Dopamine facilitates α-synuclein oligomerization in human neuroblastoma SH-SY5Y cells

Biochemical and Biophysical Research Communications

Volumn 391, Issue 1, 2010, Pages 129-134

  Yamakawa, Kentaro ^a   Izumi, Yasuhiko ^b   Takeuchi, Hiroki ^b   Yamamoto, Noriyuki ^b   Kume, Toshiaki ^b   Akaike, Akinori ^b   Takahashi, Ryosuke ^b   Shimohama, Shun ^b,c   Sawada, Hideyuki ^a  

^a UTANO NATIONAL HOSPITAL   (Japan)

^b KYOTO UNIVERSITY   (Japan)

^c SAPPORO MEDICAL UNIVERSITY SCHOOL OF MEDICINE   (Japan)

Author keywords

Synuclein; Aggregation; Dopamine; Oligomer; Parkinson's disease; Size exclusion chromatography

Indexed keywords

ALPHA SYNUCLEIN; DOPAMINE; OLIGOMER;

APOPTOSIS; ARTICLE; CELL DEATH; CONTROLLED STUDY; CYTOTOXICITY; DOPAMINERGIC NERVE CELL; EXPOSURE; GEL PERMEATION CHROMATOGRAPHY; GENE OVEREXPRESSION; HUMAN; HUMAN CELL; NEUROBLASTOMA CELL; NEUROBLASTOMA SH SY5Y CELL; OLIGOMERIZATION; PRIORITY JOURNAL; WESTERN BLOTTING; WILD TYPE;

ALPHA-SYNUCLEIN; APOPTOSIS; BLOTTING, WESTERN; CELL LINE, TUMOR; CHROMATOGRAPHY, GEL; DOPAMINE; HUMANS; LEWY BODIES; NEURONS; PARKINSON DISEASE; SUBSTANTIA NIGRA;

EID: 72949105341     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.11.015     Document Type: Article

References (14)

1. Jakes R., Spillantini M.G., and Goedert M. Identification of two distinct synucleins from human brain. FEBS Lett. 345 (1994) 27-32
2. Iwai A., Masliah E., Yoshimoto M., Ge N., Flanagan L., de Silva H.A., Kittel A., and Saitoh T. The precursor protein of non-A beta component of Alzheimer's disease amyloid is a presynaptic protein of the central nervous system. Neuron 14 (1995) 467-475
3. Weinreb P.H., Zhen W., Poon A.W., Conway K.A., and Lansbury Jr. P.T. NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded. Biochemistry 35 (1996) 13709-13715
4. Waxman E.A., and Giasson B.I. Molecular mechanisms of alpha-synuclein neurodegeneration. Biochim. Biophys. Acta 1792 (2009) 616-624
5. Volles M.J., and Lansbury Jr. P.T. Zeroing in on the pathogenic form of alpha-synuclein and its mechanism of neurotoxicity in Parkinson's disease. Biochemistry 42 (2003) 7871-7878
6. Conway K.A., Rochet J.C., Bieganski R.M., and Lansbury Jr. P.T. Kinetic stabilization of the alpha-synuclein protofibril by a dopamine-alpha-synuclein adduct. Science 294 (2001) 1346-1349
7. Cappai R., Leck S.L., Tew D.J., Williamson N.A., Smith D.P., Galatis D., Sharples R.A., Curtain C.C., Ali F.E., Cherny R.A., Culvenor J.G., Bottomley S.P., Masters C.L., Barnham K.J., and Hill A.F. Dopamine promotes alpha-synuclein aggregation into SDS-resistant soluble oligomers via a distinct folding pathway. FASEB J. 19 (2005) 1377-1379
8. Mazzulli J.R., Mishizen A.J., Giasson B.I., Lynch D.R., Thomas S.A., Nakashima A., Nagatsu T., Ota A., and Ischiropoulos H. Cytosolic catechols inhibit alpha-synuclein aggregation and facilitate the formation of intracellular soluble oligomeric intermediates. J. Neurosci. 26 (2006) 10068-10078
9. Moussa C.E., Mahmoodian F., Tomita Y., and Sidhu A. Dopamine differentially induces aggregation of A53T mutant and wild type alpha-synuclein: insights into the protein chemistry of Parkinson's disease. Biochem. Biophys. Res. Commun. 365 (2008) 833-839
10. Kohno R., Sawada H., Kawamoto Y., Uemura K., Shibasaki H., and Shimohama S. BDNF is induced by wild-type alpha-synuclein but not by the two mutants, A30P or A53T, in glioma cell line. Biochem. Biophys. Res. Commun. 318 (2004) 113-118
11. Izumi Y., Sawada H., Sakka N., Yamamoto N., Kume T., Katsuki H., Shimohama S., and Akaike A. p-Quinone mediates 6-hydroxydopamine-induced dopaminergic neuronal death and ferrous iron accelerates the conversion of p-quinone into melanin extracellularly. J. Neurosci. Res. 79 (2005) 849-860
12. Xu J., Kao S.Y., Lee F.J., Song W., Jin L.W., and Yankner B.A. Dopamine-dependent neurotoxicity of alpha-synuclein: a mechanism for selective neurodegeneration in Parkinson disease. Nat. Med. 8 (2002) 600-606
13. Cookson M.R., and van der Brug M. Cell systems and the toxic mechanism(s) of alpha-synuclein. Exp. Neurol. 209 (2008) 5-11
14. Sharon R., Bar-Joseph I., Frosch M.P., Walsh D.M., Hamilton J.A., and Selkoe D.J. The formation of highly soluble oligomers of alpha-synuclein is regulated by fatty acids and enhanced in Parkinson's disease. Neuron 37 (2003) 583-595