Addition of Exogenous α-Synuclein Oligomer up-regulates Divalent Metal Transporter-1 and Ferroportin-1 in BV2 Glial Cell Lines

Addition of Exogenous α-Synuclein Oligomer up-regulates Divalent Metal Transporter-1 and Ferroportin-1 in BV2 Glial Cell Lines

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Author(s)

Author(s): Chengkui Shi, Xinxing Du

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DOI: 10.18483/ijSci.1147 288 752 54-60 Volume 5 - Nov 2016

Abstract

It has been confirmed that α-synuclein (α-syn) aggregation in neurons or glia and formation of Lewybodies is the remarked pathognomonic hallmark of PD. Neuropathology study have found α-Syn in abnormal aggregation often accompany with iron deposits. At present ,a lot of research confirmed that divalent metal transporter 1(DMT1), is up-regulated and ferroportin-1 is downregulated in the SN of PD and accumulate of iron in this region.Therefore understanding exogenous α-Syn oligomer whether arise this phenomenon in BV2 glial cell lines is necessary.

Keywords

Microglia cell, α-Synuclein oligomer, Iron, Membrance Transport Proteins

References

  1. Haddad D, Nakamura K. Understanding the susceptibility of dopamine neurons to mitochondrial stressors in Parkinson's disease. FEBS Lett. 2015;589(24 Pt A):3702-3713.
  2. Zeineddine R, Yerbury JJ. The role of macropinocytosis in the propagation of protein aggregation associated with neurodegenerative diseases. Front Physiol. 2015;6:277.
  3. Singh N, Haldar S, Tripathi A K, et al. Iron in neurodegenerative disorders of protein misfolding: a case of prion disorders and Parkinson's disease.[J]. Antioxidants & Redox Signaling, 2014, 21(3):471-84.
  4. Maroteaux L, Campanelli J T, Scheller R H. Synuclein: a neuron-specific protein localized to the nucleus and presynaptic nerve terminal.[J]. Journal of Neuroscience the Official Journal of the Society for Neuroscience, 1988, 8(8):2804-15.
  5. Spillantini M G, Schmidt M L, Lee V M, et al. Alpha-synuclein in Lewy bodies[J]. Nature, 1997, 388(6645):839-840.
  6. Cooper A A, Susan Lindquist I I. α-Synuclein Blocks ER-Golgi Traffic and Rab1 Rescues Neuron Loss in Parkinson's Models[J]. Science, 2006, 313(5785):324-8.
  7. Murphy D D, Rueter S M, Trojanowski J Q, et al. Synucleins are developmentally expressed, and alpha-synuclein regulates the size of the presynaptic vesicular pool in primary hippocampal neurons.[J]. Journal of Neuroscience the Official Journal of the Society for Neuroscience, 2000, 20(9):3214-3220.
  8. Pieri L, Chafey P, Le G M, et al. Cellular response of human neuroblastoma cells to α-synuclein fibrils, the main constituent of Lewy bodies.[J]. Biochimica Et Biophysica Acta, 2015, 1860(1).
  9. Anna Villar-Piqué †, Tomás Lopes da Fonseca †, Outeiro T F. Structure, function and toxicity of alpha-synuclein: the Bermuda triangle in synucleinopathies[J]. Journal of Neurochemistry, 2015.
  10. Leonid Breydo, Jessica W. Wu, Vladimir N. Uversky. α-Synuclein misfolding and Parkinson's disease[J]. Biochimica Et Biophysica Acta, 2012, 1822(2):261-285.
  11. Roberts H L, Brown D R. Seeking a Mechanism for the Toxicity of Oligomeric α-Synuclein.[J]. Biomolecules, 2015, 5(5):282-305.
  12. Rockenstein E, Nuber S, Overk C R, et al. Accumulation of oligomer-prone α-synuclein exacerbates synaptic and neuronal degeneration in vivo[J]. Brain, 2014, 137(Pt 5):1496-513.
  13. Castellani R J, Siedlak S L, Perry G, et al. Sequestration of iron by Lewy bodies in Parkinson's disease.[J]. Acta Neuropathologica, 2000, 100(2):111-4.
  14. Taniguchi R, Kato HE, Font J, et al. Outward- and inward-facing structures of a putative bacterial transition-metal transporter with homology to ferroportin. Nat Commun. 2015; 6:8545.
  15. Roberts R F, Wademartins R, Alegreabarrategui J. Direct visualization of alpha-synuclein oligomers reveals previously undetected pathology in Parkinson's disease brain.[J]. Brain A Journal of Neurology, 2015, 138(6):1642-1657.
  16. Wirdefeldt K, Adami H O, Cole P, et al. Epidemiology and etiology of Parkinson’s disease: a review of the evidence[J]. European Journal of Epidemiology, 2011, 26(1 Supplement):1-58.
  17. Kozlowski H, Luczkowski M, Remelli M, et al. Copper, zinc and iron in neurodegenerative diseases (Alzheimer's, Parkinson's and prion diseases)[J]. Coordination Chemistry Reviews, 2012, 256(s 19–20):2129–2141.
  18. Ostrerova-Golts N, Petrucelli L, Hardy J, et al. The A53T alpha-synuclein mutation increases iron-dependent aggregation and toxicity.[J]. Journal of Neuroscience the Official Journal of the Society for Neuroscience, 2000, 20(16):6048-54.
  19. He Q, Song N, Xu H, et al. Alpha-synuclein aggregation is involved in the toxicity induced by ferric iron to SK-N-SH neuroblastoma cells.[J]. Journal of Neural Transmission, 2011, 118(3):397-406.
  20. Dexter D T, Wells F R, Lee A J, et al. Increased Nigral Iron Content and Alterations in Other Metal Ions Occurring in Brain in Parkinson's Disease[J]. Journal of Neurochemistry, 1989, 52(6):1830-6.
  21. Oakley A E, Collingwood J F, Dobson J, et al. Individual dopaminergic neurons show raised iron levels in Parkinson disease.[J]. Neurology, 2007, 68(21):1820-5.
  22. Castellani R J, Siedlak S L, Perry G, et al. Sequestration of iron by Lewy bodies in Parkinson's disease.[J]. Acta Neuropathologica, 2000, 100(2):111-4.
  23. Gu Y, Hinnerwisch J, Fredricks R, et al. Identification of cryptic nuclear localization signals in the prion protein[J]. Neurobiology of Disease, 2003, 12(2):133-149.
  24. Hare D, Ayton S, Bush A, et al. A delicate balance: Iron metabolism and diseases of the brain[J]. Frontiers in Aging Neuroscience, 2013, 5(34):625-626.
  25. Davies P, Moualla D, Brown D R. Alpha-Synuclein Is a Cellular Ferrireductase[J]. Plos One, 2011, 6(1):111-117.
  26. David N. Hauser, Mark R. Cookson. Astrocytes in Parkinson’s disease and DJ-1[J]. Journal of Neurochemistry, 2011, 117(3):357-8.

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International Journal of Sciences is Open Access Journal.
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