메뉴 건너뛰기




Volumn 18, Issue 3, 2003, Pages 185-190

Unfolding story of inclusion-body myositis and myopathies: Role of misfolded proteins, amyloid-β, cholesterol, and aging

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; CHOLESTEROL; PROTEIN PRECURSOR;

EID: 0038407678     PISSN: 08830738     EISSN: None     Source Type: Journal    
DOI: 10.1177/08830738030180030401     Document Type: Article
Times cited : (21)

References (48)
  • 1
    • 0034788308 scopus 로고    scopus 로고
    • Inflammatory muscle diseases
    • Hilton-Jones D: Inflammatory muscle diseases. Curr Opin Neurol 2001;14:591-596.
    • (2001) Curr. Opin. Neurol. , vol.14 , pp. 591-596
    • Hilton-Jones, D.1
  • 2
    • 0035378755 scopus 로고    scopus 로고
    • The molecular and cellular pathology of inflammatory muscle diseases
    • Dalakas MC: The molecular and cellular pathology of inflammatory muscle diseases. Curr Opin Pharmacol 2001;1:300-306.
    • (2001) Curr. Opin. Pharmacol. , vol.1 , pp. 300-306
    • Dalakas, M.C.1
  • 3
    • 0001820734 scopus 로고    scopus 로고
    • New insights, current concepts in the pathophysiology of inflammatory myopathies
    • Mendell J: New insights, current concepts in the pathophysiology of inflammatory myopathies. Adv Immunotherapy 2001;8:12-16.
    • (2001) Adv. Immunotherapy , vol.8 , pp. 12-16
    • Mendell, J.1
  • 4
    • 0001827396 scopus 로고    scopus 로고
    • Treatment of inclusion-body myositis and hereditary inclusion-body myopathy with reference to pathogenic mechanism
    • Personal experiences Askanas V, Serratrice G, Engel WK (eds): Cambridge, United Kingdom: Cambridge University Press
    • Engel WK, Askanas V: Treatment of inclusion-body myositis and hereditary inclusion-body myopathy with reference to pathogenic mechanism. Personal experiences, in Askanas V, Serratrice G, Engel WK (eds): Inclusion-Body Myositis and Myopathies. Cambridge, United Kingdom: Cambridge University Press, 1998, 351-382.
    • (1998) Inclusion-Body Myositis and Myopathies , pp. 351-382
    • Engel, W.K.1    Askanas, V.2
  • 5
    • 0035145398 scopus 로고    scopus 로고
    • Inclusion-body myositis: Newest concepts of pathogenesis and relation to aging and Alzheimer disease
    • Askanas V, Engel WK: Inclusion-body myositis: Newest concepts of pathogenesis and relation to aging and Alzheimer disease. J Neuropathol Exp Neurol 2001;60:1-14.
    • (2001) J. Neuropathol. Exp. Neurol. , vol.60 , pp. 1-14
    • Askanas, V.1    Engel, W.K.2
  • 6
    • 0031740915 scopus 로고    scopus 로고
    • Transgenic mice over-expressing the C-99 fragment of betaPP with an alpha-s myopathy similar to human inclusion body myositis
    • Jin LW, Hearn MG, Ogburn CE, et al: Transgenic mice over-expressing the C-99 fragment of betaPP with an alpha-s myopathy similar to human inclusion body myositis. Am J Pathol 1998;153:1679-1686.
    • (1998) Am. J. Pathol. , vol.153 , pp. 1679-1686
    • Jin, L.W.1    Hearn, M.G.2    Ogburn, C.E.3
  • 7
    • 0031772229 scopus 로고    scopus 로고
    • Amyloid-beta deposition in skeletal muscle of transgenic mice: Possible model of inclusion body myopathy
    • Fukuchi K, Pham D, Hart M, et al: Amyloid-beta deposition in skeletal muscle of transgenic mice: Possible model of inclusion body myopathy. Am J Pathol 1998;153:1687-1693.
    • (1998) Am. J. Pathol. , vol.153 , pp. 1687-1693
    • Fukuchi, K.1    Pham, D.2    Hart, M.3
  • 8
    • 0037197835 scopus 로고    scopus 로고
    • Inclusion body myositis-like phenotype induced by transgenic overexpression of βAPP in skeletal muscle
    • Sugarman MC, Yamasaki TR, Oddo S, et al: Inclusion body myositis-like phenotype induced by transgenic overexpression of βAPP in skeletal muscle. Proc Natl Acad Sci U S A 2002;99:8334-8339.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 8334-8339
    • Sugarman, M.C.1    Yamasaki, T.R.2    Oddo, S.3
  • 9
    • 0035846620 scopus 로고    scopus 로고
    • Inflammation in dysferlin myopathy: Immunohistochemical characterization of 13 patients
    • Gallardo E, Rojas-Garcia R, de Luna N, et al: Inflammation in dysferlin myopathy: Immunohistochemical characterization of 13 patients. Neurology 2001;57:2136-2138.
    • (2001) Neurology , vol.57 , pp. 2136-2138
    • Gallardo, E.1    Rojas-Garcia, R.2    de Luna, N.3
  • 10
    • 0033625360 scopus 로고    scopus 로고
    • Partial laminin α2 chain deficiency in a patient with myopathy resembling inclusion body myositis
    • Di Blasi C, Mora M, Pareyson D, et al: Partial laminin α2 chain deficiency in a patient with myopathy resembling inclusion body myositis. Ann Neurol 2000;47:811-816.
    • (2000) Ann. Neurol. , vol.47 , pp. 811-816
    • Di Blasi, C.1    Mora, M.2    Pareyson, D.3
  • 11
    • 0033402111 scopus 로고    scopus 로고
    • Facioscapulohumeral muscular dystrophy
    • Fitzsimmons RB: Facioscapulohumeral muscular dystrophy. Curr Opin Neurol 1999;12:501-511.
    • (1999) Curr. Opin. Neurol. , vol.12 , pp. 501-511
    • Fitzsimmons, R.B.1
  • 12
  • 13
    • 0742324250 scopus 로고    scopus 로고
    • Hereditary inclusion-body myopathies
    • Rosenberg RN, Prusiner SB, DiMauro S, et al (eds): 3rd ed. Philadelphia: Butterworth-Heinemann, in press
    • Askanas V, Engel WK: Hereditary inclusion-body myopathies, in Rosenberg RN, Prusiner SB, DiMauro S, et al (eds): The Molecular and Genetic Basis of Neurologic and Psychiatric Disease, 3rd ed. Philadelphia: Butterworth-Heinemann, in press.
    • The Molecular and Genetic Basis of Neurologic and Psychiatric Disease
    • Askanas, V.1    Engel, W.K.2
  • 15
    • 0002697494 scopus 로고    scopus 로고
    • Newest approaches to diagnosis and pathogenesis of sporadic inclusion-body myositis and hereditary inclusion-body myopathies, including molecular-pathologic similarities to Alzheimer disease
    • Askanas V, Serratrice G, Engel WK (eds): Cambridge, United Kingdom: Cambridge University Press,
    • Askanas V, Engel WK: Newest approaches to diagnosis and pathogenesis of sporadic inclusion-body myositis and hereditary inclusion-body myopathies, including molecular-pathologic similarities to Alzheimer disease, in Askanas V, Serratrice G, Engel WK (eds): Inclusion-Body Myositis and Myopathies. Cambridge, United Kingdom: Cambridge University Press, 1998, 3-78.
    • (1998) Inclusion-Body Myositis and Myopathies , pp. 3-78
    • Askanas, V.1    Engel, W.K.2
  • 16
    • 0012267680 scopus 로고    scopus 로고
    • Late-juvenile sporadic inclusion body myositis: A newly recognized syndrome
    • Askanas V, Engel WK: Late-juvenile sporadic inclusion body myositis: A newly recognized syndrome. Ann Neurol 2000;48:439-440.
    • (2000) Ann. Neurol. , vol.48 , pp. 439-440
    • Askanas, V.1    Engel, W.K.2
  • 17
    • 0034083637 scopus 로고    scopus 로고
    • Inclusion body myositis, muscle blood vessel and cardiac amyloidosis, and transthyretin Vall22lle Allele
    • Askanas V, Engel WK, Alvarez RB, et al: Inclusion body myositis, muscle blood vessel and cardiac amyloidosis, and transthyretin Vall22lle Allele. Ann Neurol 2000;47:544-549.
    • (2000) Ann. Neurol. , vol.47 , pp. 544-549
    • Askanas, V.1    Engel, W.K.2    Alvarez, R.B.3
  • 18
    • 17944366749 scopus 로고    scopus 로고
    • The UDP-N-acetylglucosamine 2-epimerase/N acetylmannosamine kinase gene is mutated in recessive hereditary inclusion body myopathy
    • 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.
    • (2001) Nat. Genet. , vol.29 , pp. 83-87
    • Eisenberg, I.1    Avidan, N.2    Potikha, T.3
  • 19
    • 0037072252 scopus 로고    scopus 로고
    • Distal myopathy with rimmed vacuoles: Novel mutations in the GNE gene
    • Tomimitsu H, Ishikawa K, Shimizu J, et al: Distal myopathy with rimmed vacuoles: Novel mutations in the GNE gene. Neurology 2002;59(Suppl 3):451-454.
    • (2002) Neurology , vol.59 , Issue.SUPPL. 3 , pp. 451-454
    • Tomimitsu, H.1    Ishikawa, K.2    Shimizu, J.3
  • 20
    • 0036791916 scopus 로고    scopus 로고
    • A novel mutation in the GNE gene and a linkage disequilibrium in Japanese pedigrees
    • 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.
    • (2002) Ann. Neurol. , vol.52 , pp. 516-519
    • Arai, A.1    Tanaka, K.2    Ikeuchi, T.3
  • 21
    • 4243307878 scopus 로고    scopus 로고
    • Detection of two mutant alleles in the UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase gene (GNE) in a cohort of patients with sporadic and hereditary inclusion body myopathies (IBM)
    • Vasconcelos OM, Raghavan R, Granger R, et al: Detection of two mutant alleles in the UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase gene (GNE) in a cohort of patients with sporadic and hereditary inclusion body myopathies (IBM). Neurology 2002;58(Suppl 3):A390.
    • (2002) Neurology , vol.58 , Issue.SUPPL. 3
    • Vasconcelos, O.M.1    Raghavan, R.2    Granger, R.3
  • 22
    • 0030827890 scopus 로고    scopus 로고
    • A bifunctional enzyme catalyzes the first two steps in N-acetylneuraminic acid biosynthesis of rat liver
    • Stäschet, Hinderlich S, Weise C, et al: A bifunctional enzyme catalyzes the first two steps in N-acetylneuraminic acid biosynthesis of rat liver. J Biol Chem 1997;272:24319-24324.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24319-24324
    • Stäschet Hinderlich, S.1    Weise, C.2
  • 23
    • 0033018503 scopus 로고    scopus 로고
    • Primary structure and expression analysis of human UDP-N-acetyl-glucosamine-2-epimerase/N-acetylmannosamine kinase, the bifunctional enzyme in neuraminic acid biosynthesis
    • Lucka L, Krause M, Danker K, et al: Primary structure and expression analysis of human UDP-N-acetyl-glucosamine-2-epimerase/N-acetylmannosamine kinase, the bifunctional enzyme in neuraminic acid biosynthesis. FEBS Lett 1999;454:341-344.
    • (1999) FEBS Lett. , vol.454 , pp. 341-344
    • Lucka, L.1    Krause, M.2    Danker, K.3
  • 24
    • 0033591388 scopus 로고    scopus 로고
    • UDP-GlcNAc 2-epimerase: A regulator of cell surface sialylation
    • Keppler OT, Hinderlich S, Langner J, et al: UDP-GlcNAc 2-epimerase: A regulator of cell surface sialylation. Science 1999;284:1372-1376.
    • (1999) Science , vol.284 , pp. 1372-1376
    • Keppler, O.T.1    Hinderlich, S.2    Langner, J.3
  • 25
    • 0027240930 scopus 로고
    • Enhanced detection of congored positive amyloid deposits in muscle fibers of inclusion-body myositis and brain of Alzheimer disease using fluorescence technique
    • Askanas V, Engel WK, Alvarez RB: Enhanced detection of congored positive amyloid deposits in muscle fibers of inclusion-body myositis and brain of Alzheimer disease using fluorescence technique. Neurology 1993;43:1265-1267.
    • (1993) Neurology , vol.43 , pp. 1265-1267
    • Askanas, V.1    Engel, W.K.2    Alvarez, R.B.3
  • 26
    • 0029944817 scopus 로고    scopus 로고
    • Use of antineurofilament antibody to identify paired-helical filaments in inclusion-body myositis
    • Askanas V, Alvarez RB, Mirabella M, et al: Use of antineurofilament antibody to identify paired-helical filaments in inclusion-body myositis. Ann Neurol 1996;39:389-391.
    • (1996) Ann. Neurol. , vol.39 , pp. 389-391
    • Askanas, V.1    Alvarez, R.B.2    Mirabella, M.3
  • 27
    • 0001698695 scopus 로고
    • Rapid examination of muscle tissue - An improved trichrome method for fresh-frozen biopsy sections
    • Engel WK, Cunningham GG: Rapid examination of muscle tissue - an improved trichrome method for fresh-frozen biopsy sections. Neurology 1963;13:919-923.
    • (1963) Neurology , vol.13 , pp. 919-923
    • Engel, W.K.1    Cunningham, G.G.2
  • 28
    • 0026556331 scopus 로고
    • Immunocytochemical localization of ubiquitin in inclusion-body myositis allows its light-microscopic distinction from polymyositis
    • Askanas V, Serdaroglu P, Engel WK, et al: Immunocytochemical localization of ubiquitin in inclusion-body myositis allows its light-microscopic distinction from polymyositis. Neurology 1992;42:460-461.
    • (1992) Neurology , vol.42 , pp. 460-461
    • Askanas, V.1    Serdaroglu, P.2    Engel, W.K.3
  • 29
    • 0030769397 scopus 로고    scopus 로고
    • Ubiquitin immunostaining and inclusion body myositis: Study of 30 patients with inclusion body myositis
    • Prayson RA, Cohen ML: Ubiquitin immunostaining and inclusion body myositis: Study of 30 patients with inclusion body myositis. Hum Pathol 1997;28:887-892.
    • (1997) Hum. Pathol. , vol.28 , pp. 887-892
    • Prayson, R.A.1    Cohen, M.L.2
  • 30
    • 0001501524 scopus 로고    scopus 로고
    • New autosomal-dominant inclusion-body myopathy (AD-IBM) with many congophilic muscle nuclei that contain paired-helical filaments (PHFs) composed of phosphorylated tau
    • Alvarez RB, Simmons Z, Engel WK: New autosomal-dominant inclusion-body myopathy (AD-IBM) with many congophilic muscle nuclei that contain paired-helical filaments (PHFs) composed of phosphorylated tau. Neurology 1998;50:A204.
    • (1998) Neurology , vol.50
    • Alvarez, R.B.1    Simmons, Z.2    Engel, W.K.3
  • 31
    • 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, et al: Difference in expression of phosphorylated tau epitopes between sporadic inclusion-body myositis and hereditary inclusion-body myopathies. J Neuropathol Exp Neurol 1996;55:774-786.
    • (1996) J. Neuropathol. Exp. Neurol. , vol.55 , pp. 774-786
    • Mirabella, M.1    Alvarez, R.B.2    Bilak, M.3
  • 32
    • 0030483060 scopus 로고    scopus 로고
    • Apolipoprotein E and apolipoprotein E messenger RNA in muscle of inclusion body myositis and myopathies
    • Mirabella M, Alvarez RB, Engel WK, et al: Apolipoprotein E and apolipoprotein E messenger RNA in muscle of inclusion body myositis and myopathies. Ann Neurol 1996;40:864-872.
    • (1996) Ann. Neurol. , vol.40 , pp. 864-872
    • Mirabella, M.1    Alvarez, R.B.2    Engel, W.K.3
  • 33
    • 0000146973 scopus 로고    scopus 로고
    • Partial expression of oculopharyngeal muscular dystrophy (OPMD) muscle fibers of the intracellular phenotype of sporadic inclusion-body myositis (s-IBM)
    • Askanas V, Alvarez RB, Sarkozi E, et al: Partial expression of oculopharyngeal muscular dystrophy (OPMD) muscle fibers of the intracellular phenotype of sporadic inclusion-body myositis (s-IBM). Neurology 1997;48:A331.
    • (1997) Neurology , vol.48
    • Askanas, V.1    Alvarez, R.B.2    Sarkozi, E.3
  • 34
  • 35
    • 0031003233 scopus 로고    scopus 로고
    • The Alzheimer family of diseases: Many etiologies, one pathogenesis?
    • Hardy J: The Alzheimer family of diseases: Many etiologies, one pathogenesis? Proc Natl Acad Sci U S A 1997;94:2095-2097.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 2095-2097
    • Hardy, J.1
  • 36
    • 0037041441 scopus 로고    scopus 로고
    • Danger - Misfolding proteins
    • Ellis RJ, Pinheiro TJT: Danger - misfolding proteins. Nature 2002;416:483-484.
    • (2002) Nature , vol.416 , pp. 483-484
    • Ellis, R.J.1    Pinheiro, T.J.T.2
  • 37
    • 0037041420 scopus 로고    scopus 로고
    • Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
    • Bucciantini M, Giannoni E, Chiti F, et al: Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature 2002;416:507-511.
    • (2002) Nature , vol.416 , pp. 507-511
    • Bucciantini, M.1    Giannoni, E.2    Chiti, F.3
  • 38
    • 0035139109 scopus 로고    scopus 로고
    • Cellular defenses against unfolded proteins: A cell biologist thinks about neurodegenerative diseases
    • Sherman MY, Goldberg AL: Cellular defenses against unfolded proteins: A cell biologist thinks about neurodegenerative diseases. Neuron 2001;29:15-32.
    • (2001) Neuron , vol.29 , pp. 15-32
    • Sherman, M.Y.1    Goldberg, A.L.2
  • 39
    • 0035818579 scopus 로고    scopus 로고
    • Specificity in intracellular protein aggregation and inclusion body formation
    • Rajan RS, Illing ME, Bence NF, et al: Specificity in intracellular protein aggregation and inclusion body formation. Proc Natl Acad Sci U S A 2001;98:13060-13065.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 13060-13065
    • Rajan, R.S.1    Illing, M.E.2    Bence, N.F.3
  • 40
    • 0001506820 scopus 로고    scopus 로고
    • Evidence of endoplasmic reticulum stress and unfolded protein response in inclusion-body myositis (IBM) muscle
    • Vattemi G, Engel WK, Askanas V: Evidence of endoplasmic reticulum stress and unfolded protein response in inclusion-body myositis (IBM) muscle. Neurology 2002;58:A491.
    • (2002) Neurology , vol.58
    • Vattemi, G.1    Engel, W.K.2    Askanas, V.3
  • 41
    • 0035966320 scopus 로고    scopus 로고
    • The unfolding tale of the unfolded protein response
    • Ma Y, Hendershot LM: The unfolding tale of the unfolded protein response. Cell 2001;107:827-830.
    • (2001) Cell , vol.107 , pp. 827-830
    • Ma, Y.1    Hendershot, L.M.2
  • 42
    • 0029671441 scopus 로고    scopus 로고
    • Transfer of β-amyloid precursor protein gene using adenovirus vector causes mitochondrial abnormalities in cultured normal human muscle
    • Askanas V, McFerrin J, Baque S, et al. Transfer of β-amyloid precursor protein gene using adenovirus vector causes mitochondrial abnormalities in cultured normal human muscle. Proc Natl Acad Sci U S A 1996;93:1314-1319.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 1314-1319
    • Askanas, V.1    McFerrin, J.2    Baque, S.3
  • 43
    • 0030857085 scopus 로고    scopus 로고
    • βAPP gene transfer into cultured human muscle induces inclusion-body myositis aspects
    • Askanas V, McFerrin J, Alvarez RB, et al: βAPP gene transfer into cultured human muscle induces inclusion-body myositis aspects. Neuroreport 1997;8:2155-2158.
    • (1997) Neuroreport , vol.8 , pp. 2155-2158
    • Askanas, V.1    McFerrin, J.2    Alvarez, R.B.3
  • 44
    • 0032487428 scopus 로고    scopus 로고
    • Impaired innervation of cultured human muscle overexpressing βAPP experimentally and genetically: Relevance to inclusion-body myopathies
    • McFerrin J, Engel WK, Askanas V: Impaired innervation of cultured human muscle overexpressing βAPP experimentally and genetically: Relevance to inclusion-body myopathies. Neuroreport 1998;9:3201-3205.
    • (1998) Neuroreport , vol.9 , pp. 3201-3205
    • McFerrin, J.1    Engel, W.K.2    Askanas, V.3
  • 45
    • 0001575898 scopus 로고    scopus 로고
    • Type III hyperlipoproteinemia (dysbetalipoproteinemia): The role of apolipoprotein E in normal and abnormal lipoprotein metabolism
    • Scriver CR, Beaudet AL, Sly WS (eds): 8th ed. New York, McGraw-Hill
    • Mahley RW, Rall SC Jr: Type III hyperlipoproteinemia (dysbetalipoproteinemia): The role of apolipoprotein E in normal and abnormal lipoprotein metabolism, in Scriver CR, Beaudet AL, Sly WS (eds): Metabolic and Molecular Bases of Inheritied Diseases, 8th ed. New York, McGraw-Hill, 2001, 2863-2913.
    • (2001) Metabolic and Molecular Bases of Inheritied Diseases , pp. 2863-2913
    • Mahley, R.W.1    Rall S.C., Jr.2
  • 46
    • 0037065833 scopus 로고    scopus 로고
    • Three lipoprotein receptors and cholesterol in inclusion-body myositis muscle
    • Jaworska-Wilczynska M, Wilczynski GM, Engel WK, et al: Three lipoprotein receptors and cholesterol in inclusion-body myositis muscle. Neurology 2002;58:438-445.
    • (2002) Neurology , vol.58 , pp. 438-445
    • Jaworska-Wilczynska, M.1    Wilczynski, G.M.2    Engel, W.K.3
  • 47
    • 0001506819 scopus 로고    scopus 로고
    • Abnormal accumulation of caveolin-1 and its co-localization with cholesterol, amyloid-β and phosphorylated tau in inclusion-body myositis (IBM) muscle
    • Kefi M, Vattemi G, Engel WK, et al: Abnormal accumulation of caveolin-1 and its co-localization with cholesterol, amyloid-β and phosphorylated tau in inclusion-body myositis (IBM) muscle. Neurology 2002;58:A391.
    • (2002) Neurology , vol.58
    • Kefi, M.1    Vattemi, G.2    Engel, W.K.3
  • 48
    • 0034672717 scopus 로고    scopus 로고
    • Cholesterol and caveolae: Structural and functional relationships
    • Fielding CJ, Fielding PE: Cholesterol and caveolae: Structural and functional relationships. Biochem Biophys Acta 2000;1529:210-222.
    • (2000) Biochem. Biophys. Acta , vol.1529 , pp. 210-222
    • Fielding, C.J.1    Fielding, P.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.