Literature DB >> 15655259

The Role of alpha-synuclein assembly and metabolism in the pathogenesis of Lewy body disease.

Makoto Hashimoto1, Kohichi Kawahara, Pazit Bar-On, Edward Rockenstein, Leslie Crews, Eliezer Masliah.   

Abstract

Parkinson's disease (PD) and dementia with Lewy bodies (DLB) are members of a family of disorders characterized by the presence of inclusion bodies, or Lewy bodies (LBs), filled with aggregates of alpha-synuclein. These diseases are a leading cause of movement disorders and dementia in the aging population, and it is crucial to understand the factors leading to the accumulation and assembly of these alpha-synuclein aggregates. Previous studies have uncovered much about the factors leading to aggregation and the mechanisms causing neurotoxicity of these inclusion bodies; however, little is known about factors that promote the degradation and prevent the aggregation of alpha-synuclein. The present article provides a review of recent efforts in the investigation of factors involved in alpha-synuclein metabolism and the mechanisms involved in preventing accumulation of alpha-synuclein and degrading this molecule. Understanding these processes might provide targets for the development of novel therapies for disorders such as DLB and PD.

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Year:  2004        PMID: 15655259     DOI: 10.1385/JMN:24:3:343

Source DB:  PubMed          Journal:  J Mol Neurosci        ISSN: 0895-8696            Impact factor:   3.444


  81 in total

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Review 2.  Ubiquitination and abnormal phosphorylation of paired helical filaments in Alzheimer's disease.

Authors:  K Iqbal; I Grundke-Iqbal
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3.  Specific increase in amyloid beta-protein 42 secretion ratio by calpain inhibition.

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Journal:  Biochemistry       Date:  1997-07-08       Impact factor: 3.162

4.  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

5.  Parkin ubiquitinates the alpha-synuclein-interacting protein, synphilin-1: implications for Lewy-body formation in Parkinson disease.

Authors:  K K Chung; Y Zhang; K L Lim; Y Tanaka; H Huang; J Gao; C A Ross; V L Dawson; T M Dawson
Journal:  Nat Med       Date:  2001-10       Impact factor: 53.440

6.  Enhanced vulnerability to oxidative stress by alpha-synuclein mutations and C-terminal truncation.

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Review 7.  Mitochondria and degenerative disorders.

Authors:  M Orth; A H Schapira
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8.  Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase.

Authors:  H Shimura; N Hattori; S i Kubo; Y Mizuno; S Asakawa; S Minoshima; N Shimizu; K Iwai; T Chiba; K Tanaka; T Suzuki
Journal:  Nat Genet       Date:  2000-07       Impact factor: 38.330

9.  Rat alpha-synuclein interacts with Tat binding protein 1, a component of the 26S proteasomal complex.

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Journal:  J Neurochem       Date:  2000-11       Impact factor: 5.372

10.  Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1.

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  22 in total

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Review 3.  The many faces of α-synuclein: from structure and toxicity to therapeutic target.

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Journal:  Nat Rev Neurosci       Date:  2013-01       Impact factor: 34.870

4.  Posttranslational modifications, localization, and protein interactions of optineurin, the product of a glaucoma gene.

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5.  Oral Administration of Silibinin Ameliorates Cognitive Deficits of Parkinson's Disease Mouse Model by Restoring Mitochondrial Disorders in Hippocampus.

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6.  Epigallocatechin Gallate (EGCG) Inhibits Alpha-Synuclein Aggregation: A Potential Agent for Parkinson's Disease.

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7.  An scFv intrabody against the nonamyloid component of alpha-synuclein reduces intracellular aggregation and toxicity.

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Journal:  J Mol Biol       Date:  2007-12-05       Impact factor: 5.469

8.  Transglutaminase-mediated intramolecular cross-linking of membrane-bound alpha-synuclein promotes amyloid formation in Lewy bodies.

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9.  Alpha-synuclein alters Notch-1 expression and neurogenesis in mouse embryonic stem cells and in the hippocampus of transgenic mice.

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Review 10.  Trends in the molecular pathogenesis and clinical therapeutics of common neurodegenerative disorders.

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Journal:  Int J Mol Sci       Date:  2009-06-03       Impact factor: 6.208

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