Impaired autophagy: A link between neurodegenerative diseases and progressive myoclonus epilepsies

Trends in Molecular Medicine

Volumn 17, Issue 6, 2011, Pages 293-300

  Polajnar, Mira ^a   Žerovnik, Eva ^a  

^a JO EF STEFAN INSTITUTE   (Slovenia)

Author keywords

[No Author keywords available]

Indexed keywords

AUTOPHAGY; CORRELATION ANALYSIS; DEGENERATIVE DISEASE; HUMAN; MUTATIONAL ANALYSIS; MYOCLONUS EPILEPSY; NEURONAL CEROID LIPOFUSCINOSIS; PATHOPHYSIOLOGY; PHENOTYPE; PROTEIN AGGREGATION; RAGGED RED FIBERS SYNDROME; REVIEW; SIALIDOSIS;

AUTOPHAGY; BIOLOGICAL MARKERS; CARRIER PROTEINS; CYSTATIN B; HUMANS; MICROTUBULE-ASSOCIATED PROTEINS; MODELS, BIOLOGICAL; MYOCLONIC EPILEPSIES, PROGRESSIVE; NEURODEGENERATIVE DISEASES; OXIDATIVE STRESS; PROTEIN TYROSINE PHOSPHATASES, NON-RECEPTOR; SIROLIMUS; TOR SERINE-THREONINE KINASES;

EID: 79958768725     PISSN: 14714914     EISSN: 1471499X     Source Type: Journal    
DOI: 10.1016/j.molmed.2011.02.005     Document Type: Review

References (91)

1. Shahwan A., et al. Progressive myoclonic epilepsies: a review of genetic and therapeutic aspects. Lancet Neurol. 2005, 4:239-248.
2. Gaitatzis A., et al. The epidemiology of the comorbidity of epilepsy in the general population. Epilepsia 2004, 45:1613-1622.
3. Ramachandran N., et al. The autosomal recessively inherited progressive myoclonus epilepsies and their genes. Epilepsia 2009, 50:29-36.
4. Pennacchio L.A., et al. Progressive ataxia, myoclonic epilepsy and cerebellar apoptosis in cystatin B-deficient mice. Nat. Genet. 1998, 20:251-258.
5. Alakurtti K., et al. Loss of lysosomal association of cystatin B proteins representing progressive myoclonus epilepsy EPM1, mutations. Eur. J. Hum. Genet. 2005, 13:208-215.
6. Lehtinen M.K., et al. Cystatin B deficiency sensitizes neurons to oxidative stress in progressive myoclonus epilepsy EPM1. J. Neurosci. 2009, 29:5910-5915.
7. Gentry M.S., et al. Lafora disease: insights into neurodegeneration from plant metabolism. Trends Biochem. Sci. 2009, 34:628-639.
8. Koike M., et al. Cathepsin D deficiency induces lysosomal storage with ceroid lipofuscin in mouse CNS neurons. J. Neurosci. 2000, 20:6898-6906.
9. Genton P. Unverricht-Lundborg disease (EPM1). Epilepsia 2010, 51:37-39.
10. Kalviainen R., et al. Clinical picture of EPM1-Unverricht-Lundborg disease. Epilepsia 2008, 49:549-556.
11. Joensuu T., et al. Molecular background of EPM1-Unverricht-Lundborg disease. Epilepsia 2008, 49:557-563.
12. Koskenkorva P., et al. Motor cortex and thalamic atrophy in Unverricht-Lundborg disease: voxel-based morphometric study. Neurology 2009, 73:606-611.
13. Lalioti M.D., et al. Identification of mutations in cystatin B, the gene responsible for the Unverricht-Lundborg type of progressive myoclonus epilepsy (EPM1). Am. J. Hum. Genet. 1997, 60:342-351.
14. Pennacchio L.A., et al. Mutations in the gene encoding cystatin B in progressive myoclonus epilepsy (EPM1). Science 1996, 271:1731-1734.
15. Riccio M., et al. Nuclear localization of cystatin B, the cathepsin inhibitor implicated in myoclonus epilepsy (EPM1). Exp. Cell Res. 2001, 262:84-94.
16. Ceru S., et al. Intracellular aggregation of human stefin B: confocal and electron microscopy study. Biol. Cell 2010, 102:319-334.
17. Cipollini E., et al. Cystatin B and its EPM1 mutants are polymeric and aggregate prone in vivo. Biochim. Biophys. Acta 2008, 1783:312-322.
18. Rabzelj S., et al. In vitro study of stability and amyloid-fibril formation of two mutants of human stefin B (cystatin B) occurring in patients with EPM1. Protein Sci. 2005, 14:2713-2722.
19. Ceru S., et al. Protein aggregation as a possible cause for pathology in a subset of familial Unverricht-Lundborg disease. Med. Hypotheses 2005, 64:955-959.
20. Singh S.M., et al. Missense mutations in dystrophin that trigger muscular dystrophy decrease protein stability and lead to cross-beta aggregates. Proc. Natl. Acad. Sci. U.S.A. 2010, 107:15069-15074.
21. Turk V., Turk B. Lysosomal cysteine proteases and their protein inhibitors: recent developments. Acta Chim. Slov. 2008, 55:727-738.
22. Turk V., et al. Lysosomal cathepsins: structure, role in antigen processing and presentation, and cancer. Adv. Enzyme Regul. 2002, 42:285-303.
23. Di Giaimo R., et al. New insights into the molecular basis of progressive myoclonus epilepsy: a multiprotein complex with cystatin B. Hum. Mol. Genet. 2002, 11:2941-2950.
24. Ceru S., et al. Stefin B interacts with histones and cathepsin L in the nucleus. J. Biol. Chem. 2010, 285:10078-10086.
25. Kopitar-Jerala N., et al. Sensitization of stefin B-deficient thymocytes towards staurosporin-induced apoptosis is independent of cysteine cathepsins. FEBS Lett. 2005, 579:2149-2155.
26. Yang F., et al. Cystatin B inhibition of TRAIL-induced apoptosis is associated with the protection of FLIP(L) from degradation by the E3 ligase itch in human melanoma cells. Cell Death Differ. 2010, 17:1354-1367.
27. Bassuk A.G., et al. A homozygous mutation in human PRICKLE1 causes an autosomal-recessive progressive myoclonus epilepsy-ataxia syndrome. Am. J. Hum. Genet. 2008, 83:572-581.
28. Berkovic S.F., et al. A new clinical and molecular form of Unverricht-Lundborg disease localized by homozygosity mapping. Brain 2005, 128:652-658.
29. Dibbens L.M., et al. SCARB2 mutations in progressive myoclonus epilepsy (PME) without renal failure. Ann. Neurol. 2009, 66:532-536.
30. Ganesh S., et al. Laforin, defective in the progressive myoclonus epilepsy of Lafora type, is a dual-specificity phosphatase associated with polyribosomes. Hum. Mol. Genet. 2000, 9:2251-2261.
31. Worby C.A., et al. Laforin, a dual specificity phosphatase that dephosphorylates complex carbohydrates. J. Biol. Chem. 2006, 281:30412-30418.
32. Gentry M.S., et al. Insights into Lafora disease: malin is an E3 ubiquitin ligase that ubiquitinates and promotes the degradation of laforin. Proc. Natl. Acad. Sci. U.S.A. 2005, 102:8501-8506.
33. Ganesh S., et al. Recent advances in the molecular basis of Lafora's progressive myoclonus epilepsy. J. Hum. Genet. 2006, 51:1-8.
34. Moreno D., et al. The laforin-malin complex, involved in Lafora disease, promotes the incorporation of K63-linked ubiquitin chains into AMP-activated protein kinase beta subunits. Mol. Biol. Cell 2010, 21:2578-2588.
35. Tagliabracci V.S., et al. Laforin is a glycogen phosphatase, deficiency of which leads to elevated phosphorylation of glycogen in vivo. Proc. Natl. Acad. Sci. U.S.A. 2007, 104:19262-19266.
36. Lohi H., et al. Novel glycogen synthase kinase 3 and ubiquitination pathways in progressive myoclonus epilepsy. Hum. Mol. Genet. 2005, 14:2727-2736.
37. Worby C.A., et al. Malin decreases glycogen accumulation by promoting the degradation of protein targeting to glycogen (PTG). J. Biol. Chem. 2008, 283:4069-4076.
38. Mittal S., et al. Lafora disease proteins malin and laforin are recruited to aggresomes in response to proteasomal impairment. Hum. Mol. Genet. 2007, 16:753-762.
39. Aguado C., et al. Laforin, the most common protein mutated in Lafora disease, regulates autophagy. Hum. Mol. Genet. 2010, 19:2867-2876.
40. Knecht E., et al. Impaired autophagy in Lafora disease. Autophagy 2010, 6:991-993.
41. Puri R., Ganesh S. Laforin in autophagy: a possible link between carbohydrate and protein in Lafora disease?. Autophagy 2009, 1229-1231.
42. Roze E., et al. Huntington's disease. Adv. Exp. Med. Biol. 2010, 685:45-63.
43. Huang C.C., et al. Amyloid formation by mutant huntingtin: threshold, progressivity and recruitment of normal polyglutamine proteins. Somat. Cell Mol. Genet. 1998, 24:217-233.
44. Perutz M.F. Glutamine repeats and neurodegenerative diseases: molecular aspects. Trends Biochem. Sci. 1999, 24:58-63.
45. Alcalay R.N., et al. Frequency of known mutations in early-onset Parkinson disease: implication for genetic counseling: the consortium on risk for early onset Parkinson disease study. Arch. Neurol. 2010, 67:1116-1122.
46. Suhara T., et al. Abeta42 generation is toxic to endothelial cells and inhibits eNOS function through an Akt/GSK-3beta signaling-dependent mechanism. Neurobiol. Aging 2003, 24:437-451.
47. Zerovnik E. Amyloid-fibril formation Proposed mechanisms and relevance to conformational disease. Eur. J. Biochem. 2002, 269:3362-3371.
48. Wisniewski T., Sigurdsson E.M. Therapeutic approaches for prion and Alzheimer's diseases. FEBS J. 2007, 274:3784-3798.
49. Wisniewski T., Boutajangout A. Vaccination as a therapeutic approach to Alzheimer's disease. Mt. Sinai J. Med. 2010, 77:17-31.
50. Bush A.I. Drug development based on the metals hypothesis of Alzheimer's disease. J. Alzheimers Dis. 2008, 15:223-240.
51. Irvine G.B., et al. Protein aggregation in the brain: the molecular basis for Alzheimer's and Parkinson's diseases. Mol. Med. 2008, 14:451-464.
52. Hardy J.A., Higgins G.A. Alzheimer's disease: the amyloid cascade hypothesis. Science 1992, 256:184-185.
53. Lue L.F., et al. Soluble amyloid beta peptide concentration as a predictor of synaptic change in Alzheimer's disease. Am. J. Pathol. 1999, 155:853-862.
54. Rhein V., et al. Amyloid-beta and tau synergistically impair the oxidative phosphorylation system in triple transgenic Alzheimer's disease mice. Proc. Natl. Acad. Sci. U.S.A. 2009, 106:20057-20062.
55. Stokin G.B., et al. Axonopathy and transport deficits early in the pathogenesis of Alzheimer's disease. Science 2005, 307:1282-1288.
56. Butterfield D.A., Bush A.I. Alzheimer's amyloid beta-peptide (1-42): involvement of methionine residue 35 in the oxidative stress and neurotoxicity properties of this peptide. Neurobiol. Aging 2004, 25:563-568.
57. Lashuel H.A., et al. Neurodegenerative disease: amyloid pores from pathogenic mutations. Nature 2002, 418:291.
58. Kopito R.R. Aggresomes, inclusion bodies and protein aggregation. Trends Cell Biol. 2000, 10:524-530.
59. Tanida I. Autophagosome formation and molecular mechanism of autophagy. Antioxid. Redox Signal. 2010, 10.1089/ars.2010.3482.
60. Cuervo A.M., et al. Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy. Science 2004, 305:1292-1295.
61. Arstila A.U., Trump B.F. Studies on cellular autophagocytosis. The formation of autophagic vacuoles in the liver after glucagon administration. Am. J. Pathol. 1968, 53:687-733.
62. McCray B.A., Taylor J.P. The role of autophagy in age-related neurodegeneration. Neurosignals 2008, 16:75-84.
63. Nedelsky N.B., et al. Autophagy and the ubiquitin-proteasome system: collaborators in neuroprotection. Biochim. Biophys. Acta 2008, 1782:691-699.
64. Chin, L.S. et al. (2010) Parkin-mediated ubiquitin signalling in aggresome formation and autophagy. Biochem. Soc. Trans. 38, 144-149.
65. Wong E., Cuervo A.M. Autophagy gone awry in neurodegenerative diseases. Nat. Neurosci. 2010, 13:805-811.
66. Cai S., et al. Kinesin-14 family proteins HSET/XCTK2 control spindle length by cross-linking and sliding microtubules. Mol. Biol. Cell 2009, 20:1348-1359.
67. Kiselyov K., et al. Autophagy, mitochondria and cell death in lysosomal storage diseases. Autophagy 2007, 3:259-262.
68. Scherz-Shouval R., et al. Reactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4. EMBO J. 2007, 26:1749-1760.
69. Lim D., et al. Calcium homeostasis and mitochondrial dysfunction in striatal neurons of Huntington disease. J. Biol. Chem. 2008, 283:5780-5789.
70. Vila M., Perier C. Molecular pathways of programmed cell death in experimental Parkinson's disease. Parkinsonism Relat. Disord. 2008, 14(Suppl. 2):S176-179.
71. Halestrap A.P. What is the mitochondrial permeability transition pore?. J. Mol. Cell. Cardiol. 2009, 46:821-831.
72. Koike M., et al. Participation of autophagy in storage of lysosomes in neurons from mouse models of neuronal ceroid-lipofuscinoses (Batten disease). Am. J. Pathol. 2005, 167:1713-1728.
73. Tizon B., et al. Induction of autophagy by cystatin C: a mechanism that protects murine primary cortical neurons and neuronal cell lines. PLoS ONE 2010, 5:e9819.
74. Zerovnik E. The emerging role of cystatins in Alzheimer's disease. Bioessays 2009, 31:597-599.
75. Cohen N.R., et al. New neuropathological findings in Unverricht-Lundborg disease: neuronal intranuclear and cytoplasmic inclusions. Acta Neuropathol. 2010, 121:421-427.
76. Depaoli-Roach A.A., et al. Genetic depletion of the malin E3 ubiquitin ligase in mice leads to Lafora bodies and the accumulation of insoluble laforin. J. Biol. Chem. 2010, 285:25372-25381.
77. Garyali P., et al. The malin-laforin complex suppresses the cellular toxicity of misfolded proteins by promoting their degradation through the ubiquitin-proteasome system. Hum. Mol. Genet. 2009, 18:688-700.
78. Alirezaei M., et al. Autophagy, inflammation and neurodegenerative disease. Eur. J. Neurosci. 2011, 33:197-204.
79. Waelter S., et al. Accumulation of mutant huntingtin fragments in aggresome-like inclusion bodies as a result of insufficient protein degradation. Mol. Biol. Cell 2001, 12:1393-1407.
80. Mizushima, N. et al. (2010) Methods in mammalian autophagy research. Cell 140, 313-326.
81. Bartolini M., Andrisano V. Strategies for the inhibition of protein aggregation in human diseases. Chembiochem 2010, 11:1018-1035.
82. Soto C., Estrada L. Amyloid inhibitors and beta-sheet breakers. Subcell. Biochem. 2005, 38:351-364.
83. Schmelzle T., Hall M.N. TOR, a central controller of cell growth. Cell 2000, 103:253-262.
84. Mehrpour M., et al. Overview of macroautophagy regulation in mammalian cells. Cell Res. 2010, 20:748-762.
85. Berger Z., et al. Rapamycin alleviates toxicity of different aggregate-prone proteins. Hum. Mol. Genet. 2006, 15:433-442.
86. Ravikumar B., et al. Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease. Nat. Genet. 2004, 36:585-595.
87. Floto R.A., et al. Small molecule enhancers of rapamycin-induced TOR inhibition promote autophagy, reduce toxicity in Huntington's disease models and enhance killing of mycobacteria by macrophages. Autophagy 2007, 3:620-622.
88. Nixon R.A., et al. Extensive involvement of autophagy in Alzheimer disease: an immuno-electron microscopy study. J. Neuropathol. Exp. Neurol. 2005, 64:113-122.
89. Anglade P., et al. Apoptosis and autophagy in nigral neurons of patients with Parkinson's disease. Histol. Histopathol. 1997, 12:25-31.
90. Sikorska B., et al. Autophagy is a part of ultrastructural synaptic pathology in Creutzfeldt-Jakob disease: a brain biopsy study. Int. J. Biochem. Cell Biol. 2004, 36:2563-2573.
91. Sapp E., et al. Huntingtin localization in brains of normal and Huntington's disease patients. Ann. Neurol. 1997, 42:604-612.