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Review

Function of α-synuclein and PINK1 in Lewy body dementia (Review)

  • Authors:
    • Akari Minami
    • Atsuko Nakanishi
    • Satoru Matsuda
    • Yasuko Kitagishi
    • Yasunori Ogura
  • View Affiliations / Copyright

    Affiliations: Department of Food Science and Nutrition, Nara Women's University, Nara 630-8506, Japan
  • Pages: 3-9
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    Published online on: October 27, 2014
       https://doi.org/10.3892/ijmm.2014.1980
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Abstract

α-synuclein (α-syn) is the major protein component of Lewy bodies, a key pathological characteristic of the degenerating brain. The misfolding and aggregation of α-syn is associated with both the idiopathic and familial forms of Parkinson's disease (PD) and Lewy body dementia (LBD). However, the function of α-syn is poorly understood, as it shows both neurotoxic and neuroprotective activities. Mutations in phosphatase and tensin homologue-induced putative kinase 1 (PINK1) also cause recessively inherited PD. Studies support the notion of neuroprotective roles for PINK1, as it protects cells from damage-induced mitochondrial dysfunction, oxidative stress and cell apoptosis. PINK1 plays an essential role in mitochondrial quality control and its homeostasis is maintained through mitochondrial stabilization. The α-syn aggregation is linked to various aspects of mitochondrial dysfunction and PINK1-related mitophagy. Determination of the molecular pathways that lead to α-syn oligomerization and further aggregation may be the basis for the successful design and development of treatments for these neurodegenerative diseases. The present review summarizes the function of PINK1 underlying α-syn aggregation and the mechanisms through which mitochondrial dysfunction plays a role in this process.
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1 

Overk CR and Masliah E: Pathogenesis of synaptic degeneration in Alzheimer’s disease and Lewy body disease. Biochem Pharmacol. 88:508–516. 2014. View Article : Google Scholar : PubMed/NCBI

2 

Walker LC and LeVine H III: Corruption and spread of pathogenic proteins in neurodegenerative diseases. J Biol Chem. 287:33109–33115. 2012. View Article : Google Scholar : PubMed/NCBI

3 

Schwarz S, Froelich L and Burns A: Pharmacological treatment of dementia. Curr Opin Psychiatry. 25:542–550. 2012. View Article : Google Scholar : PubMed/NCBI

4 

Di Giovanni S, Eleuteri S, Paleologou KE, Yin G, Zweckstetter M, Carrupt PA and Lashuel HA: Entacapone and tolcapone, two catechol O-methyltransferase inhibitors, block fibril formation of alpha-synuclein and beta-amyloid and protect against amyloid-induced toxicity. J Biol Chem. 285:14941–14954. 2010. View Article : Google Scholar : PubMed/NCBI

5 

Crews L, Tsigelny I, Hashimoto M and Masliah E: Role of synucleins in Alzheimer’s disease. Neurotox Res. 16:306–317. 2009. View Article : Google Scholar : PubMed/NCBI

6 

Goldstein DS, Holmes C, Kopin IJ and Sharabi Y: Intra-neuronal vesicular uptake of catecholamines is decreased in patients with Lewy body diseases. J Clin Invest. 121:3320–3330. 2011. View Article : Google Scholar : PubMed/NCBI

7 

Onofrj M, Bonanni L, Manzoli L and Thomas A: Cohort study on somatoform disorders in Parkinson disease and dementia with Lewy bodies. Neurology. 74:1598–1606. 2010. View Article : Google Scholar : PubMed/NCBI

8 

Paleologou KE and El-Agnaf OM: α-synuclein aggregation and modulating factors. Subcell Biochem. 65:109–164. 2012. View Article : Google Scholar

9 

Cheng F, Li X, Li Y, Wang C, Wang T, Liu G, Baskys A, Uéda K, Chan P and Yu S: α-Synuclein promotes clathrin-mediated NMDA receptor endocytosis and attenuates NMDA-induced dopaminergic cell death. J Neurochem. 119:815–825. 2011. View Article : Google Scholar : PubMed/NCBI

10 

Song JX, Lu JH, Liu LF, Chen LL, Durairajan SS, Yue Z, Zhang HQ and Li M: HMGB1 is involved in autophagy inhibition caused by SNCA/α-synuclein overexpression: a process modulated by the natural autophagy inducer corynoxine B. Autophagy. 10:144–154. 2014. View Article : Google Scholar

11 

Settembre C, Fraldi A, Jahreiss L, Spampanato C, Venturi C, Medina D, de Pablo R, Tacchetti C, Rubinsztein DC and Ballabio A: A block of autophagy in lysosomal storage disorders. Hum Mol Genet. 17:119–129. 2008. View Article : Google Scholar

12 

Todde V, Veenhuis M and van der Klei IJ: Autophagy: principles and significance in health and disease. Biochim Biophys Acta. 1792:3–13. 2009. View Article : Google Scholar

13 

Pan T, Kondo S, Le W and Jankovic J: The role of autophagy-lysosome pathway in neurodegeneration associated with Parkinson’s disease. Brain. 131:1969–1978. 2008. View Article : Google Scholar : PubMed/NCBI

14 

Matus S, Valenzuela V and Hetz C: A new method to measure autophagy flux in the nervous system. Autophagy. 10:710–714. 2014. View Article : Google Scholar : PubMed/NCBI

15 

Giordano S, Darley-Usmar V and Zhang J: Autophagy as an essential cellular antioxidant pathway in neurodegenerative disease. Redox Biol. 2:82–90. 2013. View Article : Google Scholar

16 

Spencer B, Potkar R, Trejo M, Rockenstein E, Patrick C, Gindi R, Adame A, Wyss-Coray T and Masliah E: Beclin 1 gene transfer activates autophagy and ameliorates the neurodegenerative pathology in alpha-synuclein models of Parkinson’s and Lewy body diseases. J Neurosci. 29:13578–13588. 2009. View Article : Google Scholar : PubMed/NCBI

17 

Isella V, Rucci F, Traficante D, Mapelli C, Ferri F and Appollonio IM: The applause sign in cortical and cortical-subcortical dementia. J Neurol. 260:1099–1103. 2013. View Article : Google Scholar

18 

Kahle PJ, Neumann M, Ozmen L, Müller V, Odoy S, Okamoto N, Jacobsen H, Iwatsubo T, Trojanowski JQ, Takahashi H, Wakabayashi K, Bogdanovic N, Riederer P, Kretzschmar HA and Haass C: Selective insolubility of alpha-synuclein in human Lewy body diseases is recapitulated in a transgenic mouse model. Am J Patholx. 159:2215–2225. 2013. View Article : Google Scholar

19 

Robinson PA: Protein stability and aggregation in Parkinson’s disease. Biochem J. 413:1–13. 2008. View Article : Google Scholar : PubMed/NCBI

20 

Olanow CW, Perl DP, DeMartino GN and McNaught KS: Lewy-body formation is an aggresome-related process: a hypothesis. Lancet Neurol. 3:496–503. 2004. View Article : Google Scholar : PubMed/NCBI

21 

Braak H, Müller CM, Rüb U, Ackermann H, Bratzke H, de Vos RA and Del Tredici K: Pathology associated with sporadic Parkinson’s disease - where does it end? J Neural Transm Suppl. 70:89–97. 2006.

22 

Luk KC, Hyde EG, Trojanowski JQ and Lee VM: Sensitive fluorescence polarization technique for rapid screening of alpha-synuclein oligomerization/fibrillization inhibitors. Biochemistry. 46:12522–12529. 2007. View Article : Google Scholar : PubMed/NCBI

23 

Ghosh D, Mondal M, Mohite GM, Singh PK, Ranjan P, Anoop A, Ghosh S, Jha NN, Kumar A and Maji SK: The Parkinson’s disease-associated H50Q mutation accelerates α-Synuclein aggregation in vitro. Biochemistry. 52:6925–6927. 2013. View Article : Google Scholar : PubMed/NCBI

24 

Chai YJ, Kim D, Park J, Zhao H, Lee SJ and Chang S: The secreted oligomeric form of α-synuclein affects multiple steps of membrane trafficking. FEBS Lett. 587:452–459. 2013. View Article : Google Scholar : PubMed/NCBI

25 

Campbell BC, McLean CA, Culvenor JG, Gai WP, Blumbergs PC, Jäkälä P, Beyreuther K, Masters CL and Li QX: The solubility of alpha-synuclein in multiple system atrophy differs from that of dementia with Lewy bodies and Parkinson’s disease. J Neurochem. 76:87–96. 2001. View Article : Google Scholar : PubMed/NCBI

26 

Wakabayashi K, Yoshimoto M, Fukushima T, Koide R, Horikawa Y, Morita T and Takahashi H: Widespread occurrence of alpha-synuclein/NACP-immunoreactive neuronal inclusions in juvenile and adult-onset Hallervorden-Spatz disease with Lewy bodies. Neuropathol Appl Neurobiol. 25:363–368. 1999. View Article : Google Scholar : PubMed/NCBI

27 

Sharon R, Goldberg MS, Bar-Josef I, Betensky RA, Shen J and Selkoe DJ: alpha-synuclein occurs in lipid-rich high molecular weight complexes, binds fatty acids, and shows homology to the fatty acid-binding proteins. Proc Natl Acad Sci USA. 98:9110–9115. 2001. View Article : Google Scholar : PubMed/NCBI

28 

Dryanovski DI, Guzman JN, Xie Z, Galteri DJ, Volpicelli-Daley LA, Lee VM, Miller RJ, Schumacker PT and Surmeier DJ: Calcium entry and α-synuclein inclusions elevate dendritic mitochondrial oxidant stress in dopaminergic neurons. J Neurosci. 33:10154–10164. 2013. View Article : Google Scholar : PubMed/NCBI

29 

Müller SK, Bender A, Laub C, Högen T, Schlaudraff F, Liss B, Klopstock T and Elstner M: Lewy body pathology is associated with mitochondrial DNA damage in Parkinson’s disease. Neurobiol Aging. 34:2231–2233. 2013. View Article : Google Scholar

30 

Wilkaniec A, Strosznajder JB and Adamczyk A: Toxicity of extracellular secreted alpha-synuclein: its role in nitrosative stress and neurodegeneration. Neurochem Int. 62:776–783. 2013. View Article : Google Scholar : PubMed/NCBI

31 

Xilouri M, Brekk OR and Stefanis L: α-Synuclein and protein degradation systems: a reciprocal relationship. Mol Neurobiol. 47:537–551. 2013. View Article : Google Scholar

32 

Chinta SJ, Mallajosyula JK, Rane A and Andersen JK: Mitochondrial α-synuclein accumulation impairs complex I function in dopaminergic neurons and results in increased mitophagy in vivo. Neurosci Lett. 486:235–239. 2010. View Article : Google Scholar : PubMed/NCBI

33 

Gandhi S, Muqit MM, Stanyer L, Healy DG, Abou-Sleiman PM, Hargreaves I, Heales S, Ganguly M, Parsons L, Lees AJ, Latchman DS, Holton JL, Wood NW and Revesz T: PINK1 protein in normal human brain and Parkinson’s disease. Brain. 129:1720–1731. 2006. View Article : Google Scholar : PubMed/NCBI

34 

Hong L, Ko HW, Gwag BJ, Joe E, Lee S, Kim YT and Suh YH: The cDNA cloning and ontogeny of mouse alpha-synuclein. Neuroreport. 9:1239–1243. 1998. View Article : Google Scholar : PubMed/NCBI

35 

El-Agnaf OM, Jakes R, Curran MD, Middleton D, Ingenito R, Bianchi E, Pessi A, Neill D and Wallace A: Aggregates from mutant and wild-type alpha-synuclein proteins and NAC peptide induce apoptotic cell death in human neuroblastoma cells by formation of beta-sheet and amyloid-like filaments. FEBS Lett. 440:71–75. 1998. View Article : Google Scholar : PubMed/NCBI

36 

Jensen PH, Hojrup P, Hager H, Nielsen MS, Jacobsen L, Olesen OF, Gliemann J and Jakes R: Binding of Abeta to alpha- and beta-synucleins: identification of segments in alpha-synuclein/NAC precursor that bind Abeta and NAC. Biochem J. 323:539–546. 1997.PubMed/NCBI

37 

Schapira AH and Gegg M: Mitochondrial contribution to Parkinson’s disease pathogenesis. Parkinsons Dis. 2011:1591602011.

38 

Liu F, Hindupur J, Nguyen JL, Ruf KJ, Zhu J, Schieler JL, Bonham CC, Wood KV, Davisson VJ and Rochet JC: Methionine sulfoxide reductase A protects dopaminergic cells from Parkinson’s disease-related insults. Free Radic Biol Med. 45:242–255. 2008. View Article : Google Scholar : PubMed/NCBI

39 

Dias V, Junn E and Mouradian MM: The role of oxidative stress in Parkinson’s disease. J Parkinsons Dis. 3:461–491. 2013.

40 

Weber TA and Reichert AS: Impaired quality control of mitochondria: aging from a new perspective. Exp Gerontol. 45:503–511. 2010. View Article : Google Scholar : PubMed/NCBI

41 

Israeli E and Sharon R: Beta-synuclein occurs in vivo in lipid-associated oligomers and forms hetero-oligomers with alpha-synuclein. J Neurochem. 108:465–474. 2009. View Article : Google Scholar

42 

Valente EM, Abou-Sleiman PM, Caputo V, Muqit MM, Harvey K, Gispert S, Ali Z, Del Turco D, Bentivoglio AR, Healy DG, Albanese A, Nussbaum R, González-Maldonado R, Deller T, Salvi S, Cortelli P, Gilks WP, Latchman DS, Harvey RJ, Dallapiccola B, Auburger G and Wood NW: Hereditary early-onset Parkinson’s disease caused by mutations in PINK1. Science. 304:1158–1160. 2004. View Article : Google Scholar : PubMed/NCBI

43 

Blackinton JG, Anvret A, Beilina A, Olson L, Cookson MR and Galter D: Expression of PINK1 mRNA in human and rodent brain and in Parkinson’s disease. Brain Res. 1184:10–16. 2007. View Article : Google Scholar : PubMed/NCBI

44 

Weihofen A, Thomas KJ, Ostaszewski BL, Cookson MR and Selkoe DJ: Pink1 forms a multiprotein complex with Miro and Milton, linking Pink1 function to mitochondrial trafficking. Biochemistry. 48:2045–2052. 2009. View Article : Google Scholar : PubMed/NCBI

45 

Jin SM, Lazarou M, Wang C, Kane LA, Narendra DP and Youle RJ: Mitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL. J Cell Biol. 191:933–942. 2010. View Article : Google Scholar : PubMed/NCBI

46 

Beilina A, Van Der Brug M, Ahmad R, Kesavapany S, Miller DW, Petsko GA and Cookson MR: Mutations in PTEN-induced putative kinase 1 associated with recessive parkinsonism have differential effects on protein stability. Proc Natl Acad Sci USA. 102:5703–5708. 2005. View Article : Google Scholar : PubMed/NCBI

47 

Pridgeon JW, Olzmann JA, Chin LS and Li L: PINK1 protects against oxidative stress by phosphorylating mitochondrial chaperone TRAP1. PLoS Biol. 5:e1722007. View Article : Google Scholar : PubMed/NCBI

48 

Michiorri S, Gelmetti V, Giarda E, Lombardi F, Romano F, Marongiu R, Nerini-Molteni S, Sale P, Vago R, Arena G, Torosantucci L, Cassina L, Russo MA, Dallapiccola B, Valente EM and Casari G: The Parkinson-associated protein PINK1 interacts with Beclin1 and promotes autophagy. Cell Death Differ. 17:962–974. 2010. View Article : Google Scholar : PubMed/NCBI

49 

Matsuda S, Kitagishi Y and Kobayashi M: Function and characteristics of PINK1 in mitochondria. Oxid Med Cell Longev. 2013:6015872013. View Article : Google Scholar : PubMed/NCBI

50 

Rakovic A, Shurkewitsch K, Seibler P, Grünewald A, Zanon A, Hagenah J, Krainc D and Klein C: Phosphatase and tensin homolog (PTEN)-induced putative kinase 1 (PINK1)-dependent ubiquitination of endogenous Parkin attenuates mitophagy: study in human primary fibroblasts and induced pluripotent stem cell-derived neurons. J Biol Chem. 288:2223–2237. 2013. View Article : Google Scholar :

51 

Chu CT: A pivotal role for PINK1 and autophagy in mitochondrial quality control: implications for Parkinson disease. Hum Mol Genet. 19:R28–R37. 2010. View Article : Google Scholar : PubMed/NCBI

52 

Greene AW, Grenier K, Aguileta MA, Muise S, Farazifard R, Haque ME, McBride HM, Park DS and Fon EA: Mitochondrial processing peptidase regulates PINK1 processing, import and Parkin recruitment. EMBO Rep. 13:378–385. 2012. View Article : Google Scholar : PubMed/NCBI

53 

Dexter DT and Jenner P: Parkinson disease: from pathology to molecular disease mechanisms. Free Radic Biol Med. 62:132–144. 2013. View Article : Google Scholar : PubMed/NCBI

54 

Murakami T, Moriwaki Y, Kawarabayashi T, Nagai M, Ohta Y, Deguchi K, Kurata T, Morimoto N, Takehisa Y, Matsubara E, Ikeda M, Harigaya Y, Shoji M, Takahashi R and Abe K: PINK1, a gene product of PARK6, accumulates in alpha-synucleinopathy brains. J Neurol Neurosurg Psychiatry. 78:653–654. 2007. View Article : Google Scholar : PubMed/NCBI

55 

Butler EK, Voigt A, Lutz AK, Toegel JP, Gerhardt E, Karsten P, Falkenburger B, Reinartz A, Winklhofer KF and Schulz JB: The mitochondrial chaperone protein TRAP1 mitigates α-Synuclein toxicity. PLoS Genet. 8:e10024882012. View Article : Google Scholar

56 

Bornhorst J, Chakraborty S, Meyer S, Lohren H, Brinkhaus SG, Knight AL, Caldwell KA, Caldwell GA, Karst U, Schwerdtle T, Bowman A and Aschner M: The effects of pdr1, djr1.1 and pink1 loss in manganese-induced toxicity and the role of α-synuclein in C. elegans. Metallomics. 6:476–490. 2014. View Article : Google Scholar : PubMed/NCBI

57 

Sampaio-Marques B, Felgueiras C, Silva A, Rodrigues M, Tenreiro S, Franssens V, Reichert AS, Outeiro TF, Winderickx J and Ludovico P: SNCA (α-synuclein)-induced toxicity in yeast cells is dependent on sirtuin 2 (Sir2)-mediated mitophagy. Autophagy. 8:1494–1509. 2012. View Article : Google Scholar : PubMed/NCBI

58 

Todd AM and Staveley BE: Pink1 suppresses alpha-synuclein-induced phenotypes in a Drosophila model of Parkinson’s disease. Genome. 51:1040–1046. 2008. View Article : Google Scholar : PubMed/NCBI

59 

Todd AM and Staveley BE: Expression of Pink1 with α-synuclein in the dopaminergic neurons of Drosophila leads to increases in both lifespan and healthspan. Genet Mol Res. 11:1497–1502. 2012. View Article : Google Scholar : PubMed/NCBI

60 

Hajjar T, Meng GY, Rajion MA, Vidyadaran S, Othman F, Farjam AS, Li TA and Ebrahimi M: Omega 3 polyunsaturated fatty acid improves spatial learning and hippocampal peroxisome proliferator activated receptors (PPARα and PPARγ) gene expression in rats. BMC Neurosci. 13:1092012. View Article : Google Scholar

61 

Galland L: Diet and inflammation. Nutr Clin Pract. 25:234–241. 2010. View Article : Google Scholar

62 

Eckert GP, Franke C, Nöldner M, Rau O, Wurglics M, Schubert-Zsilavecz M and Müller WE: Plant derived omega-3-fatty acids protect mitochondrial function in the brain. Pharmacol Res. 61:234–241. 2010. View Article : Google Scholar : PubMed/NCBI

63 

Lee J, Park S, Lee JY, Yeo YK, Kim JS and Lim J: Improved spatial learning and memory by perilla diet is correlated with immunoreactivities to neurofilament and α-synuclein in hilus of dentate gyrus. Proteome Sci. 10:722012. View Article : Google Scholar

64 

Pabon MM, Jernberg JN, Morganti J, Contreras J, Hudson CE, Klein RL and Bickford PC: A spirulina-enhanced diet provides neuroprotection in an α-synuclein model of Parkinson’s disease. PLoS One. 7:e452562012. View Article : Google Scholar

65 

Villegas I, Sánchez-Fidalgo S and Alarcón de la Lastra C: New mechanisms and therapeutic potential of curcumin for colorectal cancer. Mol Nutr Food Res. 52:1040–1061. 2008. View Article : Google Scholar : PubMed/NCBI

66 

Singh PK, Kotia V, Ghosh D, Mohite GM, Kumar A and Maji SK: Curcumin modulates α-synuclein aggregation and toxicity. ACS Chem Neurosci. 4:393–407. 2013. View Article : Google Scholar : PubMed/NCBI

67 

Ahmad B and Lapidus LJ: Curcumin prevents aggregation in α-synuclein by increasing reconfiguration rate. J Biol Chem. 287:9193–9199. 2012. View Article : Google Scholar : PubMed/NCBI

68 

Das S, Mitrovsky G, Vasanthi HR and Das DK: Antiaging properties of a grape-derived antioxidant are regulated by mitochondrial balance of fusion and fission leading to mitophagy triggered by a signaling network of Sirt1-Sirt3-Foxo3-PINK1-PARKIN. Oxid Med Cell Longev. 2014:3451052014. View Article : Google Scholar : PubMed/NCBI

69 

Eid N, Ito Y, Maemura K and Otsuki Y: Elevated autophagic sequestration of mitochondria and lipid droplets in steatotic hepatocytes of chronic ethanol-treated rats: an immunohistochemical and electron microscopic study. J Mol Histol. 44:311–326. 2013. View Article : Google Scholar : PubMed/NCBI

70 

Kones R: Parkinson’s disease: mitochondrial molecular pathology, inflammation, statins, and therapeutic neuroprotective nutrition. Nutr Clin Pract. 25:371–389. 2010. View Article : Google Scholar : PubMed/NCBI

71 

Girish C and Muralidhara: Propensity of Selaginella delicatula aqueous extract to offset rotenone-induced oxidative dysfunctions and neurotoxicity in Drosophila melanogaster: implications for Parkinson’s disease. Neurotoxicology. 33:444–456. 2012. View Article : Google Scholar : PubMed/NCBI

72 

Chen L, Thiruchelvam MJ, Madura K and Richfield EK: Proteasome dysfunction in aged human alpha-synuclein transgenic mice. Neurobiol Dis. 23:120–126. 2006. View Article : Google Scholar : PubMed/NCBI

73 

Liu W, Vives-Bauza C, Acín-Peréz- R, Yamamoto A, Tan Y, Li Y, Magrané J, Stavarache MA, Shaffer S, Chang S, Kaplitt MG, Huang XY, Beal MF, Manfredi G and Li C: PINK1 defect causes mitochondrial dysfunction, proteasomal deficit and alpha-synuclein aggregation in cell culture models of Parkinson’s disease. PLoS One. 4:e45972009. View Article : Google Scholar

74 

Kamp F, Exner N, Lutz AK, Wender N, Hegermann J, Brunner B, Nuscher B, Bartels T, Giese A, Beyer K, Eimer S, Winklhofer KF and Haass C: Inhibition of mitochondrial fusion by α-synuclein is rescued by PINK1, Parkin and DJ-1. EMBO J. 29:3571–3589. 2010. View Article : Google Scholar : PubMed/NCBI

75 

Wilhelmus MM, Nijland PG, Drukarch B, de Vries HE and van Horssen J: Involvement and interplay of Parkin, PINK1, and DJ1 in neurodegenerative and neuroinflammatory disorders. Free Radic Biol Med. 53:983–992. 2012. View Article : Google Scholar : PubMed/NCBI

76 

Tamura T, Yoshida M, Hashizume Y and Sobue G: Lewy body-related α-synucleinopathy in the spinal cord of cases with incidental Lewy body disease. Neuropathology. 32:13–22. 2012. View Article : Google Scholar : PubMed/NCBI

77 

Funabe S, Takao M, Saito Y, Hatsuta H, Sugiyama M, Ito S, Kanemaru K, Sawabe M, Arai T, Mochizuki H, Hattori N and Murayama S: Neuropathologic analysis of Lewy-related α-synucleinopathy in olfactory mucosa. Neuropathology. 33:47–58. 2013. View Article : Google Scholar

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Copy and paste a formatted citation
Spandidos Publications style
Minami A, Nakanishi A, Matsuda S, Kitagishi Y and Ogura Y: Function of α-synuclein and PINK1 in Lewy body dementia (Review). Int J Mol Med 35: 3-9, 2015.
APA
Minami, A., Nakanishi, A., Matsuda, S., Kitagishi, Y., & Ogura, Y. (2015). Function of α-synuclein and PINK1 in Lewy body dementia (Review). International Journal of Molecular Medicine, 35, 3-9. https://doi.org/10.3892/ijmm.2014.1980
MLA
Minami, A., Nakanishi, A., Matsuda, S., Kitagishi, Y., Ogura, Y."Function of α-synuclein and PINK1 in Lewy body dementia (Review)". International Journal of Molecular Medicine 35.1 (2015): 3-9.
Chicago
Minami, A., Nakanishi, A., Matsuda, S., Kitagishi, Y., Ogura, Y."Function of α-synuclein and PINK1 in Lewy body dementia (Review)". International Journal of Molecular Medicine 35, no. 1 (2015): 3-9. https://doi.org/10.3892/ijmm.2014.1980
Copy and paste a formatted citation
x
Spandidos Publications style
Minami A, Nakanishi A, Matsuda S, Kitagishi Y and Ogura Y: Function of α-synuclein and PINK1 in Lewy body dementia (Review). Int J Mol Med 35: 3-9, 2015.
APA
Minami, A., Nakanishi, A., Matsuda, S., Kitagishi, Y., & Ogura, Y. (2015). Function of α-synuclein and PINK1 in Lewy body dementia (Review). International Journal of Molecular Medicine, 35, 3-9. https://doi.org/10.3892/ijmm.2014.1980
MLA
Minami, A., Nakanishi, A., Matsuda, S., Kitagishi, Y., Ogura, Y."Function of α-synuclein and PINK1 in Lewy body dementia (Review)". International Journal of Molecular Medicine 35.1 (2015): 3-9.
Chicago
Minami, A., Nakanishi, A., Matsuda, S., Kitagishi, Y., Ogura, Y."Function of α-synuclein and PINK1 in Lewy body dementia (Review)". International Journal of Molecular Medicine 35, no. 1 (2015): 3-9. https://doi.org/10.3892/ijmm.2014.1980
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