메뉴 건너뛰기




Volumn 118, Issue 3, 2009, Pages 407-413

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

Author keywords

Cultured human muscle fibers; Inclusions; Lysosome inhibition; P62 sequestosome1 (p62 SQSTM1); Phosphorylated tau; Proteasome inhibition; Sporadic inclusion body myositis

Indexed keywords

MESSENGER RNA; PROTEIN P62; TAU PROTEIN;

EID: 68349097450     PISSN: 00016322     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00401-009-0564-6     Document Type: Article
Times cited : (133)

References (39)
  • 1
    • 0013499286 scopus 로고
    • Cultured normal and genetically abnormal human muscle
    • In: Rowland LP, Di Mauro S (eds) North Holland, Amsterdam
    • Askanas V, Engel WK (1992) Cultured normal and genetically abnormal human muscle. In: Rowland LP, Di Mauro S (eds) The handbook of clinical neurology, myopathies, vol 18. North Holland, Amsterdam, pp 85-116
    • (1992) The Handbook of Clinical Neurology, Myopathies , vol.18 , pp. 85-116
    • Askanas, V.1    Engel, W.K.2
  • 2
    • 34948816592 scopus 로고    scopus 로고
    • Inclusion-body myositis, a multifactorial muscle disease associated with aging: Current concepts of pathogenesis
    • Askanas V, Engel WK (2007) Inclusion-body myositis, a multifactorial muscle disease associated with aging: Current concepts of pathogenesis. Curr Opin Rheumatol 19:550-559
    • (2007) Curr Opin Rheumatol , vol.19 , pp. 550-559
    • Askanas, V.1    Engel, W.K.2
  • 3
    • 56749104288 scopus 로고    scopus 로고
    • Inclusion-body myositis: Muscle-fiber molecular pathology and possible pathogenic significance of its similarity to Alzheimer's and Parkinson's disease brains
    • Askanas V, Engel WK (2008) Inclusion-body myositis: Muscle-fiber molecular pathology and possible pathogenic significance of its similarity to Alzheimer's and Parkinson's disease brains. Acta Neuropathol 116:583-595
    • (2008) Acta Neuropathol , vol.116 , pp. 583-595
    • Askanas, V.1    Engel, W.K.2
  • 4
    • 0035145398 scopus 로고    scopus 로고
    • Inclusion-body myositis: Newest concepts of pathogenesis and relation to aging and Alzheimer disease
    • Askanas V, Engel WK (2001) Inclusion-body myositis: Newest concepts of pathogenesis and relation to aging and Alzheimer disease. J Neuropathol Exp Neurol 60:1-14
    • (2001) J Neuropathol Exp Neurol , vol.60 , pp. 1-14
    • Askanas, V.1    Engel, W.K.2
  • 5
    • 0027240930 scopus 로고
    • Enhanced detection of congo-red-positive amyloid deposits in muscle fibers of inclusion body myositis and brain of Alzheimer's disease using fluorescence technique
    • Askanas V, Engel WK, Alvarez RB (1993) Enhanced detection of congo-red-positive amyloid deposits in muscle fibers of inclusion body myositis and brain of Alzheimer's disease using fluorescence technique. Neurology 43:1265-1267
    • (1993) Neurology , vol.43 , pp. 1265-1267
    • Askanas, V.1    Engel, W.K.2    Alvarez, R.B.3
  • 6
    • 0033934231 scopus 로고    scopus 로고
    • Novel immunolocalization of alpha-synuclein in human muscle of inclusion-body myositis, regenerating and necrotic muscle fibers, and at neuromuscular junctions
    • Askanas V, Engel WK, Alvarez RB, McFerrin J, Broccolini A (2000) 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 59:592-598
    • (2000) J Neuropathol Exp Neurol , vol.59 , pp. 592-598
    • Askanas, V.1    Engel, W.K.2    Alvarez, R.B.3    McFerrin, J.4    Broccolini, A.5
  • 7
    • 66949145779 scopus 로고    scopus 로고
    • Inclusion-body myositis: A degenerative muscle disease associated with intra-muscle-fiber multiprotein aggregates, proteasome inhibition, endoplasmic reticulum stress, and decreased lysosomal degradation
    • doi: 10.1111/j.1750-3639.2009.00290.x
    • Askanas V, Engel WK, Nogalska A (2009) Inclusion-body myositis: A degenerative muscle disease associated with intra-muscle-fiber multiprotein aggregates, proteasome inhibition, endoplasmic reticulum stress, and decreased lysosomal degradation. Brain Pathol 19:493-506. doi: 10.1111/j.1750-3639.2009.00290.x
    • (2009) Brain Pathol , vol.19 , pp. 493-506
    • Askanas, V.1    Engel, W.K.2    Nogalska, A.3
  • 8
    • 21344463770 scopus 로고    scopus 로고
    • Sequestosome 1/p62 shuttles polyubiquitinated tau for proteasomal degradation
    • Babu JR, Geetha T, Wooten MW (2005) Sequestosome 1/p62 shuttles polyubiquitinated tau for proteasomal degradation. J Neurochem 94:192-203
    • (2005) J Neurochem , vol.94 , pp. 192-203
    • Babu, J.R.1    Geetha, T.2    Wooten, M.W.3
  • 10
    • 27944504351 scopus 로고    scopus 로고
    • p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death
    • Bjorkoy G, Lamark T, Brech A, Outzen H, Perander M, Overvatn A, Stenmark H, Johansen T (2005) p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death. J Cell Biol 171:603-614
    • (2005) J Cell Biol , vol.171 , pp. 603-614
    • Bjorkoy, G.1    Lamark, T.2    Brech, A.3    Outzen, H.4    Perander, M.5    Overvatn, A.6    Stenmark, H.7    Johansen, T.8
  • 11
    • 33645926989 scopus 로고    scopus 로고
    • p62/SQSTM1: A missing link between protein aggregates and the autophagy machinery
    • Bjorkoy G, Lamark T, Johansen T (2006) p62/SQSTM1: A missing link between protein aggregates and the autophagy machinery. Autophagy 2:138-139
    • (2006) Autophagy , vol.2 , pp. 138-139
    • Bjorkoy, G.1    Lamark, T.2    Johansen, T.3
  • 13
    • 24144489814 scopus 로고    scopus 로고
    • Proteasome inhibition and aggresome formation in sporadic inclusion-body myositis and in amyloid-β precursor protein-overexpressing cultured human muscle fibers
    • Fratta P, Engel WK, McFerrin J, Davies KJ, Lin SW, Askanas V (2005) Proteasome inhibition and aggresome formation in sporadic inclusion-body myositis and in amyloid-β precursor protein-overexpressing cultured human muscle fibers. Am J Pathol 167:517-526
    • (2005) Am J Pathol , vol.167 , pp. 517-526
    • Fratta, P.1    Engel, W.K.2    McFerrin, J.3    Davies, K.J.4    Lin, S.W.5    Askanas, V.6
  • 14
    • 0028946744 scopus 로고
    • Monoclonal antibody AT8 recognises tau protein phosphorylated at both serine 202 and threonine 205
    • Goedert M, Jakes R, Vanmechelen E (1995) Monoclonal antibody AT8 recognises tau protein phosphorylated at both serine 202 and threonine 205. Neurosci Lett 189:167-170
    • (1995) Neurosci Lett , vol.189 , pp. 167-170
    • Goedert, M.1    Jakes, R.2    Vanmechelen, E.3
  • 15
    • 0031555892 scopus 로고    scopus 로고
    • Low micromolar levels of hydrogen peroxide and proteasome inhibitors induce the 60-kDa A170 stress protein in murine peritoneal macrophages
    • Ishii T, Yanagawa T, Yuki K, Kawane T, Yoshida H, Bannai S (1997) Low micromolar levels of hydrogen peroxide and proteasome inhibitors induce the 60-kDa A170 stress protein in murine peritoneal macrophages. Biochem Biophys Res Comm 232:33-37
    • (1997) Biochem Biophys Res Comm , vol.232 , pp. 33-37
    • Ishii, T.1    Yanagawa, T.2    Yuki, K.3    Kawane, T.4    Yoshida, H.5    Bannai, S.6
  • 17
    • 0342519699 scopus 로고
    • Recognition of tau epitopes by anti-neurofilament antibodies that bind to Alzheimer neurofibrillary tangles
    • Ksiezak-Reding H, Dickson DW, Davies P, Yen SH (1987) Recognition of tau epitopes by anti-neurofilament antibodies that bind to Alzheimer neurofibrillary tangles. Proc Natl Acad Sci USA 84:3410-3414
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 3410-3414
    • Ksiezak-Reding, H.1    Dickson, D.W.2    Davies, P.3    Yen, S.H.4
  • 19
    • 0036284021 scopus 로고    scopus 로고
    • Early accumulation of p62 in neurofibrillary tangles in Alzheimer's disease: Possible role in tangle formation
    • Kuusisto E, Salminen A, Alafuzoff I (2002) Early accumulation of p62 in neurofibrillary tangles in Alzheimer's disease: Possible role in tangle formation. Neuropathol Appl Neurobiol 28:228-237
    • (2002) Neuropathol Appl Neurobiol , vol.28 , pp. 228-237
    • Kuusisto, E.1    Salminen, A.2    Alafuzoff, I.3
  • 20
    • 0035919837 scopus 로고    scopus 로고
    • Ubiquitin-binding protein p62 is present in neuronal and glial inclusions in human tauopathies and synucleinopathies
    • Kuusisto E, Salminen A, Alafuzoff I (2001) Ubiquitin-binding protein p62 is present in neuronal and glial inclusions in human tauopathies and synucleinopathies. NeuroReport 12:2085-2090
    • (2001) NeuroReport , vol.12 , pp. 2085-2090
    • Kuusisto, E.1    Salminen, A.2    Alafuzoff, I.3
  • 21
    • 0034805395 scopus 로고    scopus 로고
    • Ubiquitin-binding protein p62 expression is induced during apoptosis and proteasomal inhibition in neuronal cells
    • Kuusisto E, Suuronen T, Salminen A (2001) Ubiquitin-binding protein p62 expression is induced during apoptosis and proteasomal inhibition in neuronal cells. Biochem Biophys Res Comm 280:223-228
    • (2001) Biochem Biophys Res Comm , vol.280 , pp. 223-228
    • Kuusisto, E.1    Suuronen, T.2    Salminen, A.3
  • 22
    • 0026327717 scopus 로고
    • Amyloid filaments in inclusion body myositis. Novel findings provide insight into nature of filaments
    • Mendell JR, Sahenk Z, Gales T, Paul L (1991) Amyloid filaments in inclusion body myositis. Novel findings provide insight into nature of filaments. Arch Neurol 48:1229-1234
    • (1991) Arch Neurol , vol.48 , pp. 1229-1234
    • Mendell, J.R.1    Sahenk, Z.2    Gales, T.3    Paul, L.4
  • 23
    • 0033621047 scopus 로고    scopus 로고
    • Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo antiinflammatory activity
    • Meng L, Mohan R, Kwok BH, Elofsson M, Sin N, Crews CM (1999) Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo antiinflammatory activity. Proc Natl Acad Sci USA 96:10403-10408
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 10403-10408
    • Meng, L.1    Mohan, R.2    Kwok, B.H.3    Elofsson, M.4    Sin, N.5    Crews, C.M.6
  • 24
    • 0029971055 scopus 로고    scopus 로고
    • Difference in expression of phosphorylated tau epitopes between sporadic inclusion-body myositis and hereditary inclusion-body myopathies
    • Mirabella M, Alvarez RB, Bilak M, Engel WK, Askanas V (1996) Difference in expression of phosphorylated tau epitopes between sporadic inclusion-body myositis and hereditary inclusion-body myopathies. J Neuropathol Exp Neurol 55:774-786
    • (1996) J Neuropathol Exp Neurol , vol.55 , pp. 774-786
    • Mirabella, M.1    Alvarez, R.B.2    Bilak, M.3    Engel, W.K.4    Askanas, V.5
  • 25
    • 33846692198 scopus 로고    scopus 로고
    • Signal integration and diversification through the p62 scaffold protein
    • Moscat J, Diaz-Meco MT, Wooten MW (2007) Signal integration and diversification through the p62 scaffold protein. Trends Biochem Sci 32:95-100
    • (2007) Trends Biochem Sci , vol.32 , pp. 95-100
    • Moscat, J.1    Diaz-Meco, M.T.2    Wooten, M.W.3
  • 26
    • 34250377470 scopus 로고    scopus 로고
    • Inclusion body myositis: Current pathogenetic concepts and diagnostic and therapeutic approaches
    • Needham M, Mastaglia FL (2007) Inclusion body myositis: Current pathogenetic concepts and diagnostic and therapeutic approaches. Lancet Neurol 6:620-631
    • (2007) Lancet Neurol , vol.6 , pp. 620-631
    • Needham, M.1    Mastaglia, F.L.2
  • 27
    • 33645107853 scopus 로고    scopus 로고
    • Homocysteine-induced endoplasmic reticulum protein (Herp) is up-regulated in sporadic inclusion-body myositis and in endoplasmic reticulum stress-induced cultured human muscle fibers
    • Nogalska A, Engel WK, McFerrin J, Kokame K, Komano H, Askanas V (2006) Homocysteine-induced endoplasmic reticulum protein (Herp) is up-regulated in sporadic inclusion-body myositis and in endoplasmic reticulum stress-induced cultured human muscle fibers. J Neurochem 96:1491-1499
    • (2006) J Neurochem , vol.96 , pp. 1491-1499
    • Nogalska, A.1    Engel, W.K.2    McFerrin, J.3    Kokame, K.4    Komano, H.5    Askanas, V.6
  • 28
    • 33947622602 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress induces myostatin precursor protein and NF-κB in cultured human muscle fibers: Relevance to inclusion body myositis
    • Nogalska A, Wojcik S, Engel WK, McFerrin J, Askanas V (2007) Endoplasmic reticulum stress induces myostatin precursor protein and NF-κB in cultured human muscle fibers: Relevance to inclusion body myositis. Exp Neurol 204:610-618
    • (2007) Exp Neurol , vol.204 , pp. 610-618
    • Nogalska, A.1    Wojcik, S.2    Engel, W.K.3    McFerrin, J.4    Askanas, V.5
  • 29
    • 0348047708 scopus 로고
    • Recognition of Alzheimer paired helical filaments by monoclonal neurofilament antibodies is due to crossreaction with tau protein
    • Nukina N, Kosik KS, Selkoe DJ (1987) Recognition of Alzheimer paired helical filaments by monoclonal neurofilament antibodies is due to crossreaction with tau protein. Proc Natl Acad Sci USA 84:3415-3419
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 3415-3419
    • Nukina, N.1    Kosik, K.S.2    Selkoe, D.J.3
  • 30
    • 2642714342 scopus 로고
    • Fluorescence probe measurement of the intralysosomal pH in living cells and the perturbation of pH by various agents
    • Ohkuma S, Poole B (1978) Fluorescence probe measurement of the intralysosomal pH in living cells and the perturbation of pH by various agents. Proc Natl Acad Sci USA 75:3327-3331
    • (1978) Proc Natl Acad Sci USA , vol.75 , pp. 3327-3331
    • Ohkuma, S.1    Poole, B.2
  • 33
    • 33947248608 scopus 로고    scopus 로고
    • The ubiquitin-binding protein p62 identifies argyrophilic grain pathology with greater sensitivity than conventional silver stains
    • Scott IS, Lowe JS (2007) The ubiquitin-binding protein p62 identifies argyrophilic grain pathology with greater sensitivity than conventional silver stains. Acta Neuropathol 113:417-420
    • (2007) Acta Neuropathol , vol.113 , pp. 417-420
    • Scott, I.S.1    Lowe, J.S.2
  • 34
    • 4444220680 scopus 로고    scopus 로고
    • Sequestosome 1/p62 is a polyubiquitin chain binding protein involved in ubiquitin proteasome degradation
    • Seibenhener ML, Babu JR, Geetha T, Wong HC, Krishna NR, Wooten MW (2004) Sequestosome 1/p62 is a polyubiquitin chain binding protein involved in ubiquitin proteasome degradation. Mol Cell Biol 24:8055-8068
    • (2004) Mol Cell Biol , vol.24 , pp. 8055-8068
    • Seibenhener, M.L.1    Babu, J.R.2    Geetha, T.3    Wong, H.C.4    Krishna, N.R.5    Wooten, M.W.6
  • 35
    • 54949129369 scopus 로고    scopus 로고
    • In inclusion-body myositis muscle fibers Parkinson-associated DJ-1 is increased and oxidized
    • Terracciano C, Nogalska A, Engel WK, Wojcik S, Askanas V (2008) In inclusion-body myositis muscle fibers Parkinson-associated DJ-1 is increased and oxidized. Free Radic Biol Med 45:773-779
    • (2008) Free Radic Biol Med , vol.45 , pp. 773-779
    • Terracciano, C.1    Nogalska, A.2    Engel, W.K.3    Wojcik, S.4    Askanas, V.5
  • 36
    • 0030942146 scopus 로고    scopus 로고
    • Increase of nitric oxide synthases and nitrotyrosine in inclusion-body myositis
    • Yang CC, Alvarez RB, Engel WK, Askanas V (1996) Increase of nitric oxide synthases and nitrotyrosine in inclusion-body myositis. NeuroReport 8:153-158
    • (1996) NeuroReport , vol.8 , pp. 153-158
    • Yang, C.C.1    Alvarez, R.B.2    Engel, W.K.3    Askanas, V.4
  • 37
    • 0032566756 scopus 로고    scopus 로고
    • Immunolocalization of transcription factor NF-kappaB in inclusion-body myositis muscle and at normal human neuromuscular junctions
    • Yang CC, Askanas V, Engel WK, Alvarez RB (1998) Immunolocalization of transcription factor NF-kappaB in inclusion-body myositis muscle and at normal human neuromuscular junctions. Neurosci Lett 254:77-80
    • (1998) Neurosci Lett , vol.254 , pp. 77-80
    • Yang, C.C.1    Askanas, V.2    Engel, W.K.3    Alvarez, R.B.4
  • 39
    • 0032521599 scopus 로고    scopus 로고
    • Sequential phosphorylation of Tau by glycogen synthase kinase-3beta and protein kinase A at Thr212 and Ser214 generates the Alzheimer-specific epitope of antibody AT100 and requires a paired-helical-filament-like conformation
    • Zheng-Fischhèofer Q, Biernat J, Mandelkow EM, Illenberger S, Godemann R, Mandelkow E (1998) Sequential phosphorylation of Tau by glycogen synthase kinase-3beta and protein kinase A at Thr212 and Ser214 generates the Alzheimer-specific epitope of antibody AT100 and requires a paired-helical-filament-like conformation. Eur J Biochem 252:542-552
    • (1998) Eur J Biochem , vol.252 , pp. 542-552
    • Zheng-Fischhèofer, Q.1    Biernat, J.2    Mandelkow, E.M.3    Illenberger, S.4    Godemann, R.5    Mandelkow, E.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.