α-Synuclein aggregation and Parkinson's disease:: Factors affecting the aggregation of α-synuclein

被引:0
|
作者
Jin, L [1 ]
Yang, H [1 ]
机构
[1] Capital Univ Med Sci, Beijing Ctr Neural Regenerat & Repairing, Beijing Inst Neurosci, Beijing 100069, Peoples R China
关键词
alpha-synuclein; Parkinson's disease; Lewy bodies;
D O I
暂无
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Parkinson's disease (PD) is one of the most frequent neurodegenerative disorders. alpha-Synuclein was the first "PD gene" to be discovered. The involvement of a-synuclein in PD was first suspected after two different alpha-synuclein mutations were identified in two kindreds with autosomal-dominant PD. However,the discovery that alpha-synuclein is the major component of Lewy bodies-pathological hallmarks of PD, confirmed its role in PD pathogenesis. Pathological aggregation of alpha-synuclein might be responsible for neurodegeneration. Multiple factors have been shown to affect alpha-synuclein aggregation in vitro or in vivo. In addition, soluble oligomers of alpha-synuclein might be even more toxic than the insoluble fibrils found in degenerative diseases. So it is significant to investigate factors affecting a-synuclein aggregation, especially their accurate effects on the aggregation process.
引用
收藏
页码:321 / 328
页数:8
相关论文
共 32 条
  • [1] Toxicity of non-Aβ component of Alzheimer's disease amyloid, and N-terminal fragments thereof, correlates to formation of β-sheet structure and fibrils
    Bodles, AM
    Guthrie, DJS
    Harriott, P
    Campbell, P
    Irvine, GB
    [J]. EUROPEAN JOURNAL OF BIOCHEMISTRY, 2000, 267 (08): : 2186 - 2194
  • [2] Metal-catalyzed oxidation of α-synuclein -: Helping to define the relationship between oligomers, protofibrils, and filaments
    Cole, NB
    Murphy, DD
    Lebowitz, J
    Di Noto, L
    Levine, RL
    Nussbaum, RL
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2005, 280 (10) : 9678 - 9690
  • [3] 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
    Conway, KA
    Lee, SJ
    Rochet, JC
    Ding, TT
    Williamson, RE
    Lansbury, PT
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2000, 97 (02) : 571 - 576
  • [4] Kinetic stabilization of the α-synuclein protofibril by a dopamine-α-synuclein adduct
    Conway, KA
    Rochet, JC
    Bieganski, RM
    Lansbury, PT
    [J]. SCIENCE, 2001, 294 (5545) : 1346 - 1349
  • [5] Heat shock protein 70 inhibits α-synuclein fibril formation via preferential binding to prefibrillar species
    Dedmon, MM
    Christodoulou, J
    Wilson, MR
    Dobson, CM
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2005, 280 (15) : 14733 - 14740
  • [6] A peptide motif consisting of glycine, alanine, and valine is required for the fibrillization and cytotoxicity of human α-synuclein
    Du, HN
    Tang, L
    Luo, XY
    Li, HT
    Hu, J
    Zhou, JW
    Hu, HY
    [J]. BIOCHEMISTRY, 2003, 42 (29) : 8870 - 8878
  • [7] Synphilin-1 associates with α-synuclein and promotes the formation of cytosolic inclusions
    Engelender, S
    Kaminsky, Z
    Guo, X
    Sharp, AH
    Amaravi, RK
    Kleiderlein, JJ
    Margolis, RL
    Troncoso, JC
    Lanahan, AA
    Worley, PF
    Dawson, VL
    Dawson, TM
    Ross, CA
    [J]. NATURE GENETICS, 1999, 22 (01) : 110 - 114
  • [8] A hydrophobic stretch of 12 amino acid residues in the middle of α-synuclein is essential for filament assembly
    Giasson, BI
    Murray, IVJ
    Trojanowski, JQ
    Lee, VMY
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (04) : 2380 - 2386
  • [9] Magnesium inhibits spontaneous and iron-induced aggregation of α-synuclein
    Golts, N
    Snyder, H
    Frasier, M
    Theisler, C
    Choi, P
    Wolozin, B
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (18) : 16116 - 16123
  • [10] Role of cytochrome c as a stimulator of α-synuclein aggregation in Lewy body disease
    Hashimoto, M
    Takeda, A
    Hsu, LJ
    Takenouchi, T
    Masliah, E
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (41) : 28849 - 28852