Function of α-synuclein and PINK1 in Lewy body dementia (Review)
- Authors:
- Akari Minami
- Atsuko Nakanishi
- Satoru Matsuda
- Yasuko Kitagishi
- Yasunori Ogura
-
Affiliations: Department of Food Science and Nutrition, Nara Women's University, Nara 630-8506, Japan - Published online on: October 27, 2014 https://doi.org/10.3892/ijmm.2014.1980
- Pages: 3-9
This article is mentioned in:
Abstract
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 | |
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 | |
Schwarz S, Froelich L and Burns A: Pharmacological treatment of dementia. Curr Opin Psychiatry. 25:542–550. 2012. View Article : Google Scholar : PubMed/NCBI | |
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 | |
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 | |
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 | |
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 | |
Paleologou KE and El-Agnaf OM: α-synuclein aggregation and modulating factors. Subcell Biochem. 65:109–164. 2012. View Article : Google Scholar | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
Robinson PA: Protein stability and aggregation in Parkinson’s disease. Biochem J. 413:1–13. 2008. View Article : Google Scholar : PubMed/NCBI | |
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 | |
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. | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
Schapira AH and Gegg M: Mitochondrial contribution to Parkinson’s disease pathogenesis. Parkinsons Dis. 2011:1591602011. | |
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 | |
Dias V, Junn E and Mouradian MM: The role of oxidative stress in Parkinson’s disease. J Parkinsons Dis. 3:461–491. 2013. | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 : | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
Galland L: Diet and inflammation. Nutr Clin Pract. 25:234–241. 2010. View Article : Google Scholar | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 |