eMedicine Specialties > Neurology > Neuromuscular Diseases

Inclusion Body Myositis: Multimedia

Author: Helen C Lin, MD, Assistant Professor of Neurology, Medical College of Wisconsin, Milwaukee
Coauthor(s): Paul E Barkhaus, MD, Professor, Department of Neurology, Medical College of Wisconsin; Director of Neuromuscular Diseases, Milwaukee Veterans Administration Medical Center; Michael P Collins, MD, Associate Professor, Department of Neurology, Medical College of Wisconsin; M Isabel Periquet Collins, MD, Assistant Professor, Department of Neurology, Medical College of Wisconsin
Contributor Information and Disclosures

Updated: Sep 3, 2009

Multimedia

Composite of 20 motor unit action potentials (MUA...
(Enlarge Image)
Media file 1: Composite of 20 motor unit action potentials (MUAPs) recorded with a concentric needle electrode from the biceps brachii of a patient with s-IBM. Note the wide range in size and complexity in the MUAPs. Copyright, Paul E Barkhaus, MD, 2000, with permission.
[ CLOSE WINDOW ]
Composite of 20 motor unit action potentials (MUA...

Composite of 20 motor unit action potentials (MUAPs) recorded with a concentric needle electrode from the biceps brachii of a patient with s-IBM. Note the wide range in size and complexity in the MUAPs. Copyright, Paul E Barkhaus, MD, 2000, with permission.

Top - A large, complex motor unit action potentia...
(Enlarge Image)
Media file 2: Top - A large, complex motor unit action potential (MUAP; 5 phases, approximately 2500 microV amplitude and 3 ms duration) firing at a progressively increasing rate (ie, shifting left) at about 13 Hz in apparent isolation. In normal muscle, other motor units typically would be recruited at this threshold (calibration 500 microV/division vertical; 10 ms/division horizontal). In the bottom trace the sensitivity is increased to 100 microV/division vertical (no change in horizontal time base), showing very small motor unit action potentials (MUAPs) in the baseline on either side of the large MUAP. This phenomenon may give rise to a mistaken "neurogenic" impression of the MUAP, as these small potentials are overlooked easily or mistaken for baseline noise or fibrillation potentials. Note also that despite the large amplitude of this MUAP, the spikes include essentially no area, giving them a needle-like appearance. Copyright, Paul E Barkhaus, MD, 2000, with permission.
[ CLOSE WINDOW ]
Top - A large, complex motor unit action potentia...

Top - A large, complex motor unit action potential (MUAP; 5 phases, approximately 2500 microV amplitude and 3 ms duration) firing at a progressively increasing rate (ie, shifting left) at about 13 Hz in apparent isolation. In normal muscle, other motor units typically would be recruited at this threshold (calibration 500 microV/division vertical; 10 ms/division horizontal). In the bottom trace the sensitivity is increased to 100 microV/division vertical (no change in horizontal time base), showing very small motor unit action potentials (MUAPs) in the baseline on either side of the large MUAP. This phenomenon may give rise to a mistaken "neurogenic" impression of the MUAP, as these small potentials are overlooked easily or mistaken for baseline noise or fibrillation potentials. Note also that despite the large amplitude of this MUAP, the spikes include essentially no area, giving them a needle-like appearance. Copyright, Paul E Barkhaus, MD, 2000, with permission.

On the left are 3 motor unit action potentials (M...
(Enlarge Image)
Media file 3: On the left are 3 motor unit action potentials (MUAPs) that have been "captured" from the same site and analyzed using a computer-assisted method. Note that the middle one has a satellite or "early" potential linked to it, characterized by the blackened/blurred area created by their superimposition to the left of the main portion of the MUAP. The reason for this is the increased variability in the interpotential interval on successive sweeps (ie, increased jitter). On the right, this middle MUAP is displayed in faster mode (9 sweeps). Note that on the fifth trace, the early component is absent, indicating a block. This shows the infrequent phenomenon in s-IBM of increased jitter and blocking, Copyright, Paul E Barkhaus, MD, 2000, with permission.
[ CLOSE WINDOW ]
On the left are 3 motor unit action potentials (M...

On the left are 3 motor unit action potentials (MUAPs) that have been "captured" from the same site and analyzed using a computer-assisted method. Note that the middle one has a satellite or "early" potential linked to it, characterized by the blackened/blurred area created by their superimposition to the left of the main portion of the MUAP. The reason for this is the increased variability in the interpotential interval on successive sweeps (ie, increased jitter). On the right, this middle MUAP is displayed in faster mode (9 sweeps). Note that on the fifth trace, the early component is absent, indicating a block. This shows the infrequent phenomenon in s-IBM of increased jitter and blocking, Copyright, Paul E Barkhaus, MD, 2000, with permission.

Interference pattern in biceps brachii. Top trace...
(Enlarge Image)
Media file 4: Interference pattern in biceps brachii. Top trace - Normal interference pattern at full effort (calibration - 500 microV/division vertical; 1 s/division horizontal). The middle trace is an interference pattern from a patient with severe s-IBM (calibration - 100 microV/division vertical; 1 s/division horizontal). This epoch of signal actually shows the patient going from minimal activation at the left (beginning of the sweep) to full effort on the far right. The "notch" just to the right of the second division mark shows a baseline shift from needle electrode movement. Overall, no amplitude change of "fullness" is seen going from minimal to full effort, and the amplitude of the signal epoch is less than half of what might be expected in normal muscle. The bottom trace is an expanded segment showing interference pattern from biceps brachii; this trace is from a patient with advanced s-IBM (calibration - 100 microV/division vertical; 10 ms/division horizontal), from the early or far left portion of the middle sweep (see "H" bar position between the middle and lower sweeps). This shows a relatively full baseline of small-amplitude, complex motor unit action potentials (MUAPs). Copyright, Paul E Barkhaus, MD, 2000, with permission.
[ CLOSE WINDOW ]
Interference pattern in biceps brachii. Top trace...

Interference pattern in biceps brachii. Top trace - Normal interference pattern at full effort (calibration - 500 microV/division vertical; 1 s/division horizontal). The middle trace is an interference pattern from a patient with severe s-IBM (calibration - 100 microV/division vertical; 1 s/division horizontal). This epoch of signal actually shows the patient going from minimal activation at the left (beginning of the sweep) to full effort on the far right. The "notch" just to the right of the second division mark shows a baseline shift from needle electrode movement. Overall, no amplitude change of "fullness" is seen going from minimal to full effort, and the amplitude of the signal epoch is less than half of what might be expected in normal muscle. The bottom trace is an expanded segment showing interference pattern from biceps brachii; this trace is from a patient with advanced s-IBM (calibration - 100 microV/division vertical; 10 ms/division horizontal), from the early or far left portion of the middle sweep (see "H" bar position between the middle and lower sweeps). This shows a relatively full baseline of small-amplitude, complex motor unit action potentials (MUAPs). Copyright, Paul E Barkhaus, MD, 2000, with permission.

Modified Gomori trichrome stained section showing...
(Enlarge Image)
Media file 5: Modified Gomori trichrome stained section showing (1) 2 muscle fibers (MFs) containing intracytoplasmic vacuoles (open arrows) and (2) mononuclear inflammatory infiltrates invading a nonnecrotic MF (solid arrow). Copyright, Isabel P Collins, MD, 2000, with permission.
[ CLOSE WINDOW ]
Modified Gomori trichrome stained section showing...

Modified Gomori trichrome stained section showing (1) 2 muscle fibers (MFs) containing intracytoplasmic vacuoles (open arrows) and (2) mononuclear inflammatory infiltrates invading a nonnecrotic MF (solid arrow). Copyright, Isabel P Collins, MD, 2000, with permission.

Congo red-stained section showing apple green bir...
(Enlarge Image)
Media file 6: Congo red-stained section showing apple green birefringent amyloid deposits within muscle fibers (MFs) (arrow). The MF on the right side of the section is focally surrounded and invaded by inflammatory cells. Courtesy of Jerry R Mendell, MD.
[ CLOSE WINDOW ]
Congo red-stained section showing apple green bir...

Congo red-stained section showing apple green birefringent amyloid deposits within muscle fibers (MFs) (arrow). The MF on the right side of the section is focally surrounded and invaded by inflammatory cells. Courtesy of Jerry R Mendell, MD.

Electron micrograph showing characteristic 15-to1...
(Enlarge Image)
Media file 7: Electron micrograph showing characteristic 15-to18-nm tubulofilaments (arrow). Copyright, Isabel P Collins, MD, 2000, with permission.
[ CLOSE WINDOW ]
Electron micrograph showing characteristic 15-to1...

Electron micrograph showing characteristic 15-to18-nm tubulofilaments (arrow). Copyright, Isabel P Collins, MD, 2000, with permission.

More on Inclusion Body Myositis

Overview: Inclusion Body Myositis
Differential Diagnoses & Workup: Inclusion Body Myositis
Treatment & Medication: Inclusion Body Myositis
Follow-up: Inclusion Body Myositis
Multimedia: Inclusion Body Myositis
References
[ CLOSE WINDOW ]

References

  1. Argov Z. Hereditary inclusion body myopathies. In: Engel AG, Franzini-Armstrong C, eds. Myology. 3rd ed. New York: McGraw Hill;2004:1311-1320.

  2. Malicdan MC, Noguchi S, Nishino I. Recent advances in distal myopathy with rimmed vacuoles (DMRV) or hIBM: treatment perspectives. Curr Opin Neurol. Oct 2008;21(5):596-600. [Medline].

  3. Karpati G, O'Ferrall EK. Sporadic inclusion body myositis: pathogenic considerations. Ann Neurol. Jan 2009;65(1):7-11. [Medline].

  4. Pruitt JN, Showalter CJ, Engel AG. Sporadic inclusion body myositis: counts of different types of abnormal fibers. Ann Neurol. Jan 1996;39(1):139-43. [Medline].

  5. Engel AG, Arahata K. Monoclonal antibody analysis of mononuclear cells in myopathies. II: Phenotypes of autoinvasive cells in polymyositis and inclusion body myositis. Ann Neurol. Aug 1984;16(2):209-15. [Medline].

  6. Greenberg SA, Bradshaw EM, Pinkus JL, Pinkus GS, Burleson T, Due B. Plasma cells in muscle in inclusion body myositis and polymyositis. Neurology. Dec 13 2005;65(11):1782-7. [Medline].

  7. Greenberg SA, Pinkus GS, Amato AA, Pinkus JL. Myeloid dendritic cells in inclusion-body myositis and polymyositis. Muscle Nerve. Jan 2007;35(1):17-23. [Medline].

  8. Tateyama M, Fujihara K, Misu T, Itoyama Y. CCR7+ myeloid dendritic cells together with CCR7+ T cells and CCR7+ macrophages invade CCL19+ nonnecrotic muscle fibers in inclusion body myositis. J Neurol Sci. Apr 15 2009;279(1-2):47-52. [Medline].

  9. Arahata K, Engel AG. Monoclonal antibody analysis of mononuclear cells in myopathies. V: Identification and quantitation of T8+ cytotoxic and T8+ suppressor cells. Ann Neurol. May 1988;23(5):493-9. [Medline].

  10. Orimo S, Koga R, Goto K, et al. Immunohistochemical analysis of perforin and granzyme A in inflammatory myopathies. Neuromuscul Disord. May 1994;4(3):219-26. [Medline].

  11. Schmidt J, Barthel K, Wrede A, Salajegheh M, Bähr M, Dalakas MC. Interrelation of inflammation and APP in sIBM: IL-1 beta induces accumulation of beta-amyloid in skeletal muscle. Brain. May 2008;131(Pt 5):1228-40. [Medline].

  12. Amemiya K, Granger RP, Dalakas MC. Clonal restriction of T-cell receptor expression by infiltrating lymphocytes in inclusion body myositis persists over time. Studies in repeated muscle biopsies. Brain. Oct 2000;123 (Pt 10):2030-9. [Medline].

  13. Muntzing K, Lindberg C, Moslemi AR, Oldfors A. Inclusion body myositis: clonal expansions of muscle-infiltrating T cells persist over time. Scand J Immunol. Aug 2003;58(2):195-200. [Medline].

  14. Salajegheh M, Rakocevic G, Raju R, Shatunov A, Goldfarb LG, Dalakas MC. T cell receptor profiling in muscle and blood lymphocytes in sporadic inclusion body myositis. Neurology. Oct 23 2007;69(17):1672-9. [Medline].

  15. De Paepe B, Creus KK, De Bleecker JL. Chemokine profile of different inflammatory myopathies reflects humoral versus cytotoxic immune responses. Ann N Y Acad Sci. Aug 2007;1109:441-53. [Medline].

  16. Greenberg SA, Sanoudou D, Haslett JN, et al. Molecular profiles of inflammatory myopathies. Neurology. Oct 22 2002;59(8):1170-82. [Medline].

  17. Raju R, Dalakas MC. Gene expression profile in the muscles of patients with inflammatory myopathies: effect of therapy with IVIg and biological validation of clinically relevant genes. Brain. Aug 2005;128(Pt 8):1887-96. [Medline].

  18. Bradshaw EM, Orihuela A, McArdel SL, Salajegheh M, Amato AA, Hafler DA, et al. A local antigen-driven humoral response is present in the inflammatory myopathies. J Immunol. Jan 1 2007;178(1):547-56. [Medline].

  19. Koffman BM, Rugiero M, Dalakas MC. Immune-mediated conditions and antibodies associated with sporadic inclusion body myositis. Muscle Nerve. Jan 1998;21(1):115-7. [Medline].

  20. Badrising UA, Schreuder GM, Giphart MJ, et al. Associations with autoimmune disorders and HLA class I and II antigens in inclusion body myositis. Neurology. Dec 28 2004;63(12):2396-8. [Medline].

  21. Dalakas MC, Illa I, Gallardo E, Juarez C. Inclusion body myositis and paraproteinemia: incidence and immunopathologic correlations. Ann Neurol. Jan 1997;41(1):100-4. [Medline].

  22. Cupler EJ, Leon-Monzon M, Miller J, et al. Inclusion body myositis in HIV-1 and HTLV-1 infected patients. Brain. Dec 1996;119 (Pt 6):1887-93. [Medline].

  23. Tsuruta Y, Furuta A, Furuta K, Yamada T, Kira J, Iwaki T. Expression of the lysosome-associated membrane proteins in myopathies with rimmed vacuoles. Acta Neuropathol. Jun 2001;101(6):579-84. [Medline].

  24. Dalakas MC. Inflammatory, immune, and viral aspects of inclusion-body myositis. Neurology. Jan 24 2006;66(2 Suppl 1):S33-8. [Medline].

  25. Matsuura E, Umehara F, Nose H, Higuchi I, Matsuoka E, Izumi K. Inclusion body myositis associated with human T-lymphotropic virus-type I infection: eleven patients from an endemic area in Japan. J Neuropathol Exp Neurol. Jan 2008;67(1):41-9. [Medline].

  26. Carpenter S. Inclusion body myositis, a review. J Neuropathol Exp Neurol. Nov 1996;55(11):1105-14. [Medline].

  27. Karpati G, Pouliot Y, Carpenter S. Expression of immunoreactive major histocompatibility complex products in human skeletal muscles. Ann Neurol. Jan 1988;23(1):64-72. [Medline].

  28. Mikol J, Engel AG. Inclusion body myositis. In: Engel AG, Franzini-Armstrong C, eds. Myology. 3rd ed. NY: McGraw Hill;2004: 1367-1388.

  29. 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. Jul 2009;19(3):493-506. [Medline].

  30. Lee C, Yu MH. Protein folding and diseases. J Biochem Mol Biol. May 31 2005;38(3):275-80. [Medline].

  31. Ciechanover A. The ubiquitin proteolytic system: from a vague idea, through basic mechanisms, and onto human diseases and drug targeting. Neurology. Jan 24 2006;66(2 Suppl 1):S7-19. [Medline].

  32. Jayaraman M, Kannayiram G, Rajadas J. Amyloid toxicity in skeletal myoblasts: Implications for inclusion-body myositis. Arch Biochem Biophys. Jun 1 2008;474(1):15-21. [Medline].

  33. Glabe CG, Kayed R. Common structure and toxic function of amyloid oligomers implies a common mechanism of pathogenesis. Neurology. Jan 24 2006;66(2 Suppl 1):S74-8. [Medline].

  34. Vattemi G, Engel WK, McFerrin J, et al. BACE1 and BACE2 in pathologic and normal human muscle. Exp Neurol. Feb 2003;179(2):150-8. [Medline].

  35. 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. Dec 2008;116(6):583-95. [Medline].

  36. Vattemi G, Nogalska A, King Engel W, D'Agostino C, Checler F, Askanas V. Amyloid-beta42 is preferentially accumulated in muscle fibers of patients with sporadic inclusion-body myositis. Acta Neuropathol. May 2009;117(5):569-74. [Medline].

  37. Greenberg SA. Comment on 'Interrelation of inflammation and APP in sIBM: IL-1beta induces accumulation of beta-amyloid in skeletal muscle'. Brain. Apr 2009;132(Pt 4):e106; author reply e107. [Medline].

  38. Mori K. Tripartite management of unfolded proteins in the endoplasmic reticulum. Cell. May 26 2000;101(5):451-4. [Medline].

  39. Zhang K, Kaufman RJ. Protein folding in the endoplasmic reticulum and the unfolded protein response. Handb Exp Pharmacol. 2006;69-91. [Medline].

  40. Vattemi G, Engel WK, McFerrin J, Askanas V. Endoplasmic reticulum stress and unfolded protein response in inclusion body myositis muscle. Am J Pathol. Jan 2004;164(1):1-7. [Medline].

  41. Nakano S, Akiguchi I, Nakamura S, et al. Aberrant expression of cyclin-dependent kinase 5 in inclusion body myositis. Neurology. Nov 10 1999;53(8):1671-6. [Medline].

  42. Kitazawa M, Trinh DN, LaFerla FM. Inflammation induces tau pathology in inclusion body myositis model via glycogen synthase kinase-3beta. Ann Neurol. Jul 2008;64(1):15-24. [Medline].

  43. Kumamoto T, Ueyama H, Tsumura H, et al. Expression of lysosome-related proteins and genes in the skeletal muscles of inclusion body myositis. Acta Neuropathol (Berl). Jan 2004;107(1):59-65. [Medline].

  44. Lunemann JD, Schmidt J, Schmid D, Barthel K, Wrede A, Dalakas MC. Beta-amyloid is a substrate of autophagy in sporadic inclusion body myositis. Ann Neurol. May 2007;61(5):476-83. [Medline].

  45. Greenberg SA, Pinkus JL, Amato AA. Nuclear membrane proteins are present within rimmed vacuoles in inclusion-body myositis. Muscle Nerve. Oct 2006;34(4):406-16. [Medline].

  46. Nalbantoglu J, Karpati G, Carpenter S. Conspicuous accumulation of a single-stranded DNA binding protein in skeletal muscle fibers in inclusion body myositis. Am J Pathol. May 1994;144(5):874-82. [Medline].

  47. Nakano S, Shinde A, Fujita K, Ito H, Kusaka H. Histone H1 is released from myonuclei and present in rimmed vacuoles with DNA in inclusion body myositis. Neuromuscul Disord. Jan 2008;18(1):27-33. [Medline].

  48. Santorelli FM, Sciacco M, Tanji K, et al. Multiple mitochondrial DNA deletions in sporadic inclusion body myositis: a study of 56 patients. Ann Neurol. Jun 1996;39(6):789-95. [Medline].

  49. Horvath R, Fu K, Johns T, Genge A, Karpati G, Shoubridge EA. Characterization of the mitochondrial DNA abnormalities in the skeletal muscle of patients with inclusion body myositis. J Neuropathol Exp Neurol. May 1998;57(5):396-403. [Medline].

  50. Oldfors A, Moslemi AR, Jonasson L, Ohlsson M, Kollberg G, Lindberg C. Mitochondrial abnormalities in inclusion-body myositis. Neurology. Jan 24 2006;66(2 Suppl 1):S49-55. [Medline].

  51. Askanas V, McFerrin J, Baqué S, Alvarez RB, Sarkozi E, Engel WK. Transfer of beta-amyloid precursor protein gene using adenovirus vector causes mitochondrial abnormalities in cultured normal human muscle. Proc Natl Acad Sci U S A. Feb 6 1996;93(3):1314-9. [Medline].

  52. Dalakas MC. Molecular immunology and genetics of inflammatory muscle diseases. Arch Neurol. Dec 1998;55(12):1509-12. [Medline].

  53. Parker KC, Kong SW, Walsh RJ, Salajegheh M, Moghadaszadeh B, Amato AA, et al. Fast-twitch sarcomeric and glycolytic enzyme protein loss in inclusion body myositis. Muscle Nerve. Jun 2009;39(6):739-53. [Medline].

  54. Ferrer I, Martin B, Castano JG. Proteasomal expression, induction of immunoproteasome subunits, and local MHC class I presentation in myofibrillar myopathy and inclusion body myositis. J Neuropathol Exp Neurol. May 2004;63(5):484-98. [Medline].

  55. Dahlmann B. Proteasomes. Essays Biochem. 2005;41:31-48. [Medline].

  56. Lunemann JD, Munz C. Autophagy in CD4+ T-cell immunity and tolerance. Cell Death Differ. Jan 2009;16(1):79-86. [Medline].

  57. Zhang K, Kaufman RJ. From endoplasmic-reticulum stress to the inflammatory response. Nature. Jul 24 2008;454(7203):455-62. [Medline].

  58. Dalakas MC. Interplay between inflammation and degeneration: using inclusion body myositis to study "neuroinflammation". Ann Neurol. Jul 2008;64(1):1-3. [Medline].

  59. Banwell BL, Engel AG. AlphaB-crystallin immunolocalization yields new insights into inclusion body myositis. Neurology. Mar 14 2000;54(5):1033-41. [Medline].

  60. Badrising UA, Maat-Schieman M, van Duinen SG, et al. Epidemiology of inclusion body myositis in the Netherlands: a nationwide study. Neurology. Nov 14 2000;55(9):1385-7. [Medline].

  61. Phillips BA, Zilko PJ, Mastaglia FL. Prevalence of sporadic inclusion body myositis in Western Australia. Muscle Nerve. Jun 2000;23(6):970-2. [Medline].

  62. Shamim EA, Rider LG, Pandey JP, O'Hanlon TP, Jara LJ, Samayoa EA. Differences in idiopathic inflammatory myopathy phenotypes and genotypes between Mesoamerican Mestizos and North American Caucasians: ethnogeographic influences in the genetics and clinical expression of myositis. Arthritis Rheum. Jul 2002;46(7):1885-93. [Medline].

  63. Lotz BP, Engel AG, Nishino H, et al. Inclusion body myositis. Observations in 40 patients. Brain. Jun 1989;112 (Pt 3):727-47. [Medline].

  64. Lindberg C, Persson LI, Bjorkander J, Oldfors A. Inclusion body myositis: clinical, morphological, physiological and laboratory findings in 18 cases. Acta Neurol Scand. Feb 1994;89(2):123-31. [Medline].

  65. Beyenburg S, Zierz S, Jerusalem F. Inclusion body myositis: clinical and histopathological features of 36 patients. Clin Investig. May 1993;71(5):351-61. [Medline].

  66. Sayers ME, Chou SM, Calabrese LH. Inclusion body myositis: analysis of 32 cases. J Rheumatol. Sep 1992;19(9):1385-9. [Medline].

  67. Badrising UA, Maat-Schieman ML, van Houwelingen JC, et al. Inclusion body myositis. Clinical features and clinical course of the disease in 64 patients. J Neurol. Dec 2005;252(12):1448-54. [Medline].

  68. Hund E, Heckl R, Goebel HH, Meinck HM. Inclusion body myositis presenting with isolated erector spinae paresis. Neurology. May 1995;45(5):993-4. [Medline].

  69. Kraemer P, Sagui E, Brosset C, et al. [Inclusion myositis associated with primary biliary cirrhosis of the liver]. Presse Med. Mar 15 2003;32(10):460. [Medline].

  70. Kanellopoulos P, Baltoyiannis C, Tzioufas AG. Primary Sjogren's syndrome associated with inclusion body myositis. Rheumatology (Oxford). Apr 2002;41(4):440-4. [Medline].

  71. Williams SF, Mincey BA, Calamia KT. Inclusion body myositis associated with celiac sprue and idiopathic thrombocytopenic purpura. South Med J. Jul 2003;96(7):721-3. [Medline].

  72. Cherin P, Menard D, Mouton P, et al. Macrophagic myofasciitis associated with inclusion body myositis: a report of three cases. Neuromuscul Disord. Jul 2001;11(5):452-7. [Medline].

  73. Wenzel J, Uerlich M, Gerdsen R, et al. Association of inclusion body myositis with subacute cutaneous lupus erythematosus. Rheumatol Int. Oct 2001;21(2):75-7. [Medline].

  74. Derk CT, Vivino FB, Kenyon L, Mandel S. Inclusion body myositis in connective tissue disorders: case report and review of the literature. Clin Rheumatol. Oct 2003;22(4-5):324-8. [Medline].

  75. Massawi G, Hickling P, Hilton D, Patterson C. Inclusion body myositis evolving in systemic lupus erythematosus? A case report. Rheumatology (Oxford). Aug 2003;42(8):1012-4. [Medline].

  76. Kovacs GG, Lindeck-Pozza E, Chimelli L, et al. Creutzfeldt-Jakob disease and inclusion body myositis: abundant disease-associated prion protein in muscle. Ann Neurol. Jan 2004;55(1):121-5. [Medline].

  77. Arnardottir S, Ansved T, Nennesmo I, Borg K. Report of a patient with inclusion body myositis and CD8+ chronic lymphocytic leukaemia--post-mortem analysis of muscle and brain. Acta Neurol Scand. Feb 2001;103(2):131-5. [Medline].

  78. Hengstman GJ, Brouwer R, Egberts WT, et al. Clinical and serological characteristics of 125 Dutch myositis patients. Myositis specific autoantibodies aid in the differential diagnosis of the idiopathic inflammatory myopathies. J Neurol. Jan 2002;249(1):69-75. [Medline].

  79. Sekul EA, Chow C, Dalakas MC. Magnetic resonance imaging of the forearm as a diagnostic aid in patients with sporadic inclusion body myositis. Neurology. Apr 1997;48(4):863-6. [Medline].

  80. Phillips BA, Cala LA, Thickbroom GW. Patterns of muscle involvement in inclusion body myositis: clinical and magnetic resonance imaging study. Muscle Nerve. Nov 2001;24(11):1526-34. [Medline].

  81. Arnardottir S, Svanborg E, Borg K. Inclusion body myositis--sensory dysfunction revealed with quantitative determination of somatosensory thresholds. Acta Neurol Scand. Jul 2003;108(1):22-7. [Medline].

  82. Mendell JR, Sahenk Z, Gales T, Paul L. Amyloid filaments in inclusion body myositis. Novel findings provide insight into nature of filaments. Arch Neurol. Dec 1991;48(12):1229-34. [Medline].

  83. Griggs RC, Askanas V, DiMauro S, et al. Inclusion body myositis and myopathies. Ann Neurol. Nov 1995;38(5):705-13. [Medline].

  84. Salajegheh M, Pinkus JL, Taylor JP, Amato AA, Nazareno R, Baloh RH, et al. Sarcoplasmic redistribution of nuclear TDP-43 in inclusion body myositis. Muscle Nerve. Jul 2009;40(1):19-31. [Medline].

  85. Barohn RJ, Amato AA, Sahenk Z, et al. Inclusion body myositis: explanation for poor response to immunosuppressive therapy. Neurology. Jul 1995;45(7):1302-4. [Medline].

  86. Rutkove SB, Parker RA, Nardin RA, et al. A pilot randomized trial of oxandrolone in inclusion body myositis. Neurology. Apr 9 2002;58(7):1081-7. [Medline].

  87. Badrising UA, Maat-Schieman ML, Ferrari MD, et al. Comparison of weakness progression in inclusion body myositis during treatment with methotrexate or placebo. Ann Neurol. Mar 2002;51(3):369-72. [Medline].

  88. Soueidan SA, Dalakas MC. Treatment of inclusion-body myositis with high-dose intravenous immunoglobulin. Neurology. May 1993;43(5):876-9. [Medline].

  89. Amato AA, Barohn RJ, Jackson CE, et al. Inclusion body myositis: treatment with intravenous immunoglobulin. Neurology. Aug 1994;44(8):1516-8. [Medline].

  90. Walter MC, Lochmuller H, Toepfer M, et al. High-dose immunoglobulin therapy in sporadic inclusion body myositis: a double-blind, placebo-controlled study. J Neurol. Jan 2000;247(1):22-8. [Medline].

  91. Cherin P, Pelletier S, Teixeira A, et al. Intravenous immunoglobulin for dysphagia of inclusion body myositis. Neurology. Jan 22 2002;58(2):326. [Medline].

  92. Dalakas MC, Somies B, Dambrosia J, et al. Treatment of inclusion-body myositis with IVIg: A double blind, placebo-controlled study. Neurology. 1997;48:712-716. [Medline].

  93. Dalakas MC, Koffman B, Fujii M, et al. A controlled study of intravenous immunoglobulin combined with prednisone in the treatment of IBM. Neurology. Feb 13 2001;56(3):323-7. [Medline].

  94. Lindberg C, Trysberg E, Tarkowski A, Oldfors A. Anti-T-lymphocyte globulin treatment in inclusion body myositis: a randomized pilot study. Neurology. Jul 22 2003;61(2):260-2. [Medline].

  95. Muscle Study Group. Randomized pilot trial of betaINF1a (Avonex) in patients with inclusion body myositis. Neurology. Nov 13 2001;57(9):1566-70. [Medline].

  96. Muscle Study Group. Randomized pilot trial of high-dose betaINF-1a in patients with inclusion body myositis. Neurology. Aug 24 2004;63(4):718-20. [Medline].

  97. Barohn RJ, Herbelin L, Kissel JT, King W, McVey AL, Saperstein DS. Pilot trial of etanercept in the treatment of inclusion-body myositis. Neurology. Jan 24 2006;66(2 Suppl 1):S123-4. [Medline].

  98. Dalakas MC, Rakocevic G, Schmidt J, Salajegheh M, McElroy B, Harris-Love MO. Effect of Alemtuzumab (CAMPATH 1-H) in patients with inclusion-body myositis. Brain. Jun 2009;132(Pt 6):1536-44. [Medline].

  99. Rodino-Klapac LR, Haidet AM, Kota J, Handy C, Kaspar BK, Mendell JR. Inhibition of myostatin with emphasis on follistatin as a therapy for muscle disease. Muscle Nerve. Mar 2009;39(3):283-96. [Medline].

  100. Hicks J. Comprehensive rehabilitative management of patients with polymyositis and dermatomyositis. In: Dalakas M, ed. Polymyositis and Dermatomyositis. Boston, Mass: Butterworth-Heinemann; 1988:293-318.

  101. Liu LW, Tarnopolsky M, Armstrong D. Injection of botulinum toxin A to the upper esophageal sphincter for oropharyngeal dysphagia in two patients with inclusion body myositis. Can J Gastroenterol. Jun 2004;18(6):397-9. [Medline].

  102. Spector SA, Lemmer JT, Koffman BM, et al. Safety and efficacy of strength training in patients with sporadic inclusion body myositis. Muscle Nerve. Oct 1997;20(10):1242-8. [Medline].

  103. Johnson LG, Collier KE, Edwards DJ, Philippe DL, Eastwood PR, Walters SE, et al. Improvement in aerobic capacity after an exercise program in sporadic inclusion body myositis. J Clin Neuromuscul Dis. Jun 2009;10(4):178-84. [Medline].

  104. Rose MR, McDermott MP, Thornton CA, et al. A prospective natural history study of inclusion body myositis: implications for clinical trials. Neurology. Aug 14 2001;57(3):548-50. [Medline].

  105. Peng A, Koffman BM, Malley JD, Dalakas MC. Disease progression in sporadic inclusion body myositis: observations in 78 patients. Neurology. Jul 25 2000;55(2):296-8. [Medline].

  106. Amato AA, Gronseth GS, Jackson CE, et al. Inclusion body myositis: clinical and pathological boundaries. Ann Neurol. Oct 1996;40(4):581-6. [Medline].

  107. Askanas V. 1996.

  108. Askanas V, Engel WK. Inclusion-body myositis: a myodegenerative conformational disorder associated with Abeta, protein misfolding, and proteasome inhibition. Neurology. Jan 24 2006;66(2 Suppl 1):S39-48. [Medline].

  109. Askanas V, Engel WK. New advances in the understanding of sporadic inclusion-body myositis and hereditary inclusion-body myopathies. Curr Opin Rheumatol. Nov 1995;7(6):486-96. [Medline].

  110. Askanas V, Engel WK, McFerrin J, et al. Transthyretin Val122Ile, accumulated Abeta, and inclusion-body myositis aspects in cultured muscle. Neurology. Jul 22 2003;61(2):257-60. [Medline].

  111. Barkhaus PE. The electrodiagnostic evaluation of the patient with suspected myopathy. In Kincaid JC, ed. The Young, the Old, and the Weak: A Basic Course in Electrodiagnostic Medicine. Rochester, MN: American Association of Electrodiagnostic Medicine;1998.

  112. Barkhaus PE, Periquet MI, Nandedkar SD. Quantitative electrophysiologic studies in sporadic inclusion body myositis. Muscle Nerve. Apr 1999;22(4):480-7. [Medline].

  113. Barohn RJ. The therapeutic dilemma of inclusion body myositis. Neurology. Mar 1997;48(3):567-8. [Medline].

  114. Behrens L, Kerschensteiner M, Misgeld T, et al. Human muscle cells express a functional costimulatory molecule distinct from B7.1 (CD80) and B7.2 (CD86) in vitro and in inflammatory lesions. J Immunol. Dec 1 1998;161(11):5943-51. [Medline].

  115. Brannagan TH, Hays AP, Lange DJ, Trojaborg W. The role of quantitative electromyography in inclusion body myositis. J Neurol Neurosurg Psychiatry. Dec 1997;63(6):776-9. [Medline].

  116. Chou SM. Myxovirus-like structures in a case of human chronic polymyositis. Science. Dec 15 1967;158(807):1453-5. [Medline].

  117. Civatte M, Bartoli C, Schleinitz N, et al. Expression of the beta chemokines CCL3, CCL4, CCL5 and their receptors in idiopathic inflammatory myopathies. Neuropathol Appl Neurobiol. Feb 2005;31(1):70-9. [Medline].

  118. Dabby R, Lange DJ, Trojaborg W, et al. Inclusion body myositis mimicking motor neuron disease. Arch Neurol. Aug 2001;58(8):1253-6. [Medline].

  119. Dahlbom K, Lindberg C, Oldfors A. Inclusion body myositis: morphological clues to correct diagnosis. Neuromuscul Disord. Nov 2002;12(9):853-7. [Medline].

  120. Danon MJ, Friedman M. Inclusion body myositis associated with progressive dysphagia: treatment with cricopharyngeal myotomy. Can J Neurol Sci. Nov 1989;16(4):436-8. [Medline].

  121. De Paepe B, De Bleecker JL. Beta-chemokine receptor expression in idiopathic inflammatory myopathies. Muscle Nerve. May 2005;31(5):621-7. [Medline].

  122. De Paepe B, De Keyzer K, Martin JJ, De Bleecker JL. Alpha-chemokine receptors CXCR1-3 and their ligands in idiopathic inflammatory myopathies. Acta Neuropathol (Berl). Jun 2005;109(6):576-82. [Medline].

  123. Dion E, Cherin P, Payan C, et al. Magnetic resonance imaging criteria for distinguishing between inclusion body myositis and polymyositis. J Rheumatol. Sep 2002;29(9):1897-906. [Medline].

  124. Ferrer I, Carmona M, Blanco R, et al. Involvement of clusterin and the aggresome in abnormal protein deposits in myofibrillar myopathies and inclusion body myositis. Brain Pathol. Apr 2005;15(2):101-8. [Medline].

  125. Ferrer I, Martin B, Castano JG, et al. Proteasomal expression, induction of immunoproteasome subunits, and local MHC class I presentation in myofibrillar myopathy and inclusion body myositis. J Neuropathol Exp Neurol. May 2004;63(5):484-98. [Medline].

  126. Figarella-Branger D, Civatte M, Bartoli C, Pellissier JF. Cytokines, chemokines, and cell adhesion molecules in inflammatory myopathies. Muscle Nerve. Dec 2003;28(6):659-82. [Medline].

  127. Fratta P, Engel WK, McFerrin J, et al. Proteasome inhibition and aggresome formation in sporadic inclusion-body myositis and in amyloid-beta precursor protein-overexpressing cultured human muscle fibers. Am J Pathol. Aug 2005;167(2):517-26. [Medline].

  128. Fratta P, Engel WK, Van Leeuwen FW, et al. Mutant ubiquitin UBB+1 is accumulated in sporadic inclusion-body myositis muscle fibers. Neurology. Sep 28 2004;63(6):1114-7. [Medline].

  129. Hermanns B, Molnar M, Schroder JM. Peripheral neuropathy associated with hereditary and sporadic inclusion body myositis: confirmation by electron microscopy and morphometry. J Neurol Sci. Oct 1 2000;179(S 1-2):92-102. [Medline].

  130. Jaworska-Wilczynska M, Wilczynski GM, Engel WK, et al. Three lipoprotein receptors and cholesterol in inclusion-body myositis muscle. Neurology. Feb 12 2002;58(3):438-45. [Medline].

  131. Krivickas LS, Amato AA, Krishnan G, et al. Preservation of in vitro muscle fiber function in dermatomyositis and inclusion body myositis: a single fiber study. Neuromuscul Disord. May 2005;15(5):349-54. [Medline].

  132. Li M, Dalakas MC. The muscle mitogen-activated protein kinase is altered in sporadic inclusion body myositis. Neurology. Apr 25 2000;54(8):1665-70. [Medline].

  133. Luciano CA, Dalakas MC. Inclusion body myositis: no evidence for a neurogenic component. Neurology. Jan 1997;48(1):29-33. [Medline].

  134. Monsonego A, Zota V, Karni A, et al. Increased T cell reactivity to amyloid beta protein in older humans and patients with Alzheimer disease. J Clin Invest. Aug 2003;112(3):415-22. [Medline].

  135. Nakano S, Shinde A, Kawashima S, et al. Inclusion body myositis: expression of extracellular signal-regulated kinase and its substrate. Neurology. Jan 9 2001;56(1):87-93. [Medline].

  136. Nishino H, Engel AG, Rima BK. Inclusion body myositis: the mumps virus hypothesis. Ann Neurol. Mar 1989;25(3):260-4. [Medline].

  137. Oldfors A, Larsson NG, Lindberg C, Holme E. Mitochondrial DNA deletions in inclusion body myositis. Brain. Apr 1993;116 (Pt 2):325-36. [Medline].

  138. Oldfors A, Lindberg C. Diagnosis, pathogenesis and treatment of inclusion body myositis. Curr Opin Neurol. Oct 2005;18(5):497-503. [Medline].

  139. Parissis D, Karkavelas G, Taskos N, Milonas I. Inclusion body myositis in a patient with a presumed diagnosis of post-polio syndrome. J Neurol. May 2003;250(5):619-21. [Medline].

  140. Price P, Santoso L, Mastaglia F, et al. Two major histocompatibility complex haplotypes influence susceptibility to sporadic inclusion body myositis: critical evaluation of an association with HLA-DR3. Tissue Antigens. Nov 2004;64(5):575-80. [Medline].

  141. Raju R, Vasconcelos O, Granger R, Dalakas MC. Expression of IFN-gamma-inducible chemokines in inclusion body myositis. J Neuroimmunol. Aug 2003;141(1-2):125-31. [Medline].

  142. Sekul EA, Dalakas MC. Inclusion body myositis: new concepts. Semin Neurol. Sep 1993;13(3):256-63. [Medline].

  143. Van der Muelen MF, Hoogendijk JE, Moons KG, et al. Rimmed vacuoles and the added predictive value of SM-31 staining in diagnosing sporadic inclusion body myositis. Neuromuscular Disorders. 2001;11:447-451.

  144. Verma A, Bradley WG, Adesina AM, et al. Inclusion body myositis with cricopharyngeus muscle involvement and severe dysphagia. Muscle Nerve. May 1991;14(5):470-3. [Medline].

  145. Verma A, Tandan R. TDP-43: a reliable immunohistochemistry marker for inclusion body myositis?. Muscle Nerve. Jul 2009;40(1):8-9. [Medline].

  146. Wiendl H, Mitsdoerffer M, Schneider D, et al. Human muscle cells express a B7-related molecule, B7-H1, with strong negative immune regulatory potential: a novel mechanism of counterbalancing the immune attack in idiopathic inflammatory myopathies. FASEB J. Oct 2003;17(13):1892-4. [Medline].

[ CLOSE WINDOW ]

Further Reading

[ CLOSE WINDOW ]

Keywords

sporadic inclusion body myositis, s-IBM, hereditary inclusion body myopathies, h-IBM, idiopathic inflammatory myopathies, polymyositis, PM, dermatomyositis, DM, myositis, amyloid precursor protein, APP, alien molecules, AB oligomers, alpha beta oligomers, endoplasmic reticulum, ER, unfolded protein response, UPR, heat shock protein 70, phosphorylated tau, p-tau

[ CLOSE WINDOW ]

Contributor Information and Disclosures

Author

Helen C Lin, MD, Assistant Professor of Neurology, Medical College of Wisconsin, Milwaukee
Helen C Lin, MD is a member of the following medical societies: American Academy of Neurology and American Association of Neuromuscular and Electrodiagnostic Medicine
Disclosure: Nothing to disclose.

Coauthor(s)

Paul E Barkhaus, MD, Professor, Department of Neurology, Medical College of Wisconsin; Director of Neuromuscular Diseases, Milwaukee Veterans Administration Medical Center
Paul E Barkhaus, MD is a member of the following medical societies: American Academy of Neurology, American Association of Neuromuscular and Electrodiagnostic Medicine, and American Neurological Association
Disclosure: Nothing to disclose.

Michael P Collins, MD, Associate Professor, Department of Neurology, Medical College of Wisconsin
Michael P Collins, MD is a member of the following medical societies: Alpha Omega Alpha, American Academy of Neurology, American Association of Neuromuscular and Electrodiagnostic Medicine, Peripheral Nerve Society, and World Muscle Society
Disclosure: Nothing to disclose.

M Isabel Periquet Collins, MD, Assistant Professor, Department of Neurology, Medical College of Wisconsin
M Isabel Periquet Collins, MD is a member of the following medical societies: American Academy of Neurology and American Association of Neuromuscular and Electrodiagnostic Medicine
Disclosure: Nothing to disclose.

Medical Editor

Dianna Quan, MD, Associate Professor of Neurology, Director, Electromyography Laboratory, University of Colorado Health Sciences Center
Dianna Quan, MD is a member of the following medical societies: American Academy of Neurology, American Association of Neuromuscular and Electrodiagnostic Medicine, and Phi Beta Kappa
Disclosure: e-medicine Honoraria Other

Pharmacy Editor

Francisco Talavera, PharmD, PhD, Senior Pharmacy Editor, eMedicine
Disclosure: eMedicine Salary Employment

Managing Editor

Glenn Lopate, MD, Associate Professor, Department of Neurology, Division of Neuromuscular Diseases, Washington University School of Medicine; Chief of Neurology, St Louis ConnectCare, Consulting Staff, Barnes Jewish Hospital
Glenn Lopate, MD is a member of the following medical societies: American Academy of Neurology, American Association of Neuromuscular and Electrodiagnostic Medicine, and Phi Beta Kappa
Disclosure: Nothing to disclose.

CME Editor

Selim R Benbadis, MD, Professor, Director of Comprehensive Epilepsy Program, Departments of Neurology and Neurosurgery, University of South Florida School of Medicine, Tampa General Hospital
Selim R Benbadis, MD is a member of the following medical societies: American Academy of Neurology, American Academy of Sleep Medicine, American Clinical Neurophysiology Society, American Epilepsy Society, and American Medical Association
Disclosure: Nothing to disclose.

Chief Editor

Nicholas Y Lorenzo, MD, Chief Editor, eMedicine Neurology; Consulting Staff, Neurology Specialists and Consultants
Nicholas Y Lorenzo, MD is a member of the following medical societies: Alpha Omega Alpha and American Academy of Neurology
Disclosure: Nothing to disclose.

 
 
HONcode

We subscribe to the
HONcode principles of the
Health On the Net Foundation

All material on this website is protected by copyright, Copyright© 1994- by Medscape.
This website also contains material copyrighted by 3rd parties.

DISCLAIMER: The content of this Website is not influenced by sponsors. The site is designed primarily for use by qualified physicians and other medical professionals. The information contained herein should NOT be used as a substitute for the advice of an appropriately qualified and licensed physician or other health care provider. The information provided here is for educational and informational purposes only. In no way should it be considered as offering medical advice. Please check with a physician if you suspect you are ill.