Sporadic inclusion-body myositis: A degenerative muscle disease associated with aging, impaired muscle protein homeostasis and abnormal mitophagy

Biochimica et Biophysica Acta - Molecular Basis of Disease

Volumn 1852, Issue 4, 2015, Pages 633-643

  Askanas, Valerie ^a   Engel, W King ^a   Nogalska, Anna ^a  

^a UNIVERSITY OF SOUTHERN CALIFORNIA   (United States)

Author keywords

Aging; Amyloid 42; Autophagy; Inclusion body myositis; Mitophagy; Multiprotein aggregates

Indexed keywords

AMYLOID BETA PROTEIN[1-42]; MUSCLE PROTEIN; TAU PROTEIN; AMYLOID BETA PROTEIN; AMYLOID BETA-PROTEIN (1-42); PEPTIDE FRAGMENT;

AGING; ARTICLE; HUMAN; INCLUSION BODY MYOSITIS; MITOPHAGY; MOLECULAR PATHOLOGY; MUSCLE BIOPSY; MUSCLE CELL; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN HOMEOSTASIS; PROTEIN PHOSPHORYLATION; PROTEIN PROCESSING; ALZHEIMER DISEASE; ANIMAL; BRAIN; METABOLISM; MORTALITY; PARKINSON DISEASE; PATHOLOGY; PROTEIN SYNTHESIS; PROTEINOSIS; PROTEOSTASIS DEFICIENCY; SKELETAL MUSCLE;

AGING; ALZHEIMER DISEASE; AMYLOID BETA-PEPTIDES; ANIMALS; BRAIN; HUMANS; MUSCLE FIBERS, SKELETAL; MYOSITIS, INCLUSION BODY; PARKINSON DISEASE; PEPTIDE FRAGMENTS; PROTEIN AGGREGATION, PATHOLOGICAL; PROTEIN BIOSYNTHESIS; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEOSTASIS DEFICIENCIES;

EID: 84922324292     PISSN: 09254439     EISSN: 1879260X     Source Type: Journal    
DOI: 10.1016/j.bbadis.2014.09.005     Document Type: Article

References (137)

1. Askanas V., Engel W.K. Inclusion-body myositis, a multifactorial muscle disease associated with aging: current concepts of pathogenesis. Curr. Opin. Rheumatol. 2007, 19:550-559.
2. Askanas V., Engel W.K. Inclusion-body myositis: muscle-fiber molecular pathology and possible pathogenic significance of its similarity to Alzheimer's and Parkinson's disease brains. Acta Neuropathol. 2008, 116:583-595.
3. Askanas V., Engel W.K., Nogalska A. Inclusion body myositis: a degenerative muscle disease associated with intra-muscle fiber multi-protein aggregates, proteasome inhibition, endoplasmic reticulum stress and decreased lysosomal degradation. Brain Pathol. 2009, 19:493-506.
4. Engel W.K., Askanas V. Inclusion-body myositis: clinical, diagnostic, and pathologic aspects. Neurology 2006, 66:S20-S29.
5. Askanas V., Engel W.K. Inclusion-body myositis: a myodegenerative conformational disorder associated with Abeta, protein misfolding, and proteasome inhibition. Neurology 2006, 66:S39-S48.
6. Amouri R., Driss A., Murayama K., Kefi M., Nishino I., Hentati F. Allelic heterogeneity of GNE gene mutation in two Tunisian families with autosomal recessive inclusion body myopathy. Neuromuscul. Disord. 2005, 15:361-363.
7. Askanas V., Engel W.K. Hereditary inclusion body myopathies. The Molecular and Genetic Basis of Neurologic and Psychiatric Disease 2008, 524-531. Wolters Kluver, Lippincott Williams & Wilkins. R.N. Rosenberg, S. Di Mauro, H.L. Paulson, L. Ptacek, E.J. Nestler (Eds.).
8. Krause S., Schlotter-Weigel B., Walter M.C., Najmabadi H., Wiendl H., Muller-Hocker J., Muller-Felber W., Pongratz D., Lochmuller H. A novel homozygous missense mutation in the GNE gene of a patient with quadriceps-sparing hereditary inclusion body myopathy associated with muscle inflammation. Neuromuscul. Disord. 2003, 13:830-834.
9. Askanas V., Engel W.K. Inclusion-body myositis and myopathies: different etiologies, possibly similar pathogenic mechanisms. Curr. Opin. Neurol. 2002, 15:525-531.
10. Page L.J., Suk J.Y., Bazhenova L., Fleming S.M., Wood M., Jiang Y., Guo L.T., Mizisin A.P., Kisilevsky R., Shelton G.D., Balch W.E., Kelly J.W. Secretion of amyloidogenic gelsolin progressively compromises protein homeostasis leading to the intracellular aggregation of proteins. Proc. Natl. Acad. Sci. U. S. A. 2009, 106:11125-11130.
11. Dalakas M.C. Immunotherapy of myositis: issues, concerns and future prospects. Nat. Rev. Rheumatol. 2010, 6:129-137.
12. Benveniste O., Guiguet M., Freebody J., Dubourg O., Squier W., Maisonobe T., Stojkovic T., Leite M.I., Allenbach Y., Herson S., Brady S., Eymard B., Hilton-Jones D. Long-term observational study of sporadic inclusion body myositis. Brain 2011, 134:3176-3184.
13. Dimachkie M.M., Barohn R.J. Inclusion body myositis. Curr. Neurol. Neurosci. Rep. 2013, 13:321.
14. Dalakas M.C. Review: an update on inflammatory and autoimmune myopathies. Neuropathol. Appl. Neurobiol. 2011, 37:226-242.
15. Schmidt J., Dalakas M.C. Inclusion body myositis: from immunopathology and degenerative mechanisms to treatment perspectives. Expert. Rev. Clin. Immunol. 2013, 9:1125-1133.
16. Dalakas M.C. Inflammatory and autoimmune features of inclusion-body myositis. Muscle aging, inclusion-body myositis and myopathies 2012, 146-158. Wiley-Blackwell, Oxford, UK. V. Askanas, W.K. Engel (Eds.).
17. Rojana-udomsart A., James I., Castley A., Needham M., Scott A., Day T., Kiers L., Corbett A., Sue C., Witt C., Martinez P., Christiansen F., Mastaglia F. High-resolution HLA-DRB1 genotyping in an Australian inclusion body myositis (s-IBM) cohort: an analysis of disease-associated alleles and diplotypes. J. Neuroimmunol. 2012, 250:77-82.
18. Mastaglia F.L., Rojana-udomsart A., James I., Needham M., Day T.J., Kiers L., Corbett J.A., Saunders A.M., Lutz M.W., Roses A.D. Polymorphism in the TOMM40 gene modifies the risk of developing sporadic inclusion body myositis and the age of onset of symptoms. Neuromuscul. Disord. 2013, 23:969-974.
19. Hansson Petersen C.A., Alikhani N., Behbahani H., Wiehager B., Pavlov P.F., Alafuzoff I., Leinonen V., Ito A., Winblad B., Glaser E., Ankarcrona M. The amyloid β-peptide is imported into mitochondria via the TOM import machinery and localized to mitochondrial cristae. Proc. Natl. Acad. Sci. U. S. A. 2008, 105:13145-13150.
20. Spinney L. Alzheimer's disease: the forgetting gene. Nature 2014, 510:26-28.
21. Mastaglia F. Sporadic inclusion-body myositis: clinical symptoms, physical findings, and diagnostic investigations. Muscle aging, inclusion-body myositis and myopathies 2012, 159-167. Wiley-Blackwell, Oxford, UK. V. Askanas, W.K. Engel (Eds.).
22. Rojana-udomsart A., Bundell C., James I., Castley A., Martinez P., Christiansen F., Hollingsworth P., Mastaglia F. Frequency of autoantibodies and correlation with HLA-DRB1 genotype in sporadic inclusion body myositis (s-IBM): a population control study. J. Neuroimmunol. 2012, 249:66-70.
23. Larman B.H., Salajegheh M., Nazareno R., Lam T., Sauld J., Steen H., Won Kong S., Pinkus J.L., Amato A.A., Elledge S.J., Greenberg S.A. Cytosolic 5'-nucleotidase 1A autoimmunity in sporadic inclusion body myositis. Ann. Neurol. 2013, 73:408-418.
24. Pluk H., van Hoeve B.J.A., van Dooren S.H.J., Stammen-Vogelzangs J., van der Heijden A., Schelhaas H.J., Verbeek M.M., Badrising U.A., Arnardottir S., Gheorghe K., Lundberg I.E., Boelens W.C., van Engelen B.G., Pruijn G.J.M. Autoantibodies to cytosolic 5'-nucleotidase 1A in inclusion body myositis. Ann. Neurol. 2013, 73:397-407.
25. Askanas V., Engel W.K., Nogalska A. Pathogenic considerations in sporadic inclusion-body myositis, a degenerative muscle disease associated with aging and abnormalities of myoproteostasis. J. Neuropathol. Exp. Neurol. 2012, 71:680-693.
26. Askanas V., Engel W.K., Nogalska A. Pathogenesis of sporadic inclusion-body myositis; role of ageing and muscle-fibre degeneration, and accumulation of the same proteins as in Alzheimer and Parkinson brains. Muscle Ageing 2012, 111-145. Inclusion-Body Myositis and Myopathies Wiley-Blackwell, Oxford, UK. V. Askanas, W.K. Engel (Eds.).
27. Askanas V., Engel W.K. Sporadic inclusion-body myositis: conformational multifactorial ageing-related degenerative muscle disease associated with proteasomal and lysosomal inhibition, endoplasmic reticulum stress, and accumulation of amyloid-beta42 oligomers and phosphorylated tau. Presse Med. 2011, 40:e219-e235.
28. Morosetti R., Mirabella M., Gliubizzi C., Broccolini A., De Angelis L., Tagliafico E., Sampaolesi M., Gidaro T., Papacci M., Roncaglia E., Rutella S., Ferrari S., Tonali P.A., Ricci E., Cossu G. MyoD expression restores defective myogenic differentiation of human mesoangioblasts from inclusion-body myositis muscle. Proc. Natl. Acad. Sci. U. S. A. 2006, 103:16995-17000.
29. Morosetti R., Gliubizzi C., Sancricca C., Broccolini A., Gidaro T., Lucchini M., Mirabella M. TWEAK in inclusion-body myositis muscle: possible pathogenic role of a cytokine inhibiting myogenesis. Am. J. Pathol. 2012, 180:1603-1613.
30. Hogrel J.Y., Allenbach Y., Canal A., Leroux G., Ollivier G., Mariampillai K., Servais L., Herson S., Decostre V., Benveniste O. Four-year longitudinal study of clinical and functional endpoints in sporadic inclusion body myositis: implications for therapeutic trials. Neuromuscul. Disord. 2014, 24:604-610.
31. Abdo W.F., van Mierlo T., Hengstman G.J., Schelhaas H.J., van Engelen B.G., Verbeek M.M. Increased plasma amyloid-beta42 protein in sporadic inclusion body myositis. Acta Neuropathol. 2009, 118:429-431.
32. Brady S., Squier W., Sewry C., Hanna M., Hilton-Jones D., Holton J.L. A retrospective cohort study identifying the principal pathological features useful in the diagnosis of inclusion body myositis. BMJ Open 2014, 4:e004552.
33. Klingstedt T., Blechschmidt C., Nogalska A., Prokop S., Haggqvist B., Danielsson O., Engel W.K., Askanas V., Heppner F.L., Nilsson K.P. Luminescent conjugated oligothiophenes for sensitive fluorescent assignment of protein inclusion bodies. Chembiochem 2013, 14:607-616.
34. Oldfors A., Moslemi A.R., Jonasson L., Ohlsson M., Kollberg G., Lindberg C. Mitochondrial abnormalities in inclusion-body myositis. Neurology 2006, 66:S49-S55.
35. Weihl C.C., Temiz P., Miller S.E., Watts G., Smith C., Forman M., Hanson P.I., Kimonis V., Pestronk A. TDP-43 accumulation in inclusion body myopathy muscle suggests a common pathogenic mechanism with frontotemporal dementia. J. Neurol. Neurosurg. Psychiatry 2008, 79:1186-1189.
36. Olive M., Janue A., Moreno D., Gamez J., Torrejon-Escribano B., Ferrer I. TAR DNA-binding protein 43 accumulation in protein aggregate myopathies. J. Neuropathol. Exp. Neurol. 2009, 68:262-273.
37. D'Agostino C., Nogalska A., Engel W.K., Askanas V. In sporadic inclusion-body myositis muscle fibres TDP-43-positive inclusions are less frequent and robust than p62-inclusions, and are not associated with paired helical filaments. Neuropathol. Appl. Neurobiol. 2011, 37:315-320.
38. Martinez A., Portero-Otin M., Pamplona R., Ferrer I. Protein targets of oxidative damage in human neurodegenerative diseases with abnormal protein aggregates. Brain Pathol. 2010, 20:281-297.
39. Terracciano C., Nogalska A., Engel W.K., Wojcik S., Askanas V. In inclusion-body myositis muscle fibers Parkinson-associated DJ-1 is increased and oxidized. Free Radic. Biol. Med. 2008, 45:773-779.
40. Yang C.C., Alvarez R.B., Engel W.K., Askanas V. Increase of nitric oxide synthases and nitrotyrosine in inclusion-body myositis. Neuroreport 1996, 8:153-158.
41. Reynolds M.R., Berry R.W., Binder L.I. Site-specific nitration and oxidative dityrosine bridging of the tau protein by peroxynitrite: implications for Alzheimer's disease. Biochemistry 2005, 44:1690-1700.
42. Zhang Y.J., Xu Y.F., Chen X.Q., Wang X.C., Wang J.Z. Nitration and oligomerization of tau induced by peroxynitrite inhibit its microtubule-binding activity. FEBS Lett. 2005, 579:2421-2427.
43. Ciechanover A. Intracellular protein degradation: from a vague idea thru the lysosome and the ubiquitin-proteasome system and onto human diseases and drug targeting. Neurology 2006, 7-19.
44. Shacka J.J., Roth K.A., Zhang J. The autophagy-lysosomal degradation pathway: role in neurodegenerative disease and therapy. Front. Biosci. 2008, 13:718-736.
45. Cuervo A.M. Autophagy and aging: keeping that old broom working. Trends Genet. 2008, 24:604-612.
46. Douglas P.M., Dillin A. Protein homeostasis and aging in neurodegeneration. J. Cell Biol. 2010, 190:719-729.
47. Wolff S., Weissman J.S., Dillin A. Differential scales of protein quality control. Cell 2014, 157:52-64.
48. Sarkozi E., Askanas V., Johnson S.A., Engel W.K., Alvarez R.B. beta-Amyloid precursor protein mRNA is increased in inclusion-body myositis muscle. Neuroreport 1993, 4:815-818.
49. Tanaka S., Shiojiri S., Takahashi Y., Kitaguchi N., Ito H., Kameyama M., Kimura J., Nakamura S., Ueda K. Tissue-specific expression of three types of beta-protein precursor mRNA: enhancement of protease inhibitor-harboring types in Alzheimer's disease brain. Biochem. Biophys. Res. Commun. 1989, 165:1406-1414.
50. Terracciano C., Nogalska A., Engel W.K., Askanas V. In AbetaPP-overexpressing cultured human muscle fibers proteasome inhibition enhances phosphorylation of AbetaPP751 and GSK3beta activation: effects mitigated by lithium and apparently relevant to sporadic inclusion-body myositis. J. Neurochem. 2010, 112:389-396.
51. Nogalska A., Engel W.K., Askanas V. Increased BACE1 mRNA and noncoding BACE1-antisense transcript in sporadic inclusion-body myositis muscle fibers-possibly caused by endoplasmic reticulum stress. Neurosci. Lett. 2010, 474:140-143.
52. Sun X., Bromley-Brits K., Song W. Regulation of beta-site APP-cleaving enzyme 1 gene expression and its role in Alzheimer's disease. J. Neurochem. 2012, 120(Suppl. 1):62-70.
53. Faghihi M.A., Modarresi F., Khalil A.M., Wood D.E., Sahagan B.G., Morgan T.E., Finch C.E., St Laurent G., Kenny P.J., Wahlestedt C. Expression of a noncoding RNA is elevated in Alzheimer's disease and drives rapid feed-forward regulation of beta-secretase. Nat. Med. 2008, 14:723-730.
54. Cech T.R., Steitz J.A. The noncoding RNA revolution-trashing old rules to forge new ones. Cell 2014, 157:77-94.
55. Nogalska A., D'Agostino C., Engel W.K., Askanas V. Activation of the gamma-secretase complex and presence of gamma-secretase-activating protein may contribute to Abeta42 production in sporadic inclusion-body myositis muscle fibers. Neurobiol. Dis. 2012, 48:141-149.
56. De Strooper B., Annaert W. Novel research horizons for presenilins and gamma-secretases in cell biology and disease. Annu. Rev. Cell Dev. Biol. 2010, 26:235-260.
57. Askanas V., Alvarez R.B., Engel W.K. Beta-amyloid precursor epitopes in muscle fibers of inclusion body myositis. Ann. Neurol. 1993, 34:551-560.
58. Askanas V., Engel W.K., Alvarez R.B., Glenner G.G. beta-Amyloid protein immunoreactivity in muscle of patients with inclusion-body myositis. Lancet 1992, 339:560-561.
59. Askanas V., Engel W.K. Does overexpression of betaAPP in aging muscle have a pathogenic role and a relevance to Alzheimer's disease? Clues from inclusion body myositis, cultured human muscle, and transgenic mice. Am. J. Pathol. 1998, 153:1673-1677.
60. Selkoe D.J. Resolving controversies on the path to Alzheimer's therapeutics. Nat. Med. 2011, 17:1060-1065.
61. LaFerla F.M., Green K.N., Oddo S. Intracellular amyloid-beta in Alzheimer's disease. Nat. Rev. Neurosci. 2007, 8:499-509.
62. Larson M.E., Lesne S.E. Soluble Abeta oligomer production and toxicity. J. Neurochem. 2012, 120(Suppl. 1):125-139.
63. Vattemi G., Nogalska A., Engel W.K., D'Agostino C., Checler F., Askanas V. Amyloid-beta42 is preferentially accumulated in muscle fibers of patients with sporadic inclusion-body myositis. Acta Neuropathol. 2009, 117:569-574.
64. Cacciottolo M., Nogalska A., D'Agostino C., Engel W.K., Askanas V. Dysferlin is a newly identified binding partner of AβPP and it co-aggregates with amyloid-β42 within sporadic inclusion-body myositis (s-IBM) muscle fibers. Acta Neuropathol. 2013, 126:781-783.
65. Barthélémy F., Wein N., Krahn M., Lévy N., Bartoli M. Translational research and therapeutic perspectives in dysferlinopathies. Mol. Med. 2011, 17:875-882.
66. Nogalska A., D'Agostino C., Engel W.K., Klein W.L., Askanas V. Novel demonstration of amyloid-beta oligomers in sporadic inclusion-body myositis muscle fibers. Acta Neuropathol. 2010, 120:661-666.
67. Klein W.L., Stine W.B., Teplow D.B. Small assemblies of unmodified amyloid beta-protein are the proximate neurotoxin in Alzheimer's disease. Neurobiol. Aging 2004, 25:569-580.
68. Engel W.K., Trotter J.L. Plasma-cell dyscrasic amyloid neuropathy: A parasparafucile phenomenon?. Peroneal Atrophies and Related Disorders 1979, 333-338. Masson Publishing Co., New York. G. Serratrice, H. Roux (Eds.).
69. Honson N.S., Kuret J. Tau aggregation and toxicity in tauopathic neurodegenerative diseases. J. Alzheimers Dis. 2008, 14:417-422.
70. Iqbal K., Liu F., Gong C.X., Alonso Adel C., Grundke-Iqbal I. Mechanisms of tau-induced neurodegeneration. Acta Neuropathol. 2009, 118:53-69.
71. Mirabella M., Alvarez R.B., Bilak M., Engel W.K., Askanas V. Difference in expression of phosphorylated tau epitopes between sporadic inclusion-body myositis and hereditary inclusion-body myopathies. J. Neuropathol. Exp. Neurol. 1996, 55:774-786.
72. Nogalska A., Terracciano C., D'Agostino C., Engel W.K., Askanas V. p62/SQSTM1 is overexpressed and prominently accumulated in inclusions of sporadic inclusion-body myositis muscle fibers, and can help differentiating it from polymyositis and dermatomyositis. Acta Neuropathol. 2009, 118:407-413.
73. Jicha G.A., Lane E., Vincent I., Otvos L., Hoffmann R., Davies P. A conformation- and phosphorylation-dependent antibody recognizing the paired helical filaments of Alzheimer's disease. J. Neurochem. 1997, 69:2087-2095.
74. Nogalska A., D'Agostino C., Engel W.K., Askanas V. Novel demonstration of conformationally-modified tau in sporadic inclusion-body myositis muscle fibers. Neurosci. Lett. 2011, 503:229-233.
75. Kannanayakal T.J., Mendell J.R., Kuret J. Casein kinase 1 alpha associates with the tau-bearing lesions of inclusion body myositis. Neurosci. Lett. 2008, 431:141-145.
76. Broccolini A., Engel W.K., Alvarez R.B., Askanas V. Paired helical filaments of inclusion-body myositis muscle contain RNA and survival motor neuron protein. Am. J. Pathol. 2000, 156:1151-1155.
77. Spires-Jones T.L., Stoothoff W.H., de Calignon A., Jones P.B., Hyman B.T. Tau pathophysiology in neurodegeneration: a tangled issue. Trends Neurosci. 2009, 32:150-159.
78. Min S.W., Cho S.H., Zhou Y., Schroeder S., Haroutunian V., Seeley W.W., Huang E.J., Shen Y., Masliah E., Mukherjee C., Meyers D., Cole P.A., Ott M., Gan L. Acetylation of tau inhibits its degradation and contributes to tauopathy. Neuron 2010, 67:953-966.
79. Wang Y., Martinez-Vicente M., Kruger U., Kaushik S., Wong E., Mandelkow E.M., Cuervo A.M., Mandelkow E. Tau fragmentation, aggregation and clearance: the dual role of lysosomal processing. Hum. Mol. Genet. 2009, 18:4153-4170.
80. Fratta P., Engel W.K., McFerrin J., Davies K.J.A., Lin S.W., Askanas V. Proteasome inhibition and aggresome formation in sporadic inclusion-body myositis and in AbPP-overexpressing cultured human muscle fibers. Am. J. Pathol. 2005, 167:517-526.
81. Nogalska A., D'Agostino C., Terracciano C., Engel W.K., Askanas V. Impaired autophagy in sporadic inclusion-body myositis and in endoplasmic reticulum stress-provoked cultured human muscle fibers. Am. J. Pathol. 2010, 177:1377-1387.
82. Bloom G.S. Amyloid-beta and tau: the trigger and bullet in Alzheimer disease pathogenesis. JAMA Neurol. 2014, 71:505-508.
83. Gonzalez-Cadavid N.F., Bhasin S. Role of myostatin in metabolism. Curr. Opin. Clin. Nutr. Metab. Care 2004, 7:451-457.
84. Wojcik S., Engel W.K., McFerrin J., Askanas V. Myostatin is increased and complexes with amyloid-beta within sporadic inclusion-body myositis muscle fibers. Acta Neuropathol. 2005, 110:173-177.
85. Wojcik S., Nogalska A., McFerrin J., Engel W.K., Oledzka G., Askanas V. Myostatin precursor protein is increased and associates with amyloid-beta precursor protein in inclusion-body myositis culture model. Neuropathol. Appl. Neurobiol. 2007, 33:238-242.
86. Starck C.S., Sutherland-Smith A.J. Cytotoxic aggregation and amyloid formation by the myostatin precursor protein. PLoS ONE 2010, 5:e9170.
87. Crews L., Tsigelny I., Hashimoto M., Masliah E. Role of synucleins in Alzheimer's disease. Neurotox. Res. 2009, 16:306-317.
88. Devine M.J., Gwinn K., Singleton A., Hardy J. Parkinson's disease and alpha-synuclein expression. Mov. Disord. 2011, 26:2160-2168.
89. Askanas V., Engel W.K., Alvarez R.B., McFerrin J., Broccolini A. Novel immunolocalization of alpha-synuclein in human muscle of inclusion-body myositis, regenerating and necrotic muscle fibers, and at neuromuscular junctions. J. Neuropathol. Exp. Neurol. 2000, 59:592-598.
90. Paciello O., Wojcik S., Engel W.K., McFerrin J., Askanas V. Parkin and its association with alpha-synuclein and AbetaPP in inclusion-body myositis and AbetaPP-overexpressing cultured human muscle fibers. Acta Myol. 2006, 25:13-22.
91. Sridhar S., Botbol Y., Macian F., Cuervo A.M. Autophagy and disease: always two sides to a problem. J. Pathol. 2012, 226:255-273.
92. Cacciottolo M., Nogalska A., D'Agostino C., Engel W.K., Askanas V. Chaperone-mediated autophagy components are upregulated in sporadic inclusion-body myositis muscle fibres. Neuropathol. Appl. Neurobiol. 2013, 39:750-761.
93. Devi L., Anandatheerthavarada H.K. Mitochondrial trafficking of APP and alpha synuclein: relevance to mitochondrial dysfunction in Alzheimer's and Parkinson's diseases. Biochim. Biophys. Acta 2010, 1802:11-19.
94. Kawakami F., Suzuki M., Shimada N., Kagiya G., Ohta E., Tamura K., Maruyama H., Ichikawa T. Stimulatory effect of alpha-synuclein on the tau-phosphorylation by GSK-3beta. FEBS J. 2011, 278:4895-4904.
95. Nixon R.A., Yang D.S. Autophagy failure in Alzheimer's disease-locating the primary defect. Neurobiol. Dis. 2011, 43:38-45.
96. Fratta P., Engel W.K., Van Leeuwen F.W., Hol E.M., Vattemi G., Askanas V. Mutant ubiquitin UBB+1 is accumulated in sporadic inclusion-body myositis muscle fibers. Neurology 2004, 63:1114-1117.
97. Lehman N.L. The ubiquitin proteasome system in neuropathology. Acta Neuropathol. 2009, 118:329-347.
98. Nixon R.A. The role of autophagy in neurodegenerative disease. Nat. Med. 2013, 19:983-997.
99. Klionsky D.J., Codogno P. The mechanism and physiological function of macroautophagy. J. Innate. Immun. 2013, 5:427-433.
100. Hamano T., Gendron T.F., Causevic E., Yen S.H., Lin W.L., Isidoro C., Deture M., Ko L.W. Autophagic-lysosomal perturbation enhances tau aggregation in transfectants with induced wild-type tau expression. Eur. J. Neurosci. 2008, 27:1119-1130.
101. Mueller-Steiner S., Zhou Y., Arai H., Roberson E.D., Sun B., Chen J., Wang X., Yu G., Esposito L., Mucke L., Gan L. Antiamyloidogenic and neuroprotective functions of cathepsin B: implications for Alzheimer's disease. Neuron 2006, 51:703-714.
102. Yu W.H., Cuervo A.M., Kumar A., Peterhoff C.M., Schmidt S.D., Lee J.H., Mohan P.S., Mercken M., Farmery M.R., Tjernberg L.O., Jiang Y., Duff K., Uchiyama Y., Naslund J., Mathews P.M., Cataldo A.M., Nixon R.A. Macroautophagy-a novel beta-amyloid peptide-generating pathway activated in Alzheimer's disease. J. Cell Biol. 2005, 171:87-98.
103. Bjorkoy G., Lamark T., Brech A., Outzen H., Perander M., Overvatn A., Stenmark H., Johansen T. p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death. J. Cell Biol. 2005, 171:603-614.
104. Kirkin V., Lamark T., Sou Y.S., Bjorkoy G., Nunn J.L., Bruun J.A., Shvets E., McEwan D.G., Clausen T.H., Wild P., Bilusic I., Theurillat J.P., Overvatn A., Ishii T., Elazar Z., Komatsu M., Dikic I., Johansen T. A role for NBR1 in autophagosomal degradation of ubiquitinated substrates. Mol. Cell 2009, 33:505-516.
105. Seibenhener M.L., Babu J.R., Geetha T., Wong H.C., Krishna N.R., Wooten M.W. Sequestosome 1/p62 is a polyubiquitin chain binding protein involved in ubiquitin proteasome degradation. Mol. Cell. Biol. 2004, 24:8055-8068.
106. D'Agostino C., Nogalska A., Cacciottolo M., Engel W.K., Askanas V. Abnormalities of NBR1, a novel autophagy-associated protein, in muscle fibers of sporadic inclusion-body myositis. Acta Neuropathol. 2011, 122:627-636.
107. Kuusisto E., Salminen A., Alafuzoff I. Early accumulation of p62 in neurofibrillary tangles in Alzheimer's disease: possible role in tangle formation. Neuropathol. Appl. Neurobiol. 2002, 28:228-237.
108. Nicot A.S., Lo Verso F., Ratti F., Pilot-Storck F., Streichenberger N., Sandri M., Schaeffer L., Goillot E. Phosphorylation of NBR1 by GSK3 modulates protein aggregation. Autophagy 2014, 10:1036-1053.
109. Wilczynski G.M., Engel W.K., Askanas V. Association of active extracellular signal-regulated protein kinase with paired helical filaments of inclusion-body myositis muscle suggests its role in inclusion-body myositis tau phosphorylation. Am. J. Pathol. 2000, 156:1835-1840.
110. Engel W.K. "Ragged-red fibers" in opthamoplegia syndromes and their differential diagnosis. Excerpta Med. Int. Congr. Ser. 1971, 237.
111. Taira T., Saito Y., Niki T., Iguchi-Ariga S.M., Takahashi K., Ariga H. DJ-1 has a role in antioxidative stress to prevent cell death. EMBO Rep. 2004, 5:213-218.
112. Rygiel K.A., Miller J., Grady J.P., Rocha M.C., Taylor R.W., Turnbull D.M. Mitochondrial and inflammatory changes in sporadic inclusion body myositis. Neuropathol. Appl. Neurobiol. 2014, [Epub ahead of print]. 10.1111/nan.12149.
113. Terracciano C., Engel W., Askanas V. In sporadic inclusion-body myositis muscle biopsies, cytochrome oxidase (COX) negative muscle fibers do not correlate with either inflammation or with aggregates containing amyloid-beta or phosphorylated tau. Neurology 2008, 70:A304.
114. Thomas R.L., Gustafsson A.B. Mitochondrial autophagy-an essential quality control mechanism for myocardial homeostasis. Circ. J. 2013, 77:2449-2454.
115. Palikaras K., Tavernarakis N. Mitochondrial homeostasis: the interplay between mitophagy and mitochondrial biogenesis. Exp. Gerontol. 2014, 56:182-188.
116. Ashrafi G., Schwarz T.L. The pathways of mitophagy for quality control and clearance of mitochondria. Cell Death Differ. 2013, 20:31-42.
117. Ding W.-X., Yin X.-M. Mitophagy: mechanisms, pathophysiological roles, and analysis. Biol. Chem. 2012, 393:547-564.
118. Batlevi Y., La Spada A.R. Mitochondrial autophagy in neural function, neurodegenerative disease, neuron cell death, and aging. Neurobiol. Dis. 2011, 43:46-51.
119. Hanna R.A., Quinsay M.N., Orogo A.M., Giang K., Rikka S., Gustafsson A.B. Microtubule-associated protein 1 light chain 3 (LC3) interacts with Bnip3 protein to selectively remove endoplasmic reticulum and mitochondria via autophagy. J. Biol. Chem. 2012, 287:19094-19104.
120. Karbowski M., Neutzner A. Neurodegeneration as a consequence of failed mitochondrial maintenance. Acta Neuropathol. 2012, 123:157-171.
121. MacVicar T. Mitophagy. Essays Biochem. 2013, 55:93-104.
122. Nogalska A., D'Agostino C., Cacciottolo M., Engel W.K., Askanas V. Abnormalities of mitophagy in sporadic inclusion-body myositis (s-IBM) muscle fibers. Neurology 2014, 82:P3.288.
123. Yim N., Ryu S.-W., Han E.C., Yoon J., Choi K., Choi C. Mutant ubiquitin UBB+1 induces mitochondrial fusion by destabilizing mitochondrial fission-specific proteins and confers resistance to oxidative stress-induced cell death in astrocytic cells. PLoS ONE 2014, 9:e99937.
124. Jovaisaite V., Mouchiroud L., Auwerx J. The mitochondrial unfolded protein response, a conserved stress response pathway with implications in health and disease. J. Exp. Biol. 2014, 217:137-143.
125. Cuadrado-Tejedor M., Garcia-Osta A., Ricobaraza A., Oyarzabal J., Franco R. Defining the mechanism of action of 4-phenylbutyrate to develop a small-molecule-based therapy for Alzheimer's disease. Curr. Med. Chem. 2011, 18:5545-5553.
126. Iannitti T., Palmieri B. Clinical and experimental applications of sodium phenylbutyrate. Drugs R D 2011, 11:227-249.
127. Papp E., Csermely P. Chemical chaperones: mechanisms of action and potential use. Handb. Exp. Pharmacol. 2006, 405-416.
128. Nogalska A., D'Agostino C., Engel W.K., Askanas V. Sodium phenylbutyrate reverses lysosomal dysfunction and decreases amyloid-beta42 in an in vitro-model of inclusion-body myositis. Neurobiol. Dis. 2014, 65:93-101.
129. Yang D.S., Stavrides P., Mohan P.S., Kaushik S., Kumar A., Ohno M., Schmidt S.D., Wesson D.W., Bandyopadhyay U., Jiang Y., Pawlik M., Peterhoff C.M., Yang A.J., Wilson D.A., St George-Hyslop P., Westaway D., Mathews P.M., Levy E., Cuervo A.M., Nixon R.A. Therapeutic effects of remediating autophagy failure in a mouse model of Alzheimer disease by enhancing lysosomal proteolysis. Autophagy 2011, 7:788-789.
130. Engel T., Goni-Oliver P., Gomez de Barreda E., Lucas J.J., Hernandez F., Avila J. Lithium, a potential protective drug in Alzheimer's disease. Neurodegener. Dis. 2008, 5:247-249.
131. Kitazawa M., Trinh D.N., LaFerla F.M. Inflammation induces tau pathology in inclusion body myositis model via glycogen synthase kinase-3beta. Ann. Neurol. 2008, 64:15-24.
132. Cucciolla V., Borriello A., Oliva A., Galletti P., Zappia V., Della Ragione F. Resveratrol: from basic science to the clinic. Cell Cycle 2007, 6:2495-2510.
133. Nogalska A., D'Agostion C., Engel W.K., Askanas V. Resveratrol, a polyphenol found in red wine, reduces NF-kB-activation and myostatin in endoplasmic-reticulum-stress (ERS)-provoked cultured human muscle fibers (CHMFs): relevance to treatment of sporadic inclusion-body myositis (s-IBM). Ann. Neurol. 2008, 64:S9.
134. Hamaguchi T., Ono K., Murase A., Yamada M. Phenolic compounds prevent Alzheimer's pathology through different effects on the amyloid-beta aggregation pathway. Am. J. Pathol. 2009, 175:2557-2565.
135. Lannfelt L., Relkin N.R., Siemers E.R. Amyloid-β-directed immunotherapy for Alzheimer disease. J. Intern. Med. 2014, 275:284-294. (open).
136. Lambracht-Washington D., Rosenberg R. Anti-amyloid-beta to tau-based immunization: Developmetnin immunotherapy for Alzheimer disease. Immunotargets Ther. 2013, 2:105-114.
137. Willmijn Menting K., Claassen J.A.H.R. β-secretase inhibitor; a promising novel therapeutic drug in Alzheimer disease. Front. Aging Neurosci. 2014, 6:1-9.