Protein aggregation and prionopathies

Pathologie Biologie

Volumn 62, Issue 3, 2014, Pages 162-168

  Renner, M ^a   Melki, R ^b  

^a INSERM   (France)

^b LABORATOIRE D ENZYMOLOGIE ET BIOCHIMIE STRUCTURALES   (France)

Author keywords

Alpha synucleinopathies; Alzheimer; Amyotrophic lateral sclerosis; Huntington; Parkinson; Prion; Protein aggregation; Tauopathies

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID BETA PROTEIN; COPPER ZINC SUPEROXIDE DISMUTASE; HUNTINGTIN; POLYGLUTAMINE; PRION PROTEIN; TAU PROTEIN; BIOPOLYMER; HOMOTAURINE; NERVE PROTEIN; POLYSACCHARIDE; PRION;

ALZHEIMER DISEASE; AMYOTROPHIC LATERAL SCLEROSIS; BLOOD BRAIN BARRIER; BRAIN HOMOGENATE; CONFORMATIONAL TRANSITION; CREUTZFELDT JAKOB DISEASE; DEGENERATIVE DISEASE; GENE MUTATION; HUMAN; HUNTINGTON CHOREA; METABOLIC CLEARANCE RATE; MOLECULAR INTERACTION; NEUROPATHOLOGY; NONHUMAN; PARKINSON DISEASE; PRION DISEASE; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN EXPRESSION; PROTEIN FOLDING; REVIEW; TAUOPATHY; TREATMENT PLANNING; AGING; AMYLOID PLAQUE; ANIMAL; AUTOPHAGY; CELL INCLUSION; CHEMISTRY; DISEASE MODEL; DRUG SCREENING; ENDOCYTOSIS; METABOLISM; MOUSE; NEUROFIBRILLARY TANGLE; PATHOLOGY; PHASE 2 CLINICAL TRIAL (TOPIC); PRION; PROTEIN CONFORMATION; PROTEINOSIS; SOLUBILITY; VETERINARY;

AGING; ALZHEIMER DISEASE; AMYOTROPHIC LATERAL SCLEROSIS; ANIMALS; AUTOPHAGY; BIOPOLYMERS; CLINICAL TRIALS, PHASE II AS TOPIC; DISEASE MODELS, ANIMAL; DRUG EVALUATION, PRECLINICAL; ENDOCYTOSIS; HUMANS; INCLUSION BODIES; MICE; NERVE TISSUE PROTEINS; NEURODEGENERATIVE DISEASES; NEUROFIBRILLARY TANGLES; PLAQUE, AMYLOID; POLYSACCHARIDES; PRION DISEASES; PRIONS; PROTEIN AGGREGATION, PATHOLOGICAL; PROTEIN CONFORMATION; SOLUBILITY;

EID: 84902550789     PISSN: 03698114     EISSN: 17683114     Source Type: Journal    
DOI: 10.1016/j.patbio.2014.01.003     Document Type: Review

References (111)

1. Ross C.A., Poirier M.A. Protein aggregation and neurodegenerative disease. Nat Med 2004, 10:S10-S17.
2. Frost B., Diamond M.I. Prion-like mechanisms in neurodegenerative diseases. Nat Rev Neurosci 2010, 11:155-159.
3. Brundin P., Melki R., Kopito R. Prion-like transmission of protein aggregates in neurodegenerative diseases. Nat Rev Mol Cell Biol 2010, 11:301-307.
4. Kopito R.R. Aggresomes, inclusion bodies and protein aggregation. Trends Cell Biol 2000, 10:524-530.
5. Jucker M., Walker L.C. Self-propagation of pathogenic protein aggregates in neurodegenerative diseases. Nature 2013, 501:45-51.
6. Chiti F., Dobson C.M. Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem 2006, 75:333-366.
7. Golde T.E., et al. Thinking laterally about neurodegenerative proteinopathies. J Clin Invest 2013, 123:1847-1855.
8. Ciechanover A., Brundin P. The ubiquitin proteasome system in neurodegenerative diseases: sometimes the chicken, sometimes the egg. Neuron 2003, 40:427-446.
9. Balch W.E., et al. Adapting proteostasis for disease intervention. Science 2008, 319:916-919.
10. Olanow C.W., McNaught K. Parkinson's disease, proteins, and prions: milestones. Mov Disord 2011, 26:1056-1071.
11. Ilieva H., Polymenidou M., Cleveland D.W. Non-cell autonomous toxicity in neurodegenerative disorders: ALS and beyond. J Cell Biol 2009, 187:761-772.
12. Braak H., Braak E. Neuropathological stageing of Alzheimer-related changes. Acta Neuropathol 1991, 82:239-259.
13. Braak H., et al. Stages in the development of Parkinson's disease-related pathology. Cell Tissue Res 2004, 318:121-134.
14. Braak H., et al. Stanley Fahn Lecture 2005: the staging procedure for the inclusion body pathology associated with sporadic Parkinson's disease reconsidered. Mov Disord 2006, 21:2042-2051.
15. Costanzo M., Zurzolo C. The cell biology of prion-like spread of protein aggregates: mechanisms and implication in neurodegeneration. Biochem J 2013, 452:1-17.
16. Aguzzi A., Rajendran L. The transcellular spread of cytosolic amyloids, prions, and prionoids. Neuron 2009, 64:783-790.
17. Gousset K., et al. Prions hijack tunnelling nanotubes for intercellular spread. Nat Cell Biol 2009, 11:328-336.
18. Costanzo M., et al. Transfer of polyglutamine aggregates in neuronal cells occurs in tunneling nanotubes. J Cell Sci 2013, 126:3678-3685.
19. Prusiner S.B. Cell biology. A unifying role for prions in neurodegenerative diseases. Science 2012, 336:1511-1513.
20. Colby D.W., Prusiner S.B. Prions. Cold Spring Harb Perspect Biol 2011, 3:a006833.
21. Soto C., Satani N. The intricate mechanisms of neurodegeneration in prion diseases. Trends Mol Med 2010, 17:14-24.
22. Head M.W. Human prion diseases: molecular, cellular and population biology. Neuropathology 2013, 33:221-236.
23. Goold R., et al. Alternative fates of newly formed PrPSc upon prion conversion on the plasma membrane. J Cell Sci 2013, 126:3552-3562.
24. Kanu N., et al. Transfer of scrapie prion infectivity by cell contact in culture. Curr Biol 2002, 12:523-530.
25. Vella L.J., et al. Packaging of prions into exosomes is associated with a novel pathway of PrP processing. J Pathol 2007, 211:582-590.
26. Fevrier B., et al. Cells release prions in association with exosomes. Proc Natl Acad Sci U S A 2004, 101:9683-9688.
27. Magalhaes A.C., et al. Uptake and neuritic transport of scrapie prion protein coincident with infection of neuronal cells. J Neurosci 2005, 25:5207-5216.
28. Hijazi N., et al. PrPSc incorporation to cells requires endogenous glycosaminoglycan expression. J Biol Chem 2005, 280:17057-17061.
29. Greil C.S., et al. Acute cellular uptake of abnormal prion protein is cell type and scrapie-strain independent. Virology 2008, 379:284-293.
30. Pacheco C., Aguayo L.G., Opazo C. An extracellular mechanism that can explain the neurotoxic effects of alpha-synuclein aggregates in the brain. Front Physiol 2012, 3:297.
31. Goedert M. Alpha-synuclein and neurodegenerative diseases. Nat Rev Neurosci 2001, 2:492-501.
32. Martin I., Dawson V.L., Dawson T.M. Recent advances in the genetics of Parkinson's disease. Annu Rev Genomics Hum Genet 2011, 12:301-325.
33. Burre J., et al. Alpha-synuclein promotes SNARE-complex assembly in vivo and in vitro. Science 2010, 329:1663-1667.
34. Venda L.L., et al. Alpha-synuclein and dopamine at the crossroads of Parkinson's disease. Trends Neurosci 2010, 33:559-568.
35. Braak H., et al. Staging of brain pathology related to sporadic Parkinson's disease. Neurobiol Aging 2003, 24:197-211.
36. Hansen C., Li J.Y. Beyond alpha-synuclein transfer: pathology propagation in Parkinson's disease. Trends Mol Med 2012, 18:248-255.
37. George S., et al. Alpha-synuclein: the long distance runner. Brain Pathol 2013, 23:350-357.
38. Li J.Y., et al. Lewy bodies in grafted neurons in subjects with Parkinson's disease suggest host-to-graft disease propagation. Nat Med 2008, 14:501-503.
39. Kordower J.H., et al. Lewy body-like pathology in long-term embryonic nigral transplants in Parkinson's disease. Nat Med 2008, 14:504-506.
40. Mollenhauer B., et al. Direct quantification of CSF alpha-synuclein by ELISA and first cross-sectional study in patients with neurodegeneration. Exp Neurol 2008, 213:315-325.
41. Desplats P., et al. Inclusion formation and neuronal cell death through neuron-to-neuron transmission of alpha-synuclein. Proc Natl Acad Sci U S A 2009, 106:13010-13015.
42. Hansen C., et al. Alpha-synuclein propagates from mouse brain to grafted dopaminergic neurons and seeds aggregation in cultured human cells. J Clin Invest 2011, 121:715-725.
43. Angot E., et al. Alpha-synuclein cell-to-cell transfer and seeding in grafted dopaminergic neurons in vivo. PLoS One 2012, 7:e39465.
44. Lee H.J., Patel S., Lee S.J. Intravesicular localization and exocytosis of alpha-synuclein and its aggregates. J Neurosci 2005, 25:6016-6024.
45. Freundt E.C., et al. Neuron-to-neuron transmission of alpha-synuclein fibrils through axonal transport. Ann Neurol 2012, 72:517-524.
46. Auluck P.K., Caraveo G., Lindquist S. alpha-Synuclein: membrane interactions and toxicity in Parkinson's disease. Annu Rev Cell Dev Biol 2010, 26:211-233.
47. Danzer K.M., et al. Different species of alpha-synuclein oligomers induce calcium influx and seeding. J Neurosci 2007, 27:9220-9232.
48. Pieri L., et al. Fibrillar alpha-synuclein and huntingtin exon 1 assemblies are toxic to the cells. Biophys J 2012, 102:2894-2905.
49. Volpicelli-Daley L.A., et al. Exogenous alpha-synuclein fibrils induce Lewy body pathology leading to synaptic dysfunction and neuron death. Neuron 2011, 72:57-71.
50. Bousset L., et al. Structural and functional characterization of two alpha-synuclein strains. Nat Commun 2013, 4:2575.
51. Mougenot A.L., et al. Prion-like acceleration of a synucleinopathy in a transgenic mouse model. Neurobiol Aging 2012, 33:2225-2228.
52. Luk K.C., et al. Pathological alpha-synuclein transmission initiates Parkinson-like neurodegeneration in nontransgenic mice. Science 2012, 338:949-953.
53. Nelson P.T., Braak H., Markesbery W.R. Neuropathology and cognitive impairment in Alzheimer disease: a complex but coherent relationship. J Neuropathol Exp Neurol 2009, 68:1-14.
54. Finder V.H., Glockshuber R. Amyloid-beta aggregation. Neurodegener Dis 2007, 4:13-27.
55. Reid A.T., Evans A.C. Structural networks in Alzheimer's disease. Eur Neuropsychopharmacol 2013, 23:63-77.
56. Lacor P.N., et al. Abeta oligomer-induced aberrations in synapse composition, shape, and density provide a molecular basis for loss of connectivity in Alzheimer's disease. J Neurosci 2007, 27:796-807.
57. Shankar G.M., et al. Amyloid-beta protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory. Nat Med 2008, 14:837-842.
58. Renner M., et al. Deleterious effects of amyloid beta oligomers acting as an extracellular scaffold for mGluR5. Neuron 2010, 66:739-754.
59. Venkitaramani D.V., et al. Beta-amyloid modulation of synaptic transmission and plasticity. J Neurosci 2007, 27:11832-11837.
60. Shrivastava A.N., et al. beta-amyloid and ATP-induced diffusional trapping of astrocyte and neuronal metabotropic glutamate type-5 receptors. Glia 2013, 61:1673-1686.
61. Kuchibhotla K.V., et al. Abeta plaques lead to aberrant regulation of calcium homeostasis in vivo resulting in structural and functional disruption of neuronal networks. Neuron 2008, 59:214-225.
62. Busche M.A., et al. Clusters of hyperactive neurons near amyloid plaques in a mouse model of Alzheimer's disease. Science 2008, 321:1686-1689.
63. Bezprozvanny I., Mattson M.P. Neuronal calcium mishandling and the pathogenesis of Alzheimer's disease. Trends Neurosci 2008, 31:454-463.
64. Ittner L.M., et al. Dendritic function of Tau mediates amyloid-beta toxicity in Alzheimer's disease mouse models. Cell 2010, 142:387-397.
65. Vossel K.A., et al. Tau reduction prevents Abeta-induced defects in axonal transport. Science 2010, 330:198.
66. Meyer-Luehmann M., et al. Exogenous induction of cerebral beta-amyloidogenesis is governed by agent and host. Science 2006, 313:1781-1784.
67. Langer F., et al. Soluble Abeta seeds are potent inducers of cerebral beta-amyloid deposition. J Neurosci 2011, 31:14488-14495.
68. Stohr J., et al. Purified and synthetic Alzheimer's amyloid beta (Abeta) prions. Proc Natl Acad Sci U S A 2012, 109:11025-11030.
69. Eisele Y.S., et al. Peripherally applied Abeta-containing inoculates induce cerebral beta-amyloidosis. Science 2010, 330:980-982.
70. Heilbronner G., et al. Seeded strain-like transmission of beta-amyloid morphotypes in APP transgenic mice. EMBO Rep 2013, 30:1017-1022.
71. Harris J.A., et al. Transsynaptic progression of amyloid-beta-induced neuronal dysfunction within the entorhinal-hippocampal network. Neuron 2010, 68:428-441.
72. Nath S., et al. Spreading of neurodegenerative pathology via neuron-to-neuron transmission of beta-amyloid. J Neurosci 2012, 32:8767-8777.
73. Goedert M., Klug A., Crowther R.A. Tau protein, the paired helical filament and Alzheimer's disease. J Alzheimers Dis 2006, 9:195-207.
74. Lace G., et al. Hippocampal Tau pathology is related to neuroanatomical connections: an ageing population-based study. Brain 2009, 132:1324-1334.
75. Delacourte A., et al. Tau aggregation in the hippocampal formation: an ageing or a pathological process?. Exp Gerontol 2002, 37:1291-1296.
76. Frost B., Jacks R.L., Diamond M.I. Propagation of Tau misfolding from the outside to the inside of a cell. J Biol Chem 2009, 284:12845-12852.
77. Guo J.L., Lee V.M. Seeding of normal Tau by pathological Tau conformers drives pathogenesis of Alzheimer-like tangles. J Biol Chem 2011, 286:15317-15331.
78. Clavaguera F., et al. Transmission and spreading of Tauopathy in transgenic mouse brain. Nat Cell Biol 2009, 11:909-913.
79. de Calignon A., et al. Propagation of Tau pathology in a model of early Alzheimer's disease. Neuron 2012, 73:685-697.
80. Kfoury N., et al. Trans-cellular propagation of Tau aggregation by fibrillar species. J Biol Chem 2012, 287:19440-19451.
81. Polymenidou M., Cleveland D.W. The seeds of neurodegeneration: prion-like spreading in ALS. Cell 2011, 147:498-508.
82. Bruijn L.I., Miller T.M., Cleveland D.W. Unraveling the mechanisms involved in motor neuron degeneration in ALS. Annu Rev Neurosci 2004, 27:723-749.
83. Ling S.C., Polymenidou M., Cleveland D.W. Converging mechanisms in ALS and FTD: disrupted RNA and protein homeostasis. Neuron 2013, 79:416-438.
84. Ravits J., Paul P., Jorg C. Focality of upper and lower motor neuron degeneration at the clinical onset of ALS. Neurology 2007, 68:1571-1575.
85. Munch C., Bertolotti A. Propagation of the prion phenomenon: beyond the seeding principle. J Mol Biol 2012, 421:491-498.
86. Munch C., O'Brien J., Bertolotti A. Prion-like propagation of mutant superoxide dismutase-1 misfolding in neuronal cells. Proc Natl Acad Sci U S A 2011, 108:3548-3553.
87. Grad L.I., et al. Intermolecular transmission of superoxide dismutase 1 misfolding in living cells. Proc Natl Acad Sci U S A 2011, 108:16398-16403.
88. Williams A.J., Paulson H.L. Polyglutamine neurodegeneration: protein misfolding revisited. Trends Neurosci 2008, 31:521-528.
89. Yang W., et al. Aggregated polyglutamine peptides delivered to nuclei are toxic to mammalian cells. Hum Mol Genet 2002, 11:2905-2917.
90. Kazantsev A., et al. Insoluble detergent-resistant aggregates form between pathological and nonpathological lengths of polyglutamine in mammalian cells. Proc Natl Acad Sci U S A 1999, 96:11404-11409.
91. Busch A., et al. Mutant huntingtin promotes the fibrillogenesis of wild-type huntingtin: a potential mechanism for loss of huntingtin function in Huntington's disease. J Biol Chem 2003, 278:41452-41461.
92. Trevino R.S., et al. Fibrillar structure and charge determine the interaction of polyglutamine protein aggregates with the cell surface. J Biol Chem 2012, 287:29722-29728.
93. Ren P.H., et al. Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates. Nat Cell Biol 2009, 11:219-225.
94. Jellinger K.A. Interaction between pathogenic proteins in neurodegenerative disorders. J Cell Mol Med 2012, 16:1166-1183.
95. Morales R., et al. Molecular cross talk between misfolded proteins in animal models of Alzheimer's and prion diseases. J Neurosci 2010, 30:4528-4535.
96. Lauren J., et al. Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers. Nature 2009, 457:1128-1132.
97. Um J.W., et al. Alzheimer amyloid-beta oligomer bound to postsynaptic prion protein activates Fyn to impair neurons. Nat Neurosci 2012, 15:1227-1235.
98. Um J.W., et al. Metabotropic glutamate receptor 5 is a coreceptor for Alzheimer abeta oligomer bound to cellular prion protein. Neuron 2013, 79:887-902.
99. Masliah E., et al. beta-amyloid peptides enhance alpha-synuclein accumulation and neuronal deficits in a transgenic mouse model linking Alzheimer's disease and Parkinson's disease. Proc Natl Acad Sci U S A 2001, 98:12245-12250.
100. Bate C., Gentleman S., Williams A. alpha-synuclein induced synapse damage is enhanced by amyloid-beta1-42. Mol Neurodegener 2010, 5:55.
101. Fuentealba R.A., et al. Interaction with polyglutamine aggregates reveals a Q/N-rich domain in TDP-43. J Biol Chem 2010, 285:26304-26314.
102. Schwab C., et al. Colocalization of transactivation-responsive DNA-binding protein 43 and huntingtin in inclusions of Huntington disease. J Neuropathol Exp Neurol 2008, 67:1159-1165.
103. Elden A.C., et al. Ataxin-2 intermediate-length polyglutamine expansions are associated with increased risk for ALS. Nature 2010, 466:1069-1075.
104. Yanamandra K., et al. Anti-Tau antibodies that block Tau aggregate seeding in vitro markedly decrease pathology and improve cognition in vivo. Neuron 2013, 80:402-414.
105. Pemberton S., et al. Hsc70 protein interaction with soluble and fibrillar alpha-synuclein. J Biol Chem 2011, 286:34690-34699.
106. Redeker V., et al. Identification of protein interfaces between alpha-synuclein, the principal component of Lewy bodies in Parkinson disease, and the molecular chaperones human Hsc70 and the yeast Ssa1p. J Biol Chem 2012, 287:32630-32639.
107. Sheehan J.J., Tsirka S.E. Fibrin-modifying serine proteases thrombin, tPA, and plasmin in ischemic stroke: a review. Glia 2005, 50:340-350.
108. Tucker H.M., et al. The plasmin system is induced by and degrades amyloid-beta aggregates. J Neurosci 2000, 20:3937-3946.
109. Kim K.S., et al. Proteolytic cleavage of extracellular alpha-synuclein by plasmin: implications for Parkinson disease. J Biol Chem 2012, 287:24862-24872.
110. Lansbury P.T., Lashuel H.A. A century-old debate on protein aggregation and neurodegeneration enters the clinic. Nature 2006, 443:774-779.
111. Garden G.A., La Spada A.R. Intercellular (mis)communication in neurodegenerative disease. Neuron 2012, 73:886-901.