Neuromuscular Disorders
Volume 18, Issue 1 , Pages 27-33 , January 2008

Histone H1 is released from myonuclei and present in rimmed vacuoles with DNA in inclusion body myositis

Received 24 May 2007 ,Revised 6 August 2007 ,Accepted 14 August 2007.

References 

  1. Mikol J, Engel AG. Inclusion body myositis. In:  Engel AG,  Franzini-Armstrong C editor. Myology. New York, NY: McGraw-Hill; 2004;p. 1367–1388
  2. Dalakas MC. Sporadic inclusion body myositis–diagnosis, pathogenesis and therapeutic strategies. Nat Clin Pract Neurol. 2006;2:437–447
  3. 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. 1994;144:874–882
  4. Nakano S, Akiguchi I, Nakamura S, Satoi H, Kawashima S, Kimura J. Aberrant expression of cyclin-dependent kinase 5 in inclusion body myositis. Neurology. 1999;53:1671–1676
  5. Nakano S, Shinde A, Kawashima S, Nakamura S, Akiguchi I, Kimura J. Inclusion body myositis: expression of extracellular signal-regulated kinase and its substrate. Neurology. 2001;56:87–93
  6. Greenberg SA, Pinkus JL, Amato AA. Nuclear membrane proteins are present within rimmed vacuoles in inclusion-body myositis. Muscle Nerve. 2006;34:406–416
  7. 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 (Berl). 2001;101:579–584
  8. Kumamoto T, Ueyama H, Tsumura H, Toyoshima I, Tsuda T. Expression of lysosome-related proteins and genes in the skeletal muscles of inclusion body myositis. Acta Neuropathol (Berl). 2004;107:59–65
  9. Bustin M, Catez F, Lim JH. The dynamics of histone H1 function in chromatin. Mol Cell. 2005;17:617–620
  10. Woodcock CL, Skoultchi AI, Fan Y. Role of linker histone in chromatin structure and function: H1 stoichiometry and nucleosome repeat length. Chromosome Res. 2006;14:17–25
  11. Griggs R, Askanas V, DiMauro S, et al. Inclusion body myositis and myopathies. Ann Neurol. 1995;38:705–713
  12. Brown DT. Histone H1 and the dynamic regulation of chromatin function. Biochem Cell Biol. 2003;81:221–227
  13. Askanas V, Engel WK. Molecular pathology and pathogenesis of inclusion-body myositis. Microsc Res Tech. 2005;67:114–120
  14. Konishi A, Shimizu S, Hirota J, et al. Involvement of histone H1 2 in apoptosis induced by DNA double-strand breaks. Cell. 2003;114:673–688
  15. Ferrer I, Martin B, Castano JG, Lucas JJ, Moreno D, Olive M. Proteasomal expression, induction of immunoproteasome subunits, and local MHC class I presentation in myofibrillar myopathy and inclusion body myositis. J Neuropathol Exp Neurol. 2004;63:484–498
  16. Juang YT, Solomou EE, Rellahan B, Tsokos GC. Phosphorylation and O-linked glycosylation of Elf-1 leads to its translocation to the nucleus and binding to the promoter of the TCR zeta-chain. J Immunol. 2002;168:2865–2871
  17. Fahrenkrog B, Aebi U. The nuclear pore complex: nucleocytoplasmic transport and beyond. Nat Rev Mol Cell Biol. 2003;4:757–766
  18. Gustin KE, Sarnow P. Effects of poliovirus infection on nucleo-cytoplasmic trafficking and nuclear pore complex composition. EMBO J. 2001;20:240–249
  19. Belov GA, Lidsky PV, Mikitas OV, et al. Bidirectional increase in permeability of nuclear envelope upon poliovirus infection and accompanying alterations of nuclear pores. J Virol. 2004;78:10166–10177
  20. Semino-Mora C, Dalakas MC. Rimmed vacuoles with beta-amyloid and ubiquitinated filamentous deposits in the muscles of patients with long-standing denervation (postpoliomyelitis muscular atrophy): similarities with inclusion body myositis. Hum Pathol. 1998;29:1128–1133
  21. Featherstone C, Darby MK, Gerace L. A monoclonal antibody against the nuclear pore complex inhibits nucleocytoplasmic transport of protein and RNA in vivo. J Cell Biol. 1988;107:1289–1297
  22. Nonaka I, Noguchi S, Nishino I. Distal myopathy with rimmed vacuoles and hereditary inclusion body myopathy. Curr Neurol Neurosci Rep. 2005;5:61–65
  23. Eisenberg I, Avidan N, Potikha T, et al. The UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase gene is mutated in recessive hereditary inclusion body myopathy. Nat Genet. 2001;29:83–87
  24. Arai A, Tanaka K, Ikeuchi T, et al. A novel mutation in the GNE gene and a linkage disequilibrium in Japanese pedigrees. Ann Neurol. 2002;52:516–519
  25. Nishino I, Noguchi S, Murayama K, et al. Distal myopathy with rimmed vacuoles is allelic to hereditary inclusion body myopathy. Neurology. 2002;59:1689–1693
  26. Krause S, Hinderlich S, Amsili S, et al. Localization of UDP-GlcNAc 2-epimerase/ManAc kinase (GNE) in the golgi complex and the nucleus of mammalian cells. Exp Cell Res. 2005;304:365–379
  27. Whelan SA, Hart GW. Proteomic approaches to analyze the dynamic relationships between nucleocytoplasmic protein glycosylation and phosphorylation. Circ Res. 2003;93:1047–1058
  28. Calado A, Tome FM, Brais B, et al. Nuclear inclusions in oculopharyngeal muscular dystrophy consist of poly(A) binding protein 2 aggregates which sequester poly(A) RNA. Hum Mol Genet. 2000;9:2321–2328

PII: S0960-8966(07)00689-X

doi: 10.1016/j.nmd.2007.08.005

Neuromuscular Disorders
Volume 18, Issue 1 , Pages 27-33 , January 2008

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