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Volumn 24, Issue SUPPL. 2, 2011, Pages 211-221

Role of advanced glycation on aggregation and DNA binding properties of α-synuclein

Author keywords

AGEs; DNA conformation; glycation; Parkinson's disease; protein aggregation; synuclein

Indexed keywords

ADVANCED GLYCATION END PRODUCT; ALPHA SYNUCLEIN; DEOXYRIBONUCLEASE I; DNA; ETHIDIUM BROMIDE; FRUCTOSAMINE; METHYLGLYOXAL; TYROSINE;

EID: 79955657305     PISSN: 13872877     EISSN: None     Source Type: Journal    
DOI: 10.3233/JAD-2011-101965     Document Type: Article
Times cited : (72)

References (51)
  • 1
    • 74249119940 scopus 로고    scopus 로고
    • Etiopathogenesis and treatment of Parkinson's disease
    • Gallagher DA, Schapira AH (2009) Etiopathogenesis and treatment of Parkinson's disease. Curr Top Med Chem 9, 860-868.
    • (2009) Curr Top Med Chem , vol.9 , pp. 860-868
    • Gallagher, D.A.1    Schapira, A.H.2
  • 2
    • 59649110692 scopus 로고    scopus 로고
    • Structural insights on physiological functions and pathological effects of alphasynuclein
    • Bisaglia M, Mammi S, Bubacco L (2009) Structural insights on physiological functions and pathological effects of alphasynuclein. FASEB J 23, 329-340.
    • (2009) FASEB J , vol.23 , pp. 329-340
    • Bisaglia, M.1    Mammi, S.2    Bubacco, L.3
  • 3
    • 43449091022 scopus 로고    scopus 로고
    • α-synuclein and Parkinson's disease: A proteomic view
    • DOI 10.1586/14789450.5.2.239
    • Fasano M, Lopiano L (2008) Alpha-synuclein and Parkinson's disease: a proteomic view. Expert Rev Proteomics 5, 239-248. (Pubitemid 351670928)
    • (2008) Expert Review of Proteomics , vol.5 , Issue.2 , pp. 239-248
    • Fasano, M.1    Lopiano, L.2
  • 4
    • 68749116710 scopus 로고    scopus 로고
    • A critical evaluation of current staging of alpha-synuclein pathology in Lewy body disorders
    • Jellinger KA (2009) A critical evaluation of current staging of alpha-synuclein pathology in Lewy body disorders. Biochim Biophys Acta 1792, 730-740.
    • (2009) Biochim Biophys Acta , vol.1792 , pp. 730-740
    • Jellinger, K.A.1
  • 5
    • 0023722437 scopus 로고
    • Synuclein: A neuron-specific protein localized to the nucleus and presynaptic nerve terminal
    • Maroteaux L, Campanelli JT, Scheller RH (1988) Synuclein: a neuron-specific protein localized to the nucleus and presynaptic nerve terminal. J Neurosci 8, 2804-2815.
    • (1988) J Neurosci , vol.8 , pp. 2804-2815
    • Maroteaux, L.1    Campanelli, J.T.2    Scheller, R.H.3
  • 6
    • 77951248437 scopus 로고    scopus 로고
    • DNA induced folding/fibrillation of alpha-synuclein: New insights in Parkinson's disease
    • Hegde ML, Vasudevaraju P, Rao KJ (2010) DNA induced folding/fibrillation of alpha-synuclein: new insights in Parkinson's disease. Front Biosci 15, 418-436.
    • (2010) Front Biosci , vol.15 , pp. 418-436
    • Hegde, M.L.1    Vasudevaraju, P.2    Rao, K.J.3
  • 8
    • 0038279986 scopus 로고    scopus 로고
    • α-synuclein: Its biological function and role in neurodegenerative diseases
    • DOI 10.1385/JMN:20:2:83
    • Kaplan B, Ratner V, Haas E (2003) Alpha-synuclein: its biological function and role in neurodegenerative diseases. JMol Neurosci 20, 83-92. (Pubitemid 36693813)
    • (2003) Journal of Molecular Neuroscience , vol.20 , Issue.2 , pp. 83-92
    • Kaplan, B.1    Ratner, V.2    Haas, E.3
  • 10
    • 34247139885 scopus 로고    scopus 로고
    • Over-expression of alpha-synuclein in human neural progenitors leads to specific changes in fate and differentiation
    • DOI 10.1093/hmg/ddm008
    • Schneider BL, Seehus CR, Capowski EE, Aebischer P, Zhang SC, Svendsen CN (2007) Over-expression of alpha-synuclein in human neural progenitors leads to specific changes in fate and differentiation. Hum Mol Genet 16, 651-666. (Pubitemid 46591118)
    • (2007) Human Molecular Genetics , vol.16 , Issue.6 , pp. 651-666
    • Schneider, B.L.1    Seehus, C.R.2    Capowski, E.E.3    Aebischer, P.4    Zhang, S.-C.5    Svendsen, C.N.6
  • 11
    • 0037150773 scopus 로고    scopus 로고
    • Immunohistochemical comparison of α- and β-synuclein in adult rat central nervous system
    • DOI 10.1016/S0006-8993(02)02643-4, PII S0006899302026434
    • Mori F, Tanji K, Yoshimoto M, Takahashi H, Wakabayashi K (2002) Immunohistochemical comparison of alpha-and beta-synuclein in adult rat central nervous system. Brain Res 941, 118-126. (Pubitemid 34603290)
    • (2002) Brain Research , vol.941 , Issue.1-2 , pp. 118-126
    • Mori, F.1    Tanji, K.2    Yoshimoto, M.3    Takahashi, H.4    Wakabayashi, K.5
  • 13
    • 4043107784 scopus 로고    scopus 로고
    • Inhibition of tyrosine hydroxylase expression in α-synuclein- transfected dopaminergic neuronal cells
    • DOI 10.1016/j.neulet.2004.05.118, PII S0304394004006755
    • Yu S, Zuo X, Li Y, Zhang C, Zhou M, Zhang YA, Uéda K, Chan P (2004) Inhibition of tyrosine hydroxylase expression in alpha-synuclein- transfected dopaminergic neuronal cells. Neurosci Lett 367, 34-39. (Pubitemid 39078779)
    • (2004) Neuroscience Letters , vol.367 , Issue.1 , pp. 34-39
    • Yu, S.1    Zuo, X.2    Li, Y.3    Zhang, C.4    Zhou, M.5    Zhang, Y.A.6    Ueda, K.7    Chan, P.8
  • 14
    • 33749583553 scopus 로고    scopus 로고
    • α-synuclein acts in the nucleus to inhibit histone acetylation and promote neurotoxicity
    • DOI 10.1093/hmg/ddl243
    • Kontopoulos E, Parvin JD, Feany MB (2006) Alpha-synuclein acts in the nucleus to inhibit histone acetylation and promote neurotoxicity. Hum Mol Genet 15, 3012-3023. (Pubitemid 44530705)
    • (2006) Human Molecular Genetics , vol.15 , Issue.20 , pp. 3012-3023
    • Kontopoulos, E.1    Parvin, J.D.2    Feany, M.B.3
  • 16
    • 0141540494 scopus 로고    scopus 로고
    • Challenges and complexities of α-synuclein toxicity: New postulates in unfolding the mystery associated with Parkinson's disease
    • DOI 10.1016/j.abb.2003.08.015
    • Hegde ML, Jagannatha Rao KS (2003) Challenges and complexities of alpha-synuclein toxicity: new postulates in unfolding the mystery associated with Parkinson's disease. Arch Biochem Biophys 418, 169-178. (Pubitemid 37159383)
    • (2003) Archives of Biochemistry and Biophysics , vol.418 , Issue.2 , pp. 169-178
    • Hegde, M.L.1    Jagannatha Rao, K.S.2
  • 17
    • 34447618598 scopus 로고    scopus 로고
    • DNA induces folding in α-synuclein: Understanding the mechanism using chaperone property of osmolytes
    • DOI 10.1016/j.abb.2007.03.042, PII S0003986107001634
    • Hegde ML, Rao KS (2007) DNA induces folding in alpha-synuclein: understanding the mechanism using chaperone property of osmolytes. Arch Biochem Biophys 464, 57-69. (Pubitemid 47088357)
    • (2007) Archives of Biochemistry and Biophysics , vol.464 , Issue.1 , pp. 57-69
    • Hegde, M.L.1    Rao, K.S.J.2
  • 18
    • 8544264563 scopus 로고    scopus 로고
    • Double-stranded DNA stimulates the fibrillation of α-synuclein in vitro and is associated with the mature fibrils: An electron microscopy study
    • DOI 10.1016/j.jmb.2004.09.096, PII S0022283604012677
    • Cherny D, Hoyer W, Subramaniam V, Jovin TM (2004) Double-stranded DNA stimulates the fibrillation of alpha-synuclein in vitro and is associated with the mature fibrils: an electron microscopy study. J Mol Biol 344, 929-938. (Pubitemid 39491240)
    • (2004) Journal of Molecular Biology , vol.344 , Issue.4 , pp. 929-938
    • Cherny, D.1    Hoyer, W.2    Subramaniam, V.3    Jovin, T.M.4
  • 20
    • 68649095418 scopus 로고    scopus 로고
    • Molecular mechanisms of alpha-synuclein neurodegeneration
    • Waxman EA, Giasson BI (2009) Molecular mechanisms of alpha-synuclein neurodegeneration. Biochim Biophys Acta 1792, 616-624.
    • (2009) Biochim Biophys Acta , vol.1792 , pp. 616-624
    • Waxman, E.A.1    Giasson, B.I.2
  • 21
    • 70349503591 scopus 로고    scopus 로고
    • Biophysics of Parkinson's disease: Structure and aggregation of alpha-synuclein
    • Uversky VN, Eliezer D (2009) Biophysics of Parkinson's disease: structure and aggregation of alpha-synuclein. Curr Protein Pept Sci 10, 483-499.
    • (2009) Curr Protein Pept Sci , vol.10 , pp. 483-499
    • Uversky, V.N.1    Eliezer, D.2
  • 22
    • 35848966786 scopus 로고    scopus 로고
    • Protein aggregation mechanisms in synucleinopathies: Commonalities and differences
    • DOI 10.1097/nen.0b013e3181587d64, PII 0000507220071100000001
    • Beyer K, Ariza A (2007) Protein aggregation mechanisms in synucleinopathies: commonalities and differences. J Neu-ropathol Exp Neurol 66, 965-974. (Pubitemid 350060365)
    • (2007) Journal of Neuropathology and Experimental Neurology , vol.66 , Issue.11 , pp. 965-974
    • Beyer, K.1    Ariza, A.2
  • 24
    • 0026347369 scopus 로고
    • Advanced nonenzymatic glycation endproducts (AGE): Their relevance to aging and the pathogenesis of late diabetic complications
    • Sensi M, Pricci F, Andreani D, Di Mario U (1991) Advanced nonenzymatic glycation endproducts (AGE): their relevance to aging and the pathogenesis of late diabetic complications. Diabetes Res 16, 1-9.
    • (1991) Diabetes Res , vol.16 , pp. 1-9
    • Sensi, M.1    Pricci, F.2    Andreani, D.3    Di Mario, U.4
  • 25
    • 0027561888 scopus 로고
    • The relationship between diabetes mellitus and Parkinson's disease
    • Sandyk R (1993) The relationship between diabetes mellitus and Parkinson's disease. Int J Neurosci 69, 125-130.
    • (1993) Int J Neurosci , vol.69 , pp. 125-130
    • Sandyk, R.1
  • 26
    • 0034468706 scopus 로고    scopus 로고
    • Crosslinking of α-synuclein by advanced glycation endproducts - An early pathophysiological step in Lewy body formation?
    • DOI 10.1016/S0891-0618(00)00096-X, PII S089106180000096X
    • Münch G, Lüth HJ, Wong A, Arendt T, Hirsch E, Ravid R, Riederer P (2000) Crosslinking of alpha-synuclein by advanced glycation endproducts-an early pathophysiologi-cal step in Lewy body formation? J Chem Neuroanat 20, 253-257. (Pubitemid 32162884)
    • (2000) Journal of Chemical Neuroanatomy , vol.20 , Issue.3-4 , pp. 253-257
    • Munch, G.1    Luth, H.J.2    Wong, A.3    Arendt, Th.4    Hirsch, E.5    Ravid, R.6    Riederer, P.7
  • 27
    • 48249103154 scopus 로고    scopus 로고
    • Advanced glycation end products induce in vitro cross-linking of alpha-synuclein and accelerate the process of intracellular inclusion body formation
    • Shaikh S, Nicholson LF (2008) Advanced glycation end products induce in vitro cross-linking of alpha-synuclein and accelerate the process of intracellular inclusion body formation. J Neurosci Res 86, 2071-2082.
    • (2008) J Neurosci Res , vol.86 , pp. 2071-2082
    • Shaikh, S.1    Nicholson, L.F.2
  • 28
    • 0037378026 scopus 로고    scopus 로고
    • Oxidative stress in Parkinson's disease
    • discussion S36-S38
    • Jenner P (2003) Oxidative stress in Parkinson's disease. Ann Neurol 53 Suppl 3, S26-S36; discussion S36-S38.
    • (2003) Ann Neurol , vol.53 , Issue.SUPPL. 3
    • Jenner, P.1
  • 29
    • 0021231172 scopus 로고
    • Nonenzymatic glycosylation and the pathogenesis of diabetic complications
    • Brownlee M, Vlassara H, Cerami A (1984) Nonenzymatic glycosylation and the pathogenesis of diabetic complications. Ann Intern Med 101, 527-537. (Pubitemid 14018054)
    • (1984) Annals of Internal Medicine , vol.101 , Issue.4 , pp. 527-537
    • Brownlee, M.1    Vlassara, H.2    Cerami, A.3
  • 33
    • 78449282609 scopus 로고    scopus 로고
    • Metals, oxidative stress and neurodegenerative disorders
    • Jomova K, Vondrakova D, Lawson M, Valko M (2010) Metals, oxidative stress and neurodegenerative disorders. Mol Cell Biochem 345, 91-104.
    • (2010) Mol Cell Biochem , vol.345 , pp. 91-104
    • Jomova, K.1    Vondrakova, D.2    Lawson, M.3    Valko, M.4
  • 34
    • 77950989148 scopus 로고    scopus 로고
    • The sour side of neurodegenerative disorders: The effects of protein glycation
    • Vicente Miranda H, Outeiro TF (2010) The sour side of neurodegenerative disorders: the effects of protein glycation. J Pathol 221, 13-25.
    • (2010) J Pathol , vol.221 , pp. 13-25
    • Vicente Miranda, H.1    Outeiro, T.F.2
  • 35
    • 77954142794 scopus 로고    scopus 로고
    • Advancedglycation end products enhance amyloid precursor protein expression by inducing reactive oxygen species
    • Ko SY, Lin YP, Lin YS, Chang SS (2010) Advancedglycation end products enhance amyloid precursor protein expression by inducing reactive oxygen species. Free Radic Biol Med 49, 474-480.
    • (2010) Free Radic Biol Med , vol.49 , pp. 474-480
    • Ko, S.Y.1    Lin, Y.P.2    Lin, Y.S.3    Chang, S.S.4
  • 36
    • 77951647591 scopus 로고    scopus 로고
    • RAGE-dependent signaling in microglia contributes to neuroinflammation, Abeta accumulation, and impaired learning/memory in a mouse model of Alzheimer's disease
    • Fang F, Lue LF, Yan S, Xu H, Luddy JS, Chen D, Walker DG, Stern DM, Yan S, Schmidt AM, Chen JX, Yan SS (2010) RAGE-dependent signaling in microglia contributes to neuroinflammation, Abeta accumulation, and impaired learning/memory in a mouse model of Alzheimer's disease. FASEB J24, 1043-1055.
    • (2010) FASEB J , vol.24 , pp. 1043-1055
    • Fang, F.1    Lue, L.F.2    Yan, S.3    Xu, H.4    Luddy, J.S.5    Chen, D.6    Walker, D.G.7    Stern, D.M.8    Yan, S.9    Schmidt, A.M.10    Chen, J.X.11    Yan, S.S.12
  • 37
    • 0029912028 scopus 로고    scopus 로고
    • Dynamics ofribonuclease A and ribonuclease S: Computationalandexperimentalstudies
    • Nadig G, Ratnaparkhi GS, Varadarajan R, Vishveshwara S (1996) Dynamics ofribonuclease A and ribonuclease S: computationalandexperimentalstudies.Protein Sci5, 2104-2114.
    • (1996) Protein Sci , vol.5 , pp. 2104-2114
    • Nadig, G.1    Ratnaparkhi, G.S.2    Varadarajan, R.3    Vishveshwara, S.4
  • 39
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 40
    • 0022406591 scopus 로고
    • Quasielastic laser light scattering and electron microscopy studies of the conformational transitions and condensation of poly(dA-dT)·poly(dA- dT)
    • DOI 10.1002/bip.360241203
    • Thomas TJ, Bloomfield VA (1985) Quasielastic laser light scattering and electron microscopy studies of the conformational transitions and condensation of poly(dA-dT).poly(dA-dT). Biopolymers 24, 2185-2194. (Pubitemid 16180662)
    • (1985) Biopolymers , vol.24 , Issue.12 , pp. 2185-2194
    • Thomas, T.J.1    Bloomfield, V.A.2
  • 41
    • 84969001783 scopus 로고
    • The attraction of proteins for small molecules and ions
    • Scatchard G (1949) The attraction of proteins for small molecules and ions. Ann N Y Acad Sci 51, 660-672.
    • (1949) Ann N y Acad Sci , vol.51 , pp. 660-672
    • Scatchard, G.1
  • 42
    • 0028380369 scopus 로고
    • Superhelical density of goat mitochondrial DNA: Fluorescent studies
    • Chatterjee B, Rao GRK (1994) Superhelical density of goat mitochondrial DNA: Fluorescent studies. Indian J Biochem Biophys 31, 77-79.
    • (1994) Indian J Biochem Biophys , vol.31 , pp. 77-79
    • Chatterjee, B.1    Grk, R.2
  • 43
    • 0035941201 scopus 로고    scopus 로고
    • Metal-triggered struc-tural transformations, aggregation, and fibrillation of human alpha-synuclein. A possible molecular NK between Parkin-son's disease and heavy metal exposure
    • Uversky VN, Li J, Fink AL (2001) Metal-triggered struc-tural transformations, aggregation, and fibrillation of human alpha-synuclein. A possible molecular NK between Parkin-son's disease and heavy metal exposure. J Biol Chem 276, 44284-44296.
    • (2001) J Biol Chem , vol.276 , pp. 44284-44296
    • Uversky, V.N.1    Li, J.2    Fink, A.L.3
  • 44
    • 0017874455 scopus 로고
    • Dehydrated circular DNA: circular dichroism of molecules in ethanolic solutions
    • Gray DM, Taylor TN, Lang D (1978) Dehydrated circular DNA: circular dichroism of molecules in ethanolic solutions. Biopolymers 17, 145-157. (Pubitemid 8275362)
    • (1978) Biopolymers , vol.17 , Issue.1 , pp. 145-157
    • Gray, D.M.1    Taylor, T.N.2    Lang, D.3
  • 45
    • 77958114712 scopus 로고    scopus 로고
    • Some current insights into oxidative stress
    • Duracková Z (2010) Some current insights into oxidative stress. Physiol Res 59, 459-469.
    • (2010) Physiol Res , vol.59 , pp. 459-469
    • Duracková, Z.1
  • 46
    • 0030597071 scopus 로고    scopus 로고
    • Glycoxidation and oxidative stress in Parkinson disease and diffuse Lewy body disease
    • DOI 10.1016/0006-8993(96)00729-9, PII S0006899396007299
    • Castellani R, Smith MA, Richey PL, Perry G (1996) Glycox-idation and oxidative stress in Parkinson disease and diffuse Lewy body disease. Brain Res 737, 195-200. (Pubitemid 26366614)
    • (1996) Brain Research , vol.737 , Issue.1-2 , pp. 195-200
    • Castellani, R.1    Smith, M.A.2    Richey, P.L.3    Perry, G.4
  • 47
    • 77957109627 scopus 로고    scopus 로고
    • N()-(carboxymethyl) lysinelinkageto α-synuclein and involvement of advanced glycation end prod-ucts in α-synuclein deposits in an MPTP-intoxicated mouse model
    • Choi YG, Lim S (2010)N()-(carboxymethyl)lysinelinkageto α-synuclein and involvement of advanced glycation end prod-ucts in α-synuclein deposits in an MPTP-intoxicated mouse model.Biochimie92, 1379-1386.
    • (2010) Biochimie , vol.92 , pp. 1379-1386
    • Choi, Y.G.1    Lim, S.2
  • 49
    • 0028075410 scopus 로고
    • Alterations in glutathione levels in Parkinson's disease and other neurodegenerative disorders affecting basal ganglia
    • Sian J, Dexter DT, Lees AJ, Daniel S, Agid Y, Javoy-Agid F, Jenner P, Marsden CD (1994) Alterations in glutathione levels in Parkinson's disease and other neurodegenerative disorders affecting basal ganglia. Ann Neurol 36, 348-355. (Pubitemid 24280055)
    • (1994) Annals of Neurology , vol.36 , Issue.3 , pp. 348-355
    • Sian, J.1    Dexter, D.T.2    Lees, A.J.3    Daniel, S.4    Agid, Y.5    Javoy-Agid, F.6    Jenner, P.7    Marsden, C.D.8
  • 50
    • 59349088294 scopus 로고    scopus 로고
    • The modifica-tion of alpha-synuclein by dicarbonyl compounds inhibits its fibril-formingprocess
    • Lee D, Park CW, Paik SR, Choi KY (2009) The modifica-tion of alpha-synuclein by dicarbonyl compounds inhibits its fibril-formingprocess. Biochim Biophys Acta 1794, 421-430.
    • (2009) Biochim Biophys Acta , vol.1794 , pp. 421-430
    • Lee, D.1    Park, C.W.2    Paik, S.R.3    Choi, K.Y.4
  • 51
    • 77949359499 scopus 로고    scopus 로고
    • Ribosylation rapidly induces alpha-synuclein to form highly cytotoxic molten globules of advanced glycation end products
    • Chen L, Wei Y, Wang X, He R (2010) Ribosylation rapidly induces alpha-synuclein to form highly cytotoxic molten globules of advanced glycation end products. PLoS One 5, e 9052.
    • (2010) PLoS One , vol.5 , pp. 9052
    • Chen, L.1    Wei, Y.2    Wang, X.3    He, R.4


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