Optineurin is potentially associated with TDP-43 and involved in the pathogenesis of inclusion body myositis

Neuropathology and Applied Neurobiology

Volumn 39, Issue 4, 2013, Pages 406-416

  Yamashita, S ^a   Kimura, E ^a   Tawara, N ^a   Sakaguchi, H ^a   Nakama, T ^a   Maeda, Y ^a   Hirano, T ^a   Uchino, M ^a   Ando, Y ^a  

^a KUMAMOTO UNIVERSITY   (Japan)

Author keywords

Amyotrophic lateral sclerosis; Cu Zn superoxide dismutase; Fused in sarcoma translocated in liposarcoma; Optineurin; Sporadic inclusion body myositis; TAR DNA binding protein 43

Indexed keywords

COPPER ZINC SUPEROXIDE DISMUTASE; FUSED IN SARCOMA PROTEIN; OPTINEURIN; PROTEIN P62; TAR DNA BINDING PROTEIN; TAU PROTEIN;

ADULT; AGED; ARTICLE; CLINICAL ARTICLE; CONFOCAL MICROSCOPY; CONTROLLED STUDY; CYTOPLASM; DERMATOMYOSITIS; ENZYME LOCALIZATION; FEMALE; HEREDITARY MOTOR SENSORY NEUROPATHY; HUMAN; HUMAN TISSUE; IMMUNOHISTOCHEMISTRY; INCLUSION BODY MYOSITIS; MALE; MUSCLE CELL; NEUROPATHOLOGY; OCULOPHARYNGEAL MUSCULAR DYSTROPHY; PATHOPHYSIOLOGY; POLYMYOSITIS; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN LOCALIZATION; PROTEIN PHOSPHORYLATION;

ADULT; AGED; AGED, 80 AND OVER; AMYOTROPHIC LATERAL SCLEROSIS; BIOPSY; DERMATOMYOSITIS; DNA-BINDING PROTEINS; FEMALE; HUMANS; IMMUNOHISTOCHEMISTRY; MALE; MIDDLE AGED; MUSCULAR ATROPHY; MUSCULAR DYSTROPHY, OCULOPHARYNGEAL; MYOSITIS, INCLUSION BODY; POLYMYOSITIS; RNA-BINDING PROTEIN FUS; SUPEROXIDE DISMUTASE; TDP-43 PROTEINOPATHIES; TRANSCRIPTION FACTOR TFIIIA;

EID: 84876874103     PISSN: 03051846     EISSN: 13652990     Source Type: Journal    
DOI: 10.1111/j.1365-2990.2012.01297.x     Document Type: Article

References (19)

1. Askanas V, Engel WK. 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: 583-95.
2. Askanas V, Engel WK, 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.
3. Dabby R, Lange DJ, Trojaborg W, Hays AP, Lovelace RE, Brannagan TH, Rowland LP. Inclusion body myositis mimicking motor neuron disease. Arch Neurol 2001; 58: 1253-6.
4. Weihl CC, Pestronk A. Sporadic inclusion body myositis: possible pathogenesis inferred from biomarkers. Curr Opin Neurol 2010; 23: 482-8.
5. Weihl CC, Temiz P, Miller SE, Watts G, Smith C, Forman M, Hanson PI, 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: 1186-9.
6. Salajegheh M, Pinkus JL, Taylor JP, Amato AA, Nazareno R, Baloh RH, Greenberg SA. Sarcoplasmic redistribution of nuclear TDP-43 in inclusion body myositis. Muscle Nerve 2009; 40: 19-31.
7. Olive M, Janue A, Moreno D, Gamez J, Torrejon-Escribano B, TAR FI. DNA-Binding protein 43 accumulation in protein aggregate myopathies. J Neuropathol Exp Neurol 2009; 68: 262-73.
8. Kusters B, van Hoeve BJ, Schelhaas HJ, Ter Laak H, van Engelen BG, Lammens M. TDP-43 accumulation is common in myopathies with rimmed vacuoles. Acta Neuropathol 2009; 117: 209-11.
9. Johnson JO, Mandrioli J, Benatar M, Abramzon Y, Van Deerlin VM, Trojanowski JQ, Gibbs JR, Brunetti M, Gronka S, Wuu J, Ding J, McCluskey L, Martinez-Lage M, Falcone D, Hernandez DG, Arepalli S, Chong S, Schymick JC, Rothstein J, Landi F, Wang YD, Calvo A, Mora G, Sabatelli M, Monsurro MR, Battistini S, Salvi F, Spataro R, Sola P, Borghero G, Galassi G, Scholz SW, Taylor JP, Restagno G, Chio A, Traynor BJ. Exome sequencing reveals VCP mutations as a cause of familial ALS. Neuron 2010; 68: 857-64.
10. Griggs RC, Askanas V, DiMauro S, Engel A, Karpati G, Mendell JR, Rowland LP. Inclusion body myositis and myopathies. Ann Neurol 1995; 38: 705-13.
11. Needham M, Mastaglia FL. Inclusion body myositis: current pathogenetic concepts and diagnostic and therapeutic approaches. Lancet Neurol 2007; 6: 620-31.
12. Dalakas MC. Review: an update on inflammatory and autoimmune myopathies. Neuropathol Appl Neurobiol 2010; 37: 226-42.
13. Brais B, Bouchard JP, Xie YG, Rochefort DL, Chretien N, Tome FM, Lafreniere RG, Rommens JM, Uyama E, Nohira O, Blumen S, Korczyn AD, Heutink P, Mathieu J, Duranceau A, Codere F, Fardeau M, Rouleau GA. Short GCG expansions in the PABP2 gene cause oculopharyngeal muscular dystrophy. Nat Genet 1998; 18: 164-7.
14. Neumann M, Mackenzie IR, Cairns NJ, Boyer PJ, Markesbery WR, Smith CD, Taylor JP, Kretzschmar HA, Kimonis VE, Forman MS. TDP-43 in the ubiquitin pathology of frontotemporal dementia with VCP gene mutations. J Neuropathol Exp Neurol 2007; 66: 152-7.
15. Maruyama H, Morino H, Ito H, Izumi Y, Kato H, Watanabe Y, Kinoshita Y, Kamada M, Nodera H, Suzuki H, Komure O, Matsuura S, Kobatake K, Morimoto N, Abe K, Suzuki N, Aoki M, Kawata A, Hirai T, Kato T, Ogasawara K, Hirano A, Takumi T, Kusaka H, Hagiwara K, Kaji R, Kawakami H. Mutations of optineurin in amyotrophic lateral sclerosis. Nature 2010; 465: 223-6.
16. Li Y, Kang J, Horwitz MS. Interaction of an adenovirus E3 14.7-kilodalton protein with a novel tumor necrosis factor alpha-inducible cellular protein containing leucine zipper domains. Mol Cell Biol 1998; 18: 1601-10.
17. Sahlender DA, Roberts RC, Arden SD, Spudich G, Taylor MJ, Luzio JP, Kendrick-Jones J, Buss F. Optineurin links myosin VI to the Golgi complex and is involved in Golgi organization and exocytosis. J Cell Biol 2005; 169: 285-95.
18. Guinto JB, Ritson GP, Taylor JP, Forman MS. Valosin-containing protein and the pathogenesis of frontotemporal dementia associated with inclusion body myopathy. Acta Neuropathol 2007; 114: 55-61.
19. Hernandez Lain A, Millecamps S, Dubourg O, Salachas F, Bruneteau G, Lacomblez L, Leguern E, Seilhean D, Duyckaerts C, Meininger V, Mallet J, Pradat PF. Abnormal TDP-43 and FUS proteins in muscles of sporadic IBM: similarities in a TARDBP-linked ALS patient. J Neurol Neurosurg Psychiatry 2011; 82: 1414-6.