Literature DB >> 19444607

Modulation of alpha-synuclein aggregation by dopamine: a review.

Su Ling Leong1, Roberto Cappai, Kevin Jeffrey Barnham, Chi Le Lan Pham.   

Abstract

Parkinson's disease (PD) is a progressive neurodegenerative disorder that is characterized by (1) the selective loss of dopaminergic neurons in the substantia nigra and (2) the deposition of misfolded alpha-synuclein (alpha-syn) as amyloid fibrils in the intracellular Lewy bodies in various region of the brain. Current thinking suggests that an interaction between alpha-syn and dopamine (DA) leads to the selective death of neuronal cells and the accumulation of misfolded alpha-syn. However, the exact mechanism by which this occurs is not fully defined. DA oxidation could play a key role is the pathogenesis of PD by causing oxidative stress, mitochondria dysfunction and impairment of protein metabolism. Here, we review the literature on the role of DA and its oxidative intermediates in modulating the aggregation pathways of alpha-syn.

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Year:  2009        PMID: 19444607     DOI: 10.1007/s11064-009-9986-8

Source DB:  PubMed          Journal:  Neurochem Res        ISSN: 0364-3190            Impact factor:   3.996


  79 in total

1.  Mice lacking alpha-synuclein display functional deficits in the nigrostriatal dopamine system.

Authors:  A Abeliovich; Y Schmitz; I Fariñas; D Choi-Lundberg; W H Ho; P E Castillo; N Shinsky; J M Verdugo; M Armanini; A Ryan; M Hynes; H Phillips; D Sulzer; A Rosenthal
Journal:  Neuron       Date:  2000-01       Impact factor: 17.173

2.  Dopamine affects the stability, hydration, and packing of protofibrils and fibrils of the wild type and variants of alpha-synuclein.

Authors:  Cristian Follmer; Luciana Romão; Carla M Einsiedler; Thaís C R Porto; Flávio Alves Lara; Marlos Moncores; Gilberto Weissmüller; Hilal A Lashuel; Peter Lansbury; Vivaldo Moura Neto; Jerson L Silva; Debora Foguel
Journal:  Biochemistry       Date:  2007-01-16       Impact factor: 3.162

Review 3.  The Lewy body in Parkinson's disease: molecules implicated in the formation and degradation of alpha-synuclein aggregates.

Authors:  Koichi Wakabayashi; Kunikazu Tanji; Fumiaki Mori; Hitoshi Takahashi
Journal:  Neuropathology       Date:  2007-10       Impact factor: 1.906

4.  Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins.

Authors:  M P Lambert; A K Barlow; B A Chromy; C Edwards; R Freed; M Liosatos; T E Morgan; I Rozovsky; B Trommer; K L Viola; P Wals; C Zhang; C E Finch; G A Krafft; W L Klein
Journal:  Proc Natl Acad Sci U S A       Date:  1998-05-26       Impact factor: 11.205

5.  Both familial Parkinson's disease mutations accelerate alpha-synuclein aggregation.

Authors:  L Narhi; S J Wood; S Steavenson; Y Jiang; G M Wu; D Anafi; S A Kaufman; F Martin; K Sitney; P Denis; J C Louis; J Wypych; A L Biere; M Citron
Journal:  J Biol Chem       Date:  1999-04-02       Impact factor: 5.157

6.  Metal-triggered structural transformations, aggregation, and fibrillation of human alpha-synuclein. A possible molecular NK between Parkinson's disease and heavy metal exposure.

Authors:  V N Uversky; J Li; A L Fink
Journal:  J Biol Chem       Date:  2001-09-11       Impact factor: 5.157

7.  Kinetic stabilization of the alpha-synuclein protofibril by a dopamine-alpha-synuclein adduct.

Authors:  K A Conway; J C Rochet; R M Bieganski; P T Lansbury
Journal:  Science       Date:  2001-11-09       Impact factor: 47.728

8.  Alpha-synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils.

Authors:  Hilal A Lashuel; Benjamin M Petre; Joseph Wall; Martha Simon; Richard J Nowak; Thomas Walz; Peter T Lansbury
Journal:  J Mol Biol       Date:  2002-10-04       Impact factor: 5.469

9.  Melanized dopaminergic neurons are differentially susceptible to degeneration in Parkinson's disease.

Authors:  E Hirsch; A M Graybiel; Y A Agid
Journal:  Nature       Date:  1988-07-28       Impact factor: 49.962

10.  Molecular cloning of cDNA encoding an unrecognized component of amyloid in Alzheimer disease.

Authors:  K Uéda; H Fukushima; E Masliah; Y Xia; A Iwai; M Yoshimoto; D A Otero; J Kondo; Y Ihara; T Saitoh
Journal:  Proc Natl Acad Sci U S A       Date:  1993-12-01       Impact factor: 11.205

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  38 in total

Review 1.  Tyrosine hydroxylase and regulation of dopamine synthesis.

Authors:  S Colette Daubner; Tiffany Le; Shanzhi Wang
Journal:  Arch Biochem Biophys       Date:  2010-12-19       Impact factor: 4.013

Review 2.  Phospholipase D: enzymology, functionality, and chemical modulation.

Authors:  Paige E Selvy; Robert R Lavieri; Craig W Lindsley; H Alex Brown
Journal:  Chem Rev       Date:  2011-09-22       Impact factor: 60.622

3.  Inflaming the diseased brain: a role for tainted melanins.

Authors:  T M Jeitner; M Kalogiannis; P A Patrick; I Gomolin; T Palaia; L Ragolia; D Brand; E J Delikatny
Journal:  Biochim Biophys Acta       Date:  2015-01-10

4.  Neuromelanin enhances the toxicity of α-synuclein in SK-N-SH cells.

Authors:  Jie Li; Junfeng Yang; Peng Zhao; Shen Li; Renyun Zhang; Xiaobin Zhang; Dan Liu; Benshu Zhang
Journal:  J Neural Transm (Vienna)       Date:  2011-12-27       Impact factor: 3.575

Review 5.  Complex molecular regulation of tyrosine hydroxylase.

Authors:  Izel Tekin; Robert Roskoski; Nurgul Carkaci-Salli; Kent E Vrana
Journal:  J Neural Transm (Vienna)       Date:  2014-05-28       Impact factor: 3.575

6.  3,4-Dihydroxyphenylacetaldehyde Is More Efficient than Dopamine in Oligomerizing and Quinonizing α-Synuclein.

Authors:  Yunden Jinsmaa; Risa Isonaka; Yehonatan Sharabi; David S Goldstein
Journal:  J Pharmacol Exp Ther       Date:  2019-11-19       Impact factor: 4.030

Review 7.  Phospholipase D in brain function and Alzheimer's disease.

Authors:  Tiago Gil Oliveira; Gilbert Di Paolo
Journal:  Biochim Biophys Acta       Date:  2010-04-23

Review 8.  The catecholaldehyde hypothesis: where MAO fits in.

Authors:  David S Goldstein
Journal:  J Neural Transm (Vienna)       Date:  2019-12-05       Impact factor: 3.575

9.  Methionine oxidation in α-synuclein inhibits its propensity for ordered secondary structure.

Authors:  Erika Ponzini; Antonella De Palma; Lucilla Cerboni; Antonino Natalello; Rossana Rossi; Rani Moons; Albert Konijnenberg; Joanna Narkiewicz; Giuseppe Legname; Frank Sobott; PierLuigi Mauri; Carlo Santambrogio; Rita Grandori
Journal:  J Biol Chem       Date:  2019-02-12       Impact factor: 5.157

10.  A spontaneous deletion of α-synuclein is associated with an increase in CB1 mRNA transcript and receptor expression in the hippocampus and amygdala: effects on alcohol consumption.

Authors:  Alejandro López-Jiménez; Nicole A R Walter; Elena Giné; Ángel Santos; Victor Echeverry-Alzate; Kora-Mareen Bühler; Pedro Olmos; Stéphanie Giezendanner; Rosario Moratalla; Lluis Montoliu; Kari J Buck; Jose Antonio López-Moreno
Journal:  Synapse       Date:  2013-03-20       Impact factor: 2.562

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