메뉴 건너뛰기




Volumn 23, Issue 4-5, 2002, Pages 527-536

Synergistic effects of pesticides and metals on the fibrillation of α-synuclein: Implications for Parkinson's disease

Author keywords

Synuclein; Aggregation; Fibrils; Metals; Pesticides

Indexed keywords

ALPHA SYNUCLEIN; METAL; PESTICIDE; ALUMINUM CHLORIDE; ALUMINUM DERIVATIVE; CHLORIDE; NERVE PROTEIN; SNCA PROTEIN, HUMAN; SYNUCLEIN;

EID: 0036777847     PISSN: 0161813X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0161-813X(02)00067-0     Document Type: Conference Paper
Times cited : (178)

References (39)
  • 1
    • 0033153770 scopus 로고    scopus 로고
    • Aluminum-containing antacids as a cause of idiopathic Parkinson's disease
    • Altschuler E. Aluminum-containing antacids as a cause of idiopathic Parkinson's disease. Med Hypotheses 1999;53:22-3.
    • (1999) Med Hypotheses , vol.53 , pp. 22-23
    • Altschuler, E.1
  • 2
    • 0031787871 scopus 로고    scopus 로고
    • Accelerated in vitro fibril formation by a mutant α-synuclein linked to early-onset Parkinson disease
    • Conway KA, Harper JD, Lansbury PT. Accelerated in vitro fibril formation by a mutant α-synuclein linked to early-onset Parkinson disease. Nat Med 1998;4:1318-20.
    • (1998) Nat Med , vol.4 , pp. 1318-1320
    • Conway, K.A.1    Harper, J.D.2    Lansbury, P.T.3
  • 3
    • 0034681163 scopus 로고    scopus 로고
    • Acceleration of oligomerization, not fibrillization, is a shared property of both α-synuclein mutations linked to early-onset Parkinson's disease: Implications for pathogenesis and therapy
    • in process citation
    • Conway KA, Lee SJ, Rochet JC, Ding TT, Williamson RE, Lansbury Jr, PT. Acceleration of oligomerization, not fibrillization, is a shared property of both α-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy. Proc Natl Acad Sci USA 2000;97:571-6[in process citation].
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 571-576
    • Conway, K.A.1    Lee, S.J.2    Rochet, J.C.3    Ding, T.T.4    Williamson, R.E.5    Lansbury P.T., Jr.6
  • 4
    • 0031728689 scopus 로고    scopus 로고
    • Synthetic filaments assembled from C-terminally truncated α-synuclein
    • Crowther RA, Jakes R, Spillantini MG, Goedert M. Synthetic filaments assembled from C-terminally truncated α-synuclein. FEBS Lett 1998;436:309-12.
    • (1998) FEBS Lett , vol.436 , pp. 309-312
    • Crowther, R.A.1    Jakes, R.2    Spillantini, M.G.3    Goedert, M.4
  • 5
    • 0032573289 scopus 로고    scopus 로고
    • 53) to Thr on the physical and morphological properties of α-synuclein protein implicated in Parkinson's disease
    • 53) to Thr on the physical and morphological properties of α-synuclein protein implicated in Parkinson's disease. FEBS Lett 1998;440:67-70.
    • (1998) FEBS Lett , vol.440 , pp. 67-70
    • El-Agnaf, O.M.A.1    Jakes, R.2    Curran, M.D.3    Wallace, A.4
  • 6
    • 0035815115 scopus 로고    scopus 로고
    • Conformational properties of α-synuclein in its free and lipid-associated states
    • Eliezer D, Kutluay E, Bussell Jr, R, Browne G. Conformational properties of α-synuclein in its free and lipid-associated states. J Mol Biol 2001;307:1061-73.
    • (2001) J Mol Biol , vol.307 , pp. 1061-1073
    • Eliezer, D.1    Kutluay, E.2    Bussell R., Jr.3    Browne, G.4
  • 7
    • 0027995384 scopus 로고
    • Classification of acid denaturation of proteins - Intermediates and unfolded states
    • Fink AL, Calciano LJ, Goto Y, Kurotsu T, Palleros DR. Classification of acid denaturation of proteins - intermediates and unfolded states. Biochemistry 1994;33:12504-11.
    • (1994) Biochemistry , vol.33 , pp. 12504-12511
    • Fink, A.L.1    Calciano, L.J.2    Goto, Y.3    Kurotsu, T.4    Palleros, D.R.5
  • 8
    • 0031933289 scopus 로고    scopus 로고
    • Discrete intermediates versus molten globule models for protein folding: Characterization of partially folded intermediates of apomyoglobin
    • Fink AL, Oberg KA, Seshadri S. Discrete intermediates versus molten globule models for protein folding: characterization of partially folded intermediates of apomyoglobin. Fold Des 1998;3:19-25.
    • (1998) Fold Des , vol.3 , pp. 19-25
    • Fink, A.L.1    Oberg, K.A.2    Seshadri, S.3
  • 9
    • 0035031135 scopus 로고    scopus 로고
    • Parkinson's disease and other α-synucleinopathies
    • Goedert M. Parkinson's disease and other α-synucleinopathies. Clin Chem Lab Med 2001;39:308-12.
    • (2001) Clin Chem Lab Med , vol.39 , pp. 308-312
    • Goedert, M.1
  • 10
    • 0026746512 scopus 로고
    • Neuromelanin-containing neurons of the substantia nigra accumulate iron and aluminum in Parkinson's disease: A LAMMA study
    • Good PF, Olanow CW, Perl DP. Neuromelanin-containing neurons of the substantia nigra accumulate iron and aluminum in Parkinson's disease: a LAMMA study. Brain Res 1992;593:343-6.
    • (1992) Brain Res , vol.593 , pp. 343-346
    • Good, P.F.1    Olanow, C.W.2    Perl, D.P.3
  • 13
    • 0025195499 scopus 로고
    • Mechanism of acid-induced folding of proteins
    • Goto Y, Takahashi N, Fink AL. Mechanism of acid-induced folding of proteins. Biochemistry 1990b;29:3480-8.
    • (1990) Biochemistry , vol.29 , pp. 3480-3488
    • Goto, Y.1    Takahashi, N.2    Fink, A.L.3
  • 14
    • 0032551656 scopus 로고    scopus 로고
    • Human recombinant NACP/α-synuclein is aggregated and fibrillated in vitro: Relevance for Lewy body disease
    • Hashimoto M, Hsu LJ, Sisk A, Xia Y, Takeda A, Sundsmo M, Masliah E. Human recombinant NACP/α-synuclein is aggregated and fibrillated in vitro: Relevance for Lewy body disease. Brain Res 1998;799:301-6.
    • (1998) Brain Res , vol.799 , pp. 301-306
    • Hashimoto, M.1    Hsu, L.J.2    Sisk, A.3    Xia, Y.4    Takeda, A.5    Sundsmo, M.6    Masliah, E.7
  • 15
    • 0033577159 scopus 로고    scopus 로고
    • Oxidative stress induces amyloid-like aggregate formation of NACP/α-synuclein in vitro
    • Hashimoto M, Hsu LJ, Xia Y, Takeda A, Sisk A, Sundsmo M, Masliah E. Oxidative stress induces amyloid-like aggregate formation of NACP/α-synuclein in vitro. Neuroreport 1999;10:717-21.
    • (1999) Neuroreport , vol.10 , pp. 717-721
    • Hashimoto, M.1    Hsu, L.J.2    Xia, Y.3    Takeda, A.4    Sisk, A.5    Sundsmo, M.6    Masliah, E.7
  • 16
    • 0035950270 scopus 로고    scopus 로고
    • β-synuclein inhibits α-synuclein aggregation. A possible role as an anti-Parkinsonian factor
    • Hashimoto M, Rockenstein E, Mante M, Mallory M, Masliah E. β-Synuclein inhibits α-synuclein aggregation. A possible role as an anti-Parkinsonian factor. Neuron 2001;32:213-23.
    • (2001) Neuron , vol.32 , pp. 213-223
    • Hashimoto, M.1    Rockenstein, E.2    Mante, M.3    Mallory, M.4    Masliah, E.5
  • 17
    • 9544227379 scopus 로고    scopus 로고
    • Diet and Parkinson's disease. II. A possible role for the past intake of specific nutrients. Results from a self-administered foodfrequency questionnaire in a case-control study
    • see comments
    • Hellenbrand W, Boeing H, Robra BP, Seidler A, Vieregge P, Nischan P, Joerg J, Oertel WH, Schneider E, Ulm G. Diet and Parkinson's disease. II. A possible role for the past intake of specific nutrients. Results from a self-administered foodfrequency questionnaire in a case-control study. Neurology 1996;47:644-50[see comments].
    • (1996) Neurology , vol.47 , pp. 644-650
    • Hellenbrand, W.1    Boeing, H.2    Robra, B.P.3    Seidler, A.4    Vieregge, P.5    Nischan, P.6    Joerg, J.7    Oertel, W.H.8    Schneider, E.9    Ulm, G.10
  • 18
    • 0027952847 scopus 로고
    • A case-control study of Parkinson's disease in a horticultural region of British Columbia
    • Hertzman C, Wiens M, Snow B, Kelly S, Calne D. A case-control study of Parkinson's disease in a horticultural region of British Columbia. Mov Disord 1994;9:69-75.
    • (1994) Mov Disord , vol.9 , pp. 69-75
    • Hertzman, C.1    Wiens, M.2    Snow, B.3    Kelly, S.4    Calne, D.5
  • 19
    • 0026034279 scopus 로고
    • Iron and aluminum increase in the substantia nigra of patients with Parkinson's disease: An X-ray microanalysis
    • Hirsch EC, Brandel JP, Galle P, Javoy-Agid F, Agid Y. Iron and aluminum increase in the substantia nigra of patients with Parkinson's disease: an X-ray microanalysis. J Neurochem 1991;56:446-51.
    • (1991) J Neurochem , vol.56 , pp. 446-451
    • Hirsch, E.C.1    Brandel, J.P.2    Galle, P.3    Javoy-Agid, F.4    Agid, Y.5
  • 22
    • 0035949542 scopus 로고    scopus 로고
    • Effect of familial Parkinson's disease point mutations A30P and A53T on the structural properties, aggregation, and fibrillation of human α-synuclein
    • Li J, Uversky VN, Fink AL. Effect of familial Parkinson's disease point mutations A30P and A53T on the structural properties, aggregation, and fibrillation of human α-synuclein. Biochemistry 2001;40:11604-13.
    • (2001) Biochemistry , vol.40 , pp. 11604-11613
    • Li, J.1    Uversky, V.N.2    Fink, A.L.3
  • 23
    • 0037127197 scopus 로고    scopus 로고
    • The herbicide paraquat causes up-regulation and aggregation of α-synuclein in mice. Paraquat and α-synuclein
    • Manning-Bog AB, McCormack AL, Li J, Uversky VN, Fink AL, Di Monte DA. The herbicide paraquat causes up-regulation and aggregation of α-synuclein in mice. Paraquat and α-synuclein. J Biol Chem 2002a;277:1641-4.
    • (2002) J Biol Chem , vol.277 , pp. 1641-1644
    • Manning-Bog, A.B.1    McCormack, A.L.2    Li, J.3    Uversky, V.N.4    Fink, A.L.5    Di Monte, D.A.6
  • 24
    • 0037127197 scopus 로고    scopus 로고
    • The herbicide paraquat causes up-regulation and aggregation of α-synuclein in mice. Paraquat and α-synuclein
    • Manning-Bog AB, McCormack AL, Li J, Uversky VN, Fink AL, Di Monte DA. The herbicide paraquat causes up-regulation and aggregation of α-synuclein in mice. Paraquat and α-synuclein. J Biol Chem 2002b;277:1641-4.
    • (2002) J Biol Chem , vol.277 , pp. 1641-1644
    • Manning-Bog, A.B.1    McCormack, A.L.2    Li, J.3    Uversky, V.N.4    Fink, A.L.5    Di Monte, D.A.6
  • 26
    • 0025440053 scopus 로고
    • Fluorometric examination of tissue amyloid fibrils in murine senile amyloidosis: Use of the fluorescent indicator, thioflavine T
    • Naiki H, Higuchi K, Matsushima K, Shimada A, Chen WH, Hosokawa M, Takeda T. Fluorometric examination of tissue amyloid fibrils in murine senile amyloidosis: use of the fluorescent indicator, thioflavine T. Lab Invest 1990;62:768-73.
    • (1990) Lab Invest , vol.62 , pp. 768-773
    • Naiki, H.1    Higuchi, K.2    Matsushima, K.3    Shimada, A.4    Chen, W.H.5    Hosokawa, M.6    Takeda, T.7
  • 28
    • 0028286474 scopus 로고
    • Protein conformational changes induced by 1,1′-bis(4-anilino-5-naphthalenesulfonic acid) - Preferential binding to the molten globule of dnak
    • Shi L, Palleros DR, Fink AL. Protein conformational changes induced by 1,1′-bis(4-anilino-5-naphthalenesulfonic acid) - preferential binding to the molten globule of dnak. Biochemistry 1994;33:7536-46.
    • (1994) Biochemistry , vol.33 , pp. 7536-7546
    • Shi, L.1    Palleros, D.R.2    Fink, A.L.3
  • 29
    • 0032568534 scopus 로고    scopus 로고
    • α-synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with Lewy bodies
    • Spillantini MG, Crowther RA, Jakes R, Hasegawa M, Goedert M. α-Synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with Lewy bodies. Proc Natl Acad Sci USA 1998;95:6469-73.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 6469-6473
    • Spillantini, M.G.1    Crowther, R.A.2    Jakes, R.3    Hasegawa, M.4    Goedert, M.5
  • 30
    • 0024546234 scopus 로고
    • The role of environmental toxins in the etiology of Parkinson's disease
    • Tanner CM. The role of environmental toxins in the etiology of Parkinson's disease. Trends Neurosci 1989;12:49-54.
    • (1989) Trends Neurosci , vol.12 , pp. 49-54
    • Tanner, C.M.1
  • 32
    • 0032525256 scopus 로고    scopus 로고
    • Anion-induced folding of staphylococcal nuclease: Characterization of multiple equilibrium partially folded intermediates
    • Uversky VN, Karnoup AS, Segel DJ, Seshadri S, Doniach S, Fink AL. Anion-induced folding of staphylococcal nuclease: characterization of multiple equilibrium partially folded intermediates. J Mol Biol 1998;278:879-94.
    • (1998) J Mol Biol , vol.278 , pp. 879-894
    • Uversky, V.N.1    Karnoup, A.S.2    Segel, D.J.3    Seshadri, S.4    Doniach, S.5    Fink, A.L.6
  • 33
    • 0034669882 scopus 로고    scopus 로고
    • Why are "natively unfolded" proteins unstructured under physiologic conditions?
    • Uversky VN, Gillespie JR, Fink AL. Why are "natively unfolded" proteins unstructured under physiologic conditions? Proteins 2000;41:415-27.
    • (2000) Proteins , vol.41 , pp. 415-427
    • Uversky, V.N.1    Gillespie, J.R.2    Fink, A.L.3
  • 34
    • 0035941305 scopus 로고    scopus 로고
    • Stabilization of partially folded conformation during α-synuclein oligomerization in both purified and cytosolic preparations
    • Uversky VN, Lee HJ, Li J, Fink AL, Lee SJ. Stabilization of partially folded conformation during α-synuclein oligomerization in both purified and cytosolic preparations. J Biol Chem 2001a;276:43495-8.
    • (2001) J Biol Chem , vol.276 , pp. 43495-43498
    • Uversky, V.N.1    Lee, H.J.2    Li, J.3    Fink, A.L.4    Lee, S.J.5
  • 35
    • 0035815664 scopus 로고    scopus 로고
    • Evidence for a partially folded intermediate in α-synuclein fibril formation
    • Uversky VN, Li J, Fink AL. Evidence for a partially folded intermediate in α-synuclein fibril formation. J Biol Chem 2001b;276:10737-44.
    • (2001) J Biol Chem , vol.276 , pp. 10737-10744
    • Uversky, V.N.1    Li, J.2    Fink, A.L.3
  • 36
    • 0035941201 scopus 로고    scopus 로고
    • Metal-triggered structural transformations, aggregation, and fibrillation of human α-synuclein. A possible molecular link between Parkinson's disease and heavy metal exposure
    • Uversky VN, Li J, Fink AL. Metal-triggered structural transformations, aggregation, and fibrillation of human α-synuclein. A possible molecular link between Parkinson's disease and heavy metal exposure. J Biol Chem 2001c;276:44284-96.
    • (2001) J Biol Chem , vol.276 , pp. 44284-44296
    • Uversky, V.N.1    Li, J.2    Fink, A.L.3
  • 37
    • 0035816404 scopus 로고    scopus 로고
    • Pesticides directly accelerate the rate of α-synuclein fibril formation: A possible factor in Parkinson's disease
    • Uversky VN, Li J, Fink AL. Pesticides directly accelerate the rate of α-synuclein fibril formation: a possible factor in Parkinson's disease. FEBS Lett 2001d;500:105-8.
    • (2001) FEBS Lett , vol.500 , pp. 105-108
    • Uversky, V.N.1    Li, J.2    Fink, A.L.3
  • 38
    • 0029904487 scopus 로고    scopus 로고
    • NACP a protein implicated in Alzheimer's disease and learning, is natively unfolded
    • Weinreb PH, Zhen WG, Poon AW, Conway KA, Lansbury Jr, PT. NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded. Biochemistry 1996;35:13709-15.
    • (1996) Biochemistry , vol.35 , pp. 13709-13715
    • Weinreb, P.H.1    Zhen, W.G.2    Poon, A.W.3    Conway, K.A.4    Lansbury P.T., Jr.5
  • 39
    • 0026454505 scopus 로고
    • Calcium, magnesium and aluminum concentrations in Parkinson's disease
    • Yasui M, Kihira T, Ota K. Calcium, magnesium and aluminum concentrations in Parkinson's disease. Neurotoxicology 1992;13:593-600.
    • (1992) Neurotoxicology , vol.13 , pp. 593-600
    • Yasui, M.1    Kihira, T.2    Ota, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.