:460–5. · DOI
  50. Hinkle KM, Yue M, Behrouz B, Dächsel JC, Lincoln SJ, Bowles EE, Beevers JE, Dugger B, Winner B, Prots I, Kent CB, Nishioka K, Lin WL, Dickson DW, Janus CJ, Farrer MJ, Melrose HL. LRRK2 knockout mice have an intact dopaminergic system but display alterations in exploratory and motor co-ordination behaviors. Mol Neurodegener. 2012;7:25. · DOI

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Metadata

Authors
Maekawa, T., Sasaoka, T., Azuma, S., Ichikawa, T., Melrose, H. L., Farrer, M. J., & Obata, F.
Venue
BMC Neuroscience
Publisher
Springer Science and Business Media LLC
Published
2016-11-30
Volume
17
Issue
1
ISSN
1471-2202
DOI
10.1186/s12868-016-0315-2
PMC
PMC5131420
Cited by
59
References
8
Language
en
Funders
  • JSPS KAKENHI (25860720)
  • Grant-in-Aid for Scientific Research on Innovative Areas (Comprehensive Brain Science Network) from the Ministry of Education, Science, Sports and Culture of Japan
  • Kitasato University Research Grant for Young Researchers
  • Kitasato University School of Allied Health Sciences

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