Home LiteratureArticle Details
PMID: 19628769 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Research Support, N.I.H., Intramural Research Support, Non-U.S. Gov't

Metabolic activity determines efficacy of macroautophagic clearance of pathological oligomeric alpha-synuclein.

The American journal of pathology ·Vol. 175 ·No. 2 ·2009-08-00 ·Pages 736-47

Yu WH, Dorado B, Figueroa HY, Wang L, Planel E, Cookson MR, Clark LN, Duff KE

Abstract

Macroautophagy is an essential degradative pathway that can be induced to clear aggregated proteins, such as those found in Parkinson's disease and dementia with Lewy bodies, a form of Parkinsonism. This study found that both LC3-II and beclin were significantly increased in brains from humans with Dementia with Lewy bodies and transgenic mice overexpressing mutant alpha-synuclein, as compared with respective controls, suggesting that macroautophagy is induced to remove alpha-syn, particularly oligomeric or mutant forms. Aged mutant animals had higher autophagy biomarker levels relative to younger animals, suggesting that with aging, autophagy is less efficient and requires more stimulation to achieve the same outcome. Disruption of autophagy by RNA interference significantly increased alpha-syn oligomer accumulation in vitro, confirming the significance of autophagy in alpha-syn clearance. Finally, rotenone-induced alpha-syn aggregates were cleared following rapamycin stimulation of autophagy. Chronic rotenone exposure and commensurate reduction of metabolic activity limited the efficacy of rapamycin to promote autophagy, suggesting that cellular metabolism is critical for determining autophagic activity. Cumulatively, these findings support the concept that neuronal autophagy is essential for protein homeostasis and, in our system, reduction of autophagy increased the accumulation of potentially pathogenic alpha-synuclein oligomers. Aging and metabolic state were identified as important determinants of autophagic activity. This study provides therapeutic and pathological implications for both synucleinopathy and Parkinson's disease, identifying conditions in which autophagy may be insufficient to degrade alpha-syn aggregates.

MeSH Terms
Aged Aged, 80 and over Aging/metabolism,pathology Animals Autophagy/genetics Brain/metabolism,pathology Female Humans Male Mice Mice, Transgenic Parkinson Disease/metabolism,pathology alpha-Synuclein/genetics,metabolism
Chemicals
alpha-Synuclein
Authors & Affiliations
8 authors, click to expand affiliations / ORCID
Yu Wai Haung
Dept of Pathology, Columbia University Medical Center, 630 W168th St Rm 12-461, New York NY 10032, USA.
Dorado Beatriz
Figueroa Helen Yvette
Wang Lili
Planel Emmanuel
Cookson Mark R
Clark Lorraine N
Duff Karen E
References (71)
71 references, click to expand
  1. Autophagy genes are essential for dauer development and life-span extension in C. elegans.
    Science. 2003 Sep 5;301(5638):1387-91 PMID: 12958363
  2. DJ-1( PARK7), a novel gene for autosomal recessive, early onset parkinsonism.
    Neurol Sci. 2003 Oct;24(3):159-60 PMID: 14598065
  3. The alpha-synucleinopathies: Parkinson's disease, dementia with Lewy bodies, and multiple system atrophy.
    Ann N Y Acad Sci. 2000;920:16-27 PMID: 11193145
  4. Energy dependence of different steps in the autophagic-lysosomal pathway.
    J Biol Chem. 1989 Apr 25;264(12):6699-704 PMID: 2708336
  5. The formation of highly soluble oligomers of alpha-synuclein is regulated by fatty acids and enhanced in Parkinson's disease.
    Neuron. 2003 Feb 20;37(4):583-95 PMID: 12597857
  6. A cycling protein complex required for selective autophagy.
    Autophagy. 2007 Sep-Oct;3(5):422-32 PMID: 17426440
  7. Lack of nigral pathology in transgenic mice expressing human alpha-synuclein driven by the tyrosine hydroxylase promoter.
    Neurobiol Dis. 2001 Jun;8(3):535-9 PMID: 11442360
  8. Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy.
    Science. 2004 Aug 27;305(5688):1292-5 PMID: 15333840
  9. Mutation in the alpha-synuclein gene identified in families with Parkinson's disease.
    Science. 1997 Jun 27;276(5321):2045-7 PMID: 9197268
  10. Aging and dietary restriction effects on ubiquitination, sumoylation, and the proteasome in the heart.
    Mech Ageing Dev. 2008 Sep;129(9):515-21 PMID: 18533226
  11. Dynamics of alpha-synuclein aggregation and inhibition of pore-like oligomer development by beta-synuclein.
    FEBS J. 2007 Apr;274(7):1862-77 PMID: 17381514
  12. alpha-Synuclein locus triplication causes Parkinson's disease.
    Science. 2003 Oct 31;302(5646):841 PMID: 14593171
  13. Autophagy-mediated clearance of aggresomes is not a universal phenomenon.
    Hum Mol Genet. 2008 Aug 15;17(16):2570-82 PMID: 18502787
  14. Neuronal macroautophagy: from development to degeneration.
    Mol Aspects Med. 2006 Oct-Dec;27(5-6):503-19 PMID: 16999991
  15. Autophagy induction and autophagosome clearance in neurons: relationship to autophagic pathology in Alzheimer's disease.
    J Neurosci. 2008 Jul 2;28(27):6926-37 PMID: 18596167
  16. NACP, a presynaptic protein, immunoreactivity in Lewy bodies in Parkinson's disease.
    Neurosci Lett. 1997 Dec 12;239(1):45-8 PMID: 9547168
  17. Autophagy and aging: the importance of maintaining "clean" cells.
    Autophagy. 2005 Oct-Dec;1(3):131-40 PMID: 16874025
  18. Formation of toxic oligomeric alpha-synuclein species in living cells.
    PLoS One. 2008 Apr 02;3(4):e1867 PMID: 18382657
  19. Functional specificity of the mammalian Beclin-Vps34 PI 3-kinase complex in macroautophagy versus endocytosis and lysosomal enzyme trafficking.
    J Cell Sci. 2006 Jan 15;119(Pt 2):259-70 PMID: 16390869
  20. Extensive involvement of autophagy in Alzheimer disease: an immuno-electron microscopy study.
    J Neuropathol Exp Neurol. 2005 Feb;64(2):113-22 PMID: 15751225
  21. Isolation of autophagic vacuoles from rat liver: morphological and biochemical characterization.
    J Cell Biol. 1982 Apr;93(1):144-54 PMID: 7068752
  22. Lewy body diseases and multiple system atrophy as alpha-synucleinopathies.
    Mol Psychiatry. 1998 Nov;3(6):462-5 PMID: 9857966
  23. Chaperone-mediated autophagy in aging and disease.
    Curr Top Dev Biol. 2006;73:205-35 PMID: 16782460
  24. Aggregate-prone proteins are cleared from the cytosol by autophagy: therapeutic implications.
    Curr Top Dev Biol. 2006;76:89-101 PMID: 17118264
  25. Ca2+ binding to alpha-synuclein regulates ligand binding and oligomerization.
    J Biol Chem. 2001 Jun 22;276(25):22680-4 PMID: 11312271
  26. When lysosomes get old.
    Exp Gerontol. 2000 Mar;35(2):119-31 PMID: 10767573
  27. Cloning of the gene containing mutations that cause PARK8-linked Parkinson's disease.
    Neuron. 2004 Nov 18;44(4):595-600 PMID: 15541308
  28. Oncoprotein Akt/PKB induces trophic effects in murine models of Parkinson's disease.
    Proc Natl Acad Sci U S A. 2006 Dec 5;103(49):18757-62 PMID: 17116866
  29. Intron-exon structure of ubiquitin c-terminal hydrolase-L1.
    DNA Res. 1998 Dec 31;5(6):397-400 PMID: 10048490
  30. Hereditary parkinsonism with dementia is caused by mutations in ATP13A2, encoding a lysosomal type 5 P-type ATPase.
    Nat Genet. 2006 Oct;38(10):1184-91 PMID: 16964263
  31. Role of protein aggregation in mitochondrial dysfunction and neurodegeneration in Alzheimer's and Parkinson's diseases.
    Neuromolecular Med. 2003;4(1-2):21-36 PMID: 14528050
  32. Mutations in the glucocerebrosidase gene are associated with early-onset Parkinson disease.
    Neurology. 2007 Sep 18;69(12):1270-7 PMID: 17875915
  33. A protein conjugation system essential for autophagy.
    Nature. 1998 Sep 24;395(6700):395-8 PMID: 9759731
  34. LRRK2 mutations in Parkinson disease.
    Neurology. 2005 Sep 13;65(5):738-40 PMID: 16157908
  35. Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders.
    Annu Rev Neurosci. 2003;26:267-98 PMID: 12704221
  36. Loss of autophagy in the central nervous system causes neurodegeneration in mice.
    Nature. 2006 Jun 15;441(7095):880-4 PMID: 16625205
  37. Macroautophagy--a novel Beta-amyloid peptide-generating pathway activated in Alzheimer's disease.
    J Cell Biol. 2005 Oct 10;171(1):87-98 PMID: 16203860
  38. Role of autophagy in G2019S-LRRK2-associated neurite shortening in differentiated SH-SY5Y cells.
    J Neurochem. 2008 May;105(3):1048-56 PMID: 18182054
  39. Polycation-induced oligomerization and accelerated fibrillation of human alpha-synuclein in vitro.
    Protein Sci. 2003 Apr;12(4):702-7 PMID: 12649428
  40. Guidelines for the use and interpretation of assays for monitoring autophagy in higher eukaryotes.
    Autophagy. 2008 Feb;4(2):151-75 PMID: 18188003
  41. Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice.
    Nature. 2006 Jun 15;441(7095):885-9 PMID: 16625204
  42. Protein degradation and aging.
    Exp Gerontol. 2005 Aug-Sep;40(8-9):622-33 PMID: 16125351
  43. Mechanisms of hybrid oligomer formation in the pathogenesis of combined Alzheimer's and Parkinson's diseases.
    PLoS One. 2008 Sep 04;3(9):e3135 PMID: 18769546
  44. Selective degradation of annexins by chaperone-mediated autophagy.
    J Biol Chem. 2000 Oct 27;275(43):33329-35 PMID: 10938088
  45. Mutations in the glucocerebrosidase gene and Parkinson disease: phenotype-genotype correlation.
    Neurology. 2005 Nov 8;65(9):1460-1 PMID: 16148263
  46. Is there a cause-and-effect relationship between alpha-synuclein fibrillization and Parkinson's disease?
    Nat Cell Biol. 2000 Jul;2(7):E115-9 PMID: 10878819
  47. Glucocerebrosidase gene mutations: a risk factor for Lewy body disorders.
    Arch Neurol. 2008 Mar;65(3):379-82 PMID: 18332251
  48. alpha-Synuclein membrane interactions and lipid specificity.
    J Biol Chem. 2000 Nov 3;275(44):34328-34 PMID: 10915790
  49. How do intracellular proteolytic systems change with age?
    Front Biosci. 1998 Jan 01;3:d25-43 PMID: 9407152
  50. Autophagy and its possible roles in nervous system diseases, damage and repair.
    Autophagy. 2005 Apr;1(1):11-22 PMID: 16874045
  51. Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism.
    Nature. 1998 Apr 9;392(6676):605-8 PMID: 9560156
  52. Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy.
    Proc Natl Acad Sci U S A. 2000 Jan 18;97(2):571-6 PMID: 10639120
  53. Aggregate-prone proteins with polyglutamine and polyalanine expansions are degraded by autophagy.
    Hum Mol Genet. 2002 May 1;11(9):1107-17 PMID: 11978769
  54. Similar patterns of mitochondrial vulnerability and rescue induced by genetic modification of alpha-synuclein, parkin, and DJ-1 in Caenorhabditis elegans.
    J Biol Chem. 2005 Dec 30;280(52):42655-42668 PMID: 16239214
  55. Pesticides directly accelerate the rate of alpha-synuclein fibril formation: a possible factor in Parkinson's disease.
    FEBS Lett. 2001 Jul 6;500(3):105-8 PMID: 11445065
  56. Impairment of the ubiquitin-proteasome system causes dopaminergic cell death and inclusion body formation in ventral mesencephalic cultures.
    J Neurochem. 2002 Apr;81(2):301-6 PMID: 12064477
  57. Clearance of alpha-synuclein oligomeric intermediates via the lysosomal degradation pathway.
    J Neurosci. 2004 Feb 25;24(8):1888-96 PMID: 14985429
  58. Clearance of mutant aggregate-prone proteins by autophagy.
    Methods Mol Biol. 2008;445:195-211 PMID: 18425452
  59. Hereditary early-onset Parkinson's disease caused by mutations in PINK1.
    Science. 2004 May 21;304(5674):1158-60 PMID: 15087508
  60. Parkinsonism genes: culprits and clues.
    J Neurochem. 2006 Nov;99(4):1062-72 PMID: 16836655
  61. The TOR signaling cascade regulates gene expression in response to nutrients.
    Genes Dev. 1999 Dec 15;13(24):3271-9 PMID: 10617575
  62. Association of glucocerebrosidase mutations with dementia with lewy bodies.
    Arch Neurol. 2009 May;66(5):578-83 PMID: 19433657
  63. Autophagy-mediated clearance of huntingtin aggregates triggered by the insulin-signaling pathway.
    J Cell Biol. 2006 Feb 27;172(5):719-31 PMID: 16505167
  64. Mutations in PTEN-induced putative kinase 1 associated with recessive parkinsonism have differential effects on protein stability.
    Proc Natl Acad Sci U S A. 2005 Apr 19;102(16):5703-8 PMID: 15824318
  65. Aggregation of alpha-synuclein in Lewy bodies of sporadic Parkinson's disease and dementia with Lewy bodies.
    Am J Pathol. 1998 Apr;152(4):879-84 PMID: 9546347
  66. Pesticide exposure exacerbates alpha-synucleinopathy in an A53T transgenic mouse model.
    Am J Pathol. 2007 Feb;170(2):658-66 PMID: 17255333
  67. Nigral and cortical Lewy bodies and dystrophic nigral neurites in Parkinson's disease and cortical Lewy body disease contain alpha-synuclein immunoreactivity.
    J Neuropathol Exp Neurol. 1998 Apr;57(4):334-7 PMID: 9600226
  68. Autophagy, proteasomes, lipofuscin, and oxidative stress in the aging brain.
    Int J Biochem Cell Biol. 2004 Dec;36(12):2376-91 PMID: 15325579
  69. Glucocerebrosidase gene mutations are associated with Parkinson's disease in southern Italy.
    Mov Disord. 2008 Feb 15;23(3):460-3 PMID: 18074383
  70. Prelysosomal and lysosomal connections between autophagy and endocytosis.
    Biochem J. 1992 Apr 15;283 ( Pt 2):361-9 PMID: 1575680
  71. Chronic systemic pesticide exposure reproduces features of Parkinson's disease.
    Nat Neurosci. 2000 Dec;3(12):1301-6 PMID: 11100151
Article Info
Journal
The American journal of pathology
Abbr.
Am J Pathol
ISSN
1525-2191
Published
2009-08-00
Epub
2009-00-23
Pages
736-47
Language
English
Region
United States
NLM ID
0370502
PMCID
PMC2716969
Subset
IM
Grants
NINDS NIH HHS · R21 NS050487 · United States
Intramural NIH HHS · Z01 AG000948 · United States
NINDS NIH HHS · NS050487 · United States
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: [email protected]