Diagnostic value of markers of muscle degeneration in sporadic inclusion body myositis

Acta Myologica

Volumn 30, Issue OCTOBER, 2011, Pages 103-108

  Dubourg, Odile ^a   Wanschitz, J ^b   Maisonobe, T ^a   Behin A ^a   Allenbach, Y ^c   Herson, S ^c   Benveniste, O ^c  

^a PITIÉ SALPÊTRIÈRE HOSPITAL   (France)

^b INNSBRUCK MEDICAL UNIVERSITY   (Austria)

^c SORBONNE UNIVERSITÉ   (France)

Author keywords

Immunohistochemistry; Inclusion body myositis; Inflammatory myopathy; p62; Protein aggregate myopathy; Tar DNA binding protein 43

Indexed keywords

AMYLOID PRECURSOR PROTEIN; PROTEIN ANTIBODY; PROTEIN P62; TAR DNA BINDING PROTEIN; UBIQUITIN;

ARTICLE; CLINICAL ARTICLE; CLINICAL FEATURE; CONTROLLED STUDY; DIAGNOSTIC TEST ACCURACY STUDY; DIAGNOSTIC VALUE; DISEASE MARKER; FEMALE; HUMAN; HUMAN TISSUE; IMMUNOHISTOCHEMISTRY; INCLUSION BODY MYOSITIS; MALE; MUSCLE ATROPHY; MUSCLE BIOPSY; MUSCLE CELL; SENSITIVITY AND SPECIFICITY;

BIOLOGICAL MARKERS; BIOPSY; CYTOSKELETAL PROTEINS; DIAGNOSIS, DIFFERENTIAL; FEMALE; HUMANS; IMMUNOHISTOCHEMISTRY; INFLAMMATION; MALE; MIDDLE AGED; MUSCLE FIBERS, SKELETAL; MUSCULAR DYSTROPHIES; MYOSITIS, INCLUSION BODY; PATIENT SELECTION;

EID: 81455128284     PISSN: 11282460     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (26)

1. Griggs RC, Askanas V, DiMauro S, et al. Inclusion body myositis and myopathies. Ann Neurol 1995;38:705-13.
2. Askanas V, Engel 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.
3. Engel K, Askanas V. Inclusion-body myositis: Clinical, diagnostic, and pathologic aspects. Neurology 2006;66(2 Suppl 1):S20-9. (Pubitemid 43739980)
4. Dalakas MC. Sporadic inclusion body myositis - diagnosis, pathogenesis and therapeutic strategies. Nat Clin Pract Neurol 2006;2:437-47. (Pubitemid 44137945)
5. Greenberg SA. Inflammatory myopathies: evaluation and management. Semin Neurol 2008;28:241-9. (Pubitemid 351438984)
6. Chahin N, Engel AG. Correlation of muscle biopsy, clinical course, and outcome in PM and sporadic IBM. Neurology 2008;70;418-24.
7. Benveniste O, Hilton-Jones D. International workshop on inclusion body myositis held at the institute of Myology, Paris, on 29 May 2009. Neuromuscular Disord 2010;20:414-21.
8. Askanas V, Serdaroglu P, Engel WK, et al. Immunolocalization of ubiquitin in muscle biopsies of patients with inclusion body myositis and oculophayngal muscular dystrophy. Neurosci Lett 1991;130:73-6.
9. Askanas V, Engel WK, Alvarez RB. Light and electron microscopic localization of beta-amyloid protein in muscle biopsies of patients with inclusion-body myositis. Am J Pathol 1992;141:31-6.
10. Askanas V, Alvarez RB, Engel WK. Beta-amyloid precursor epitopes in muscle fibers of inclusion body myositis. Ann Neurol 1993;34:551-60. (Pubitemid 23289406)
11. Askanas V, Engel WK, Bilak M, et al. Twisted tubulofilaments of inclusion body myositis resemble paired helical filaments of Alzheimer brain and contain hyperphosphorylated tau. Am J Pathol 1994;144:177-87. (Pubitemid 24158371)
12. Askanas V, Mirabella M, Engel WK, et al. Apolipoprotein E immunoreactive deposits in inclusion-body. Lancet 1994;343:364-5.
13. Bilak M, Askanas V, Engel WK. Strong immunoreactivity of alpha 1-antichymotrypsin co-localizes with beta-amyloid protein and ubiquitin in vacuolated muscle fibers of inclusion-body myositis. Acta Neuropathol 1993;85:378-82. (Pubitemid 23100926)
14. rd AAN annual meeting, April 9-16, 2011, Honolulu, Hawaii, 055.P02.
15. Banwell BL, Engel AG. αB-Crystallin immunolocalization yields new insights into inclusion body myositis. Neurology 2000;54:1033-41. (Pubitemid 30151842)
16. Salajegheh M, Pinkus JL, Taylor JP, et al. Sarcoplasmic redistribution of nuclear TDP-43 in inclusion body myositis. Muscle Nerve 2009;40:19-31.
17. Mirabella M, Alvarez R, Bilak M, et al. Difference in expression of Phophorylated tau epitopes betwenne sporadic inclusion-body myositis and hereditary inclusion-body myopathies. J Neuropathol Exp Neurol 1996;55:774-86. (Pubitemid 26238580)
18. Van der Meulen MF, Hoogendijk JE, Moons KG, et al. Rimmed vacuoles and the added value of SMI-31 staining in diagnosing sporadic inclusion body myositis. Neuromuscul Disord 2001;11:447-51. (Pubitemid 32510004)
19. Kuusisto E, Salminen A, Alafuzoff I. Early accumulation of p62 in neurofibrillary tangles in Alzheimer's disease: possible role in tangle formation. Neuropathol Applied Neurobiol 2002;28:228-37. (Pubitemid 34639445)
20. Nogalska A, Terracciano C, D'Agostino C, et al. 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;118:407-13.
21. Olive M, Janue A, Moreno D, et al. TAR DNA-binding protein 43 accumulation in protein aggregate myopathies. J Neuropathol Exp Neurol 2009;68:262-73.
22. Goebel HH, Fardeau M, Olive M, et al. 156th ENMC International Workshop: Desmin and protein aggregate myopathies, 9-11 November 2007, Naarden, The Netherlands. Neuromuscul Disord 2008;18:583-92.
23. Weihl CC, Temiz P, Miller SE, et al. TDP-43 accumulation in inclusion body myopathy muscle suggests a common pathogenic mechanism with frontotemporal dementia. J Neurol Neurosurg Psychiatry 2008;79:1186-9.
24. Hernandez Lain A, Millecamps S, Dubourg O, et al. Abnormal TDP-43 and FUS proteins in muscles of sporadic IBM: similarities in a TARDBP-linked ALS patient. J Neurol Neurosurg Psychiatry 2010 (Epub ahead of print)
25. Buratti E, Baralle FE. Multiple role of TDP-43 in gene expression, splicing regulation, and human disease. Front Biosci 2008;13:867-78. (Pubitemid 351594732)
26. Neumann M, Sampathu DM, Kwong LK. Ubiquinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Science 2006;314:130-3. (Pubitemid 44547757)