Mechanisms of Neuronal Death in Synucleinopathy
References
J L Eriksen, T M Dawson, D W Dickson, and L Petrucelli, “Caught in the act: -synuclein is the culprit in Parkinson's disease,” Neuron, vol. 40, no. 3, pp. 453–456, 2003.
View at: Google ScholarK K Dev, K Hofele, S Barbieri, V L Buchman, and H Van der Putten, “Part II: -synuclein and its molecular pathophysiological role in neurodegenerative disease,” Neuropharmacology, vol. 45, no. 1, pp. 14–44, 2003.
View at: Google ScholarS Chandra, G Gallardo, R Fernandez-Chacon, O M Schluter, and T C Sudhof, “-synuclein cooperates with CSP in preventing neurodegeneration,” Cell, vol. 123, no. 3, pp. 383–396, 2005.
View at: Google ScholarE Munoz, R Oliva, V Obach et al., “Identification of Spanish familial Parkinson's disease and screening for the Ala53Thr mutation of the -synuclein gene in early onset patients,” Neuroscience Letters, vol. 235, no. 1-2, pp. 57–60, 1997.
View at: Google ScholarR Kruger, W Kuhn, T Muller et al., “Ala30Pro mutation in the gene encoding -synuclein in Parkinson's disease,” Nature Genetics, vol. 18, no. 2, pp. 106–108, 1998.
View at: Google ScholarJ J Zarranz, J Alegre, J C Gomez-Esteban et al., “The new mutation, E46K, of -synuclein causes Parkinson and Lewy body dementia,” Annals of Neurology, vol. 55, no. 2, pp. 164–173, 2004.
View at: Google ScholarM B Feany and W W Bender, “A Drosophila model of Parkinson's disease,” Nature, vol. 404, no. 6776, pp. 394–398, 2000.
View at: Google ScholarJ L Eriksen, Z Wszolek, and L Petrucelli, “Molecular pathogenesis of Parkinson disease,” Archives of Neurology, vol. 62, no. 3, pp. 353–357, 2005.
View at: Google ScholarM Matsuzaki, T Hasegawa, A Takeda et al., “Histochemical features of stress-induced aggregates in -synuclein overexpressing cells,” Brain Research, vol. 1004, no. 1-2, pp. 83–90, 2004.
View at: Google ScholarT Hasegawa, M Matsuzaki, A Takeda et al., “Accelerated -synuclein aggregation after differentiation of SH-SY5Y neuroblastoma cells,” Brain Research, vol. 1013, no. 1, pp. 51–59, 2004.
View at: Google ScholarB I Giasson, J E Duda, I V Murray et al., “Oxidative damage linked to neurodegeneration by selective -synuclein nitration in synucleinopathy lesions,” Science, vol. 290, no. 5493, pp. 985–989, 2000.
View at: Google ScholarS R Paik, H J Shin, and J H Lee, “Metal-catalyzed oxidation of -synuclein in the presence of Copper(II) and hydrogen peroxide,” Archives of Biochemistry and Biophysics, vol. 378, no. 2, pp. 269–277, 2000.
View at: Google ScholarE Paxinou, Q Chen, M Weisse et al., “Induction of -synuclein aggregation by intracellular nitrative insult,” The Journal of Neuroscience, vol. 21, no. 20, pp. 8053–8061, 2001.
View at: Google ScholarV N Uversky, J Li, and A L Fink, “Evidence for a partially folded intermediate in -synuclein fibril formation,” The Journal of Biological Chemistry, vol. 276, no. 14, pp. 10737–10744, 2001.
View at: Google ScholarA Kikuchi, A Takeda, and H Onodera, “Systemic increase of oxidative nucleic acid damage in Parkinson's disease and multiple system atrophy,” Neurobiology of Disease, vol. 9, no. 2, pp. 244–248, 2002.
View at: Google ScholarJ A Johnston, C L Ward, and R R Kopito, “Aggresomes: a cellular response to misfolded proteins,” The Journal of Cell Biology, vol. 143, no. 7, pp. 1883–1898, 1998.
View at: Google ScholarM Tanaka, Y M Kim, G Lee, E Junn, T Iwatsubo, and M M Mouradian, “Aggresomes formed by -synuclein and synphilin-1 are cytoprotective,” The Journal of Biological Chemistry, vol. 279, no. 6, pp. 4625–4631, 2004.
View at: Google ScholarM Arrasate, S Mitra, E S Schweitzer, M R Segal, and S Finkbeiner, “Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death,” Nature, vol. 431, no. 7010, pp. 805–810, 2004.
View at: Google ScholarM Matsuzaki-Kobayashi, T Hasegawa, A Kikuchi, A Takeda, and Y Itoyama, “Role of iron in the intracellular aggregation of -synuclein,” Movement Disorders, vol. 19, no. sup9, p. S36, 2004.
View at: Google ScholarH G Lee, R B Petersen, X Zhu et al., “Will preventing protein aggregates live up to its promise as prophylaxis against neurodegenerative diseases?,” Brain Pathology, vol. 13, no. 4, pp. 630–638, 2003.
View at: Google ScholarS Ueda, S Sakakibara, E Watanabe, K Yoshimoto, and N Koibuchi, “Vulnerability of monoaminergic neurons in the brainstem of the zitter rat in oxidative stress,” Progress in Brain Research, vol. 136, pp. 293–302, 2002.
View at: Google ScholarA H Stokes, T G Hastings, and K E Vrana, “Cytotoxic and genotoxic potential of dopamine,” Journal of Neuroscience Research, vol. 55, no. 6, pp. 659–665, 1999.
View at: Google ScholarJ L Bolton, M A Trush, T M Penning, G Dryhurst, and T J Monks, “Role of quinones in toxicology,” Chemical Research in Toxicology, vol. 13, no. 3, pp. 135–160, 2000.
View at: Google ScholarR G Perez, J C Waymire, E Lin, J J Liu, F Guo, and M J Zigmond, “A role for -synuclein in the regulation of dopamine biosynthesis,” The Journal of Neuroscience, vol. 22, no. 8, pp. 3090–3099, 2002.
View at: Google ScholarF J Lee, F Liu, Z B Pristupa, and H B Niznik, “Direct binding and functional coupling of -synuclein to the dopamine transporters accelerate dopamine-induced apoptosis,” FASEB Journal, vol. 15, no. 6, pp. 916–926, 2001.
View at: Google ScholarR G Perez and T G Hastings, “Could a loss of -synuclein function put dopaminergic neurons at risk?,” Journal of Neurochemistry, vol. 89, no. 6, pp. 1318–1324, 2004.
View at: Google ScholarA Sidhu, C Wersinger, and P Vernier, “-synuclein regulation of the dopaminergic transporter: a possible role in the pathogenesis of Parkinson's disease,” FEBS Letters, vol. 565, no. 1–3, pp. 1–5, 2004.
View at: Google ScholarK A Conway, J C Rochet, R M Bieganski, and P T Jr Lansbury, “Kinetic stabilization of the -synuclein protofibril by a dopamine--synuclein adduct,” Science, vol. 294, no. 5545, pp. 1346–1349, 2001.
View at: Google ScholarH T Li, D H Lin, X Y Luo et al., “Inhibition of -synuclein fibrillization by dopamine analogs via reaction with the amino groups of -synuclein: implication for dopaminergic neurodegeneration,” FEBS Journal, vol. 272, no. 14, pp. 3661–3672, 2005.
View at: Google ScholarA Takeda, Y Tomita, S Okinaga, H Tagami, and S Shibahara, “Functional analysis of the cDNA encoding human tyrosinase precursor,” Biochemical and Biophysical Research Communications, vol. 162, no. 3, pp. 984–990, 1989.
View at: Google ScholarT Hasegawa, M Matsuzaki, A Takeda et al., “Increased dopamine and its metabolites in SH-SY5Y neuroblastoma cells that express tyrosinase,” Journal of Neurochemistry, vol. 87, no. 2, pp. 470–475, 2003.
View at: Google ScholarT Hasegawa, M Matsuzaki-Kobayashi, A Takeda et al., “Synergistic interaction between -synuclein and oxidized catechol metabolites produced by tyrosinase: implications for selective neurodegeneration in Parkinson's disease,” FEBS Letters, vol. 580, pp. 2147–2152, 2006.
View at: Google ScholarH A Lashuel, D Hartley, B M Petre, T Walz, and P T Jr Lansbury, “Neurodegenerative disease: amyloid pores from pathogenic mutations,” Nature, vol. 418, no. 6895, p. 291, 2002.
View at: Google ScholarM J Volles and P T Jr Lansbury, “Vesicle permeabilization by protofibrillar -synuclein is sensitive to Parkinson's disease-linked mutations and occurs by a pore-like mechanism,” Biochemistry, vol. 41, no. 14, pp. 4595–4602, 2002.
View at: Google ScholarR Kayed, Y Sokolov, B Edmonds et al., “Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases,” The Journal of Biological Chemistry, vol. 279, no. 45, pp. 46363–46366, 2004.
View at: Google ScholarM R Gluck and G D Zeevalk, “Inhibition of brain mitochondrial respiration by dopamine and its metabolites: implications for Parkinson's disease and catecholamine-associated diseases,” Journal of Neurochemistry, vol. 91, no. 4, pp. 788–795, 2004.
View at: Google ScholarK Furukawa, M Matsuzaki-Kobayashi, T Hasegawa et al., “High ion permeability of plasma membrane caused by the -synuclein mutations contributes to cellular degeneration,” Journal of Neurochemistry, vol. 97, pp. 1071–1077, 2006.
View at: Google ScholarM P Mattson and S L Chan, “Dysregulation of cellular calcium homeostasis in Alzheimer's disease: bad genes and bad habits,” Journal of Molecular Neuroscience, vol. 17, no. 2, pp. 205–224, 2001.
View at: Google ScholarK Furukawa, Y Wang, P J Yao et al., “Alteration in calcium channel properties is responsible for the neurotoxic action of a familial frontotemporal dementia tau mutation,” Journal of Neurochemistry, vol. 87, no. 2, pp. 427–436, 2003.
View at: Google Scholar