메뉴 건너뛰기




Volumn 16, Issue 12, 2006, Pages 839-844

AβPP-overexpression and proteasome inhibition increase αB-crystallin in cultured human muscle: Relevance to inclusion-body myositis

Author keywords

B Crystallin; Amyloid ; Amyloid precursor protein; Cultured human muscle fibers; Inclusion body myositis

Indexed keywords

ALPHA CRYSTALLIN; AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; EPOXOMICIN; OLIGOMER; PROTEASOME; OLIGOPEPTIDE;

EID: 33845217281     PISSN: 09608966     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.nmd.2006.08.009     Document Type: Article
Times cited : (33)

References (32)
  • 1
    • 33644850570 scopus 로고    scopus 로고
    • Inclusion-body myositis: clinical, diagnostic, and pathologic aspects
    • Engel W.K., and Askanas V. Inclusion-body myositis: clinical, diagnostic, and pathologic aspects. Neurology 66 (2006) S20-S29
    • (2006) Neurology , vol.66
    • Engel, W.K.1    Askanas, V.2
  • 2
    • 33644869497 scopus 로고    scopus 로고
    • Inclusion-body myositis. A myodegenerative conformational disorder associated with Aβ, protein misfolding, and proteasome inhibition
    • Askanas V., and Engel W.K. Inclusion-body myositis. A myodegenerative conformational disorder associated with Aβ, protein misfolding, and proteasome inhibition. Neurology 66 (2006) S39-S48
    • (2006) Neurology , vol.66
    • Askanas, V.1    Engel, W.K.2
  • 3
    • 33644848845 scopus 로고    scopus 로고
    • Inflammatory, immune, and viral aspects of inclusion-body myositis
    • Dalakas M.C. Inflammatory, immune, and viral aspects of inclusion-body myositis. Neurology 66 (2006) S33-S38
    • (2006) Neurology , vol.66
    • Dalakas, M.C.1
  • 4
    • 24144489814 scopus 로고    scopus 로고
    • Proteasome inhibition and aggresome formation in sporadic inclusion-body myositis and in amyloid-beta precursor protein-overexpressing cultured human muscle fibers
    • Fratta P., Engel W.K., McFerrin J., Davies K.J., Lin S.W., and Askanas V. Proteasome inhibition and aggresome formation in sporadic inclusion-body myositis and in amyloid-beta precursor protein-overexpressing cultured human muscle fibers. Am J Pathol 167 (2005) 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
  • 5
    • 0029671441 scopus 로고    scopus 로고
    • Transfer of beta-amyloid precursor protein gene using adenovirus vector causes mitochondrial abnormalities in cultured normal human muscle
    • Askanas V., McFerrin J., Baque S., Alvarez R.B., Sarkozi E., and Engel W.K. Transfer of beta-amyloid precursor protein gene using adenovirus vector causes mitochondrial abnormalities in cultured normal human muscle. Proc Natl Acad Sci USA 93 (1996) 1314-1319
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 1314-1319
    • Askanas, V.1    McFerrin, J.2    Baque, S.3    Alvarez, R.B.4    Sarkozi, E.5    Engel, W.K.6
  • 6
    • 0030857085 scopus 로고    scopus 로고
    • βAPP gene transfer into cultured human muscle induces inclusion-body myositis aspects
    • Askanas V., McFerrin J., Alvarez R.B., Baque S., and Engel W.K. βAPP gene transfer into cultured human muscle induces inclusion-body myositis aspects. Neuroreport 8 (1997) 2155-2158
    • (1997) Neuroreport , vol.8 , pp. 2155-2158
    • Askanas, V.1    McFerrin, J.2    Alvarez, R.B.3    Baque, S.4    Engel, W.K.5
  • 7
    • 0032487428 scopus 로고    scopus 로고
    • Impaired innervation of cultured human muscle overexpressing βAPP experimentally and genetically: Relevance to inclusion-body myopathies
    • McFerrin J., Engel W.K., and Askanas V. Impaired innervation of cultured human muscle overexpressing βAPP experimentally and genetically: Relevance to inclusion-body myopathies. Neuroreport 9 (1998) 201-205
    • (1998) Neuroreport , vol.9 , pp. 201-205
    • McFerrin, J.1    Engel, W.K.2    Askanas, V.3
  • 8
    • 0031740915 scopus 로고    scopus 로고
    • Transgenic mice over-expressing the C-99 fragment of AβPP with an alpha-secretase site mutation develop a myopathy similar to human inclusion body myositis
    • Jin L.W., Hearn M.G., Ogburn C.E., et al. Transgenic mice over-expressing the C-99 fragment of AβPP with an alpha-secretase site mutation develop a myopathy similar to human inclusion body myositis. Am J Pathol 153 (1998) 1679-1686
    • (1998) Am J Pathol , vol.153 , pp. 1679-1686
    • Jin, L.W.1    Hearn, M.G.2    Ogburn, C.E.3
  • 9
    • 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., Li L., and Lindsey J.R. Amyloid-beta deposition in skeletal muscle of transgenic mice: possible model of inclusion body myopathy. Am J Pathol 153 (1998) 1687-1693
    • (1998) Am J Pathol , vol.153 , pp. 1687-1693
    • Fukuchi, K.1    Pham, D.2    Hart, M.3    Li, L.4    Lindsey, J.R.5
  • 10
    • 0037197835 scopus 로고    scopus 로고
    • Inclusion body myositis-like phenotype induced by transgenic overexpression of bAPP in skeletal muscle
    • Sugarman M.C., Yamasaki T.R., Oddo S., et al. Inclusion body myositis-like phenotype induced by transgenic overexpression of bAPP in skeletal muscle. Proc Natl Acad Sci USA 99 (2002) 6334-6339
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 6334-6339
    • Sugarman, M.C.1    Yamasaki, T.R.2    Oddo, S.3
  • 11
    • 0038796242 scopus 로고    scopus 로고
    • Transthyretin Val122Ile, accumulated Aβ and inclusion-body myositis aspects in cultured muscle
    • Askanas V., Engel W.K., McFerrin J., and Vattemi G. Transthyretin Val122Ile, accumulated Aβ and inclusion-body myositis aspects in cultured muscle. Neurology 22 61 (2003) 257-260
    • (2003) Neurology , vol.22 , Issue.61 , pp. 257-260
    • Askanas, V.1    Engel, W.K.2    McFerrin, J.3    Vattemi, G.4
  • 12
    • 0036173420 scopus 로고    scopus 로고
    • ADDLs and protofibrils: the missing links?
    • Klein W.L. ADDLs and protofibrils: the missing links?. Neurobiol Aging 23 (2002) 231-235
    • (2002) Neurobiol Aging , vol.23 , pp. 231-235
    • Klein, W.L.1
  • 13
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid-β protein potently inhibit hippocampal long-term potentiation in vivo
    • Walsh D.M., Klyubin I., Fadeeva J.V., et al. Naturally secreted oligomers of amyloid-β protein potently inhibit hippocampal long-term potentiation in vivo. Nature 416 (2002) 535-539
    • (2002) Nature , vol.416 , pp. 535-539
    • Walsh, D.M.1    Klyubin, I.2    Fadeeva, J.V.3
  • 14
    • 0037200117 scopus 로고    scopus 로고
    • Oligomeric and fibrillar species of amyloid-beta peptides differentially affect neuronal viability
    • Dahlgren K.N., Manelli A.M., Stine Jr. W.B., Baker L.K., Krafft G.A., and LaDu M.J. Oligomeric and fibrillar species of amyloid-beta peptides differentially affect neuronal viability. J Biol Chem 277 (2002) 32046-32053
    • (2002) J Biol Chem , vol.277 , pp. 32046-32053
    • Dahlgren, K.N.1    Manelli, A.M.2    Stine Jr., W.B.3    Baker, L.K.4    Krafft, G.A.5    LaDu, M.J.6
  • 15
    • 4344688011 scopus 로고    scopus 로고
    • Targeting the neurotoxic species in Alzheimer's disease: inhibitors of Abeta oligomerization
    • De Felice F.G., Vieira M.N., Saraiva L.M., et al. Targeting the neurotoxic species in Alzheimer's disease: inhibitors of Abeta oligomerization. FASEB J 18 (2004) 1366-1372
    • (2004) FASEB J , vol.18 , pp. 1366-1372
    • De Felice, F.G.1    Vieira, M.N.2    Saraiva, L.M.3
  • 16
    • 29044443820 scopus 로고    scopus 로고
    • Physicochemical characteristics of soluble oligomeric Abeta and their pathologic role in Alzheimer's disease
    • Watson D., Castano E., Kokjohn T.A., et al. Physicochemical characteristics of soluble oligomeric Abeta and their pathologic role in Alzheimer's disease. Neurol Res 27 (2005) 869-881
    • (2005) Neurol Res , vol.27 , pp. 869-881
    • Watson, D.1    Castano, E.2    Kokjohn, T.A.3
  • 17
    • 0034646141 scopus 로고    scopus 로고
    • αB-crystallin immunolocalization yields new insights into inclusion body myositis
    • Banwell B.L., and Engel A.G. αB-crystallin immunolocalization yields new insights into inclusion body myositis. Neurology 54 (2000) 1033-1041
    • (2000) Neurology , vol.54 , pp. 1033-1041
    • Banwell, B.L.1    Engel, A.G.2
  • 18
    • 0034646412 scopus 로고    scopus 로고
    • Biologically stressed muscle fibers in sporadic IBM: a clue for the enigmatic etiology?
    • Karpati G., and Hohlfeld R. Biologically stressed muscle fibers in sporadic IBM: a clue for the enigmatic etiology?. Neurology 14 54 (2000) 1020-1021
    • (2000) Neurology , vol.14 , Issue.54 , pp. 1020-1021
    • Karpati, G.1    Hohlfeld, R.2
  • 19
    • 0032986520 scopus 로고    scopus 로고
    • Alpha-crystallin as a molecular chaperone
    • Derham B.K., and Harding J.J. Alpha-crystallin as a molecular chaperone. Prog Retin Eye Res 18 (1999) 463-509
    • (1999) Prog Retin Eye Res , vol.18 , pp. 463-509
    • Derham, B.K.1    Harding, J.J.2
  • 20
    • 20444478694 scopus 로고    scopus 로고
    • The small heat shock proteins and their role in human disease
    • Yu S., and MacRae T.H. The small heat shock proteins and their role in human disease. FEBS Journal 272 (2005) 2613-2627
    • (2005) FEBS Journal , vol.272 , pp. 2613-2627
    • Yu, S.1    MacRae, T.H.2
  • 21
    • 0013499286 scopus 로고
    • Cultured normal and genetically abnormal human muscle
    • Rowland L.P., and Di Mauro S. (Eds), North Holland, Amsterdam
    • Askanas V., and Engel W.K. Cultured normal and genetically abnormal human muscle. In: Rowland L.P., and Di Mauro S. (Eds). The Handbook of Clinical Neurology, Myopathies vol. 18 (1992), North Holland, Amsterdam 85-116
    • (1992) The Handbook of Clinical Neurology, Myopathies , vol.18 , pp. 85-116
    • Askanas, V.1    Engel, W.K.2
  • 22
    • 0033621047 scopus 로고    scopus 로고
    • Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo antiinflammatory activity
    • Meng L., Mohan R., Kwok B.H., Elofsson M., Sin N., and Crews C.M. Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo antiinflammatory activity. Proc Natl Acad Sci USA 96 (1999) 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
  • 23
    • 0038472441 scopus 로고    scopus 로고
    • Cystatin C colocalizes with amyloid-beta and coimmunoprecipitates with amyloid-beta precursor protein in sporadic inclusion-body myositis muscles
    • Vattemi G., Engel W.K., McFerrin J., and Askanas V. Cystatin C colocalizes with amyloid-beta and coimmunoprecipitates with amyloid-beta precursor protein in sporadic inclusion-body myositis muscles. J Neurochem 85 (2003) 1539-1546
    • (2003) J Neurochem , vol.85 , pp. 1539-1546
    • Vattemi, G.1    Engel, W.K.2    McFerrin, J.3    Askanas, V.4
  • 24
    • 1542784578 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and unfolded protein response in inclusion body myositis muscle
    • Vattemi G., Engel W.K., McFerrin J., and Askanas V. Endoplasmic reticulum stress and unfolded protein response in inclusion body myositis muscle. Am J Pathol 164 (2004) 1-7
    • (2004) Am J Pathol , vol.164 , pp. 1-7
    • Vattemi, G.1    Engel, W.K.2    McFerrin, J.3    Askanas, V.4
  • 25
    • 24344458115 scopus 로고    scopus 로고
    • Myostatin is increased and complexes with amyloid-beta within sporadic inclusion-body myositis muscle fibers
    • Wojcik S., Engel W.K., McFerrin J., and Askanas V. Myostatin is increased and complexes with amyloid-beta within sporadic inclusion-body myositis muscle fibers. Acta Neuropathol (Berl) 110 (2005) 173-177
    • (2005) Acta Neuropathol (Berl) , vol.110 , pp. 173-177
    • Wojcik, S.1    Engel, W.K.2    McFerrin, J.3    Askanas, V.4
  • 26
    • 23244456099 scopus 로고    scopus 로고
    • A pilot proteomic study of amyloid precursor interactors in Alzheimer's disease
    • Cottrell B.A., Galvan V., Banwait S., et al. A pilot proteomic study of amyloid precursor interactors in Alzheimer's disease. Ann Neurol 58 (2005) 277-289
    • (2005) Ann Neurol , vol.58 , pp. 277-289
    • Cottrell, B.A.1    Galvan, V.2    Banwait, S.3
  • 27
    • 29644445485 scopus 로고    scopus 로고
    • αB-crystallin, a small heat-shock protein, prevents the amyloid fibril growth of an amyloid-β peptide and beta2 microglobulin
    • Raman B., Ban T., Sakai M., et al. αB-crystallin, a small heat-shock protein, prevents the amyloid fibril growth of an amyloid-β peptide and beta2 microglobulin. Biochem J 392 (2005) 573-581
    • (2005) Biochem J , vol.392 , pp. 573-581
    • Raman, B.1    Ban, T.2    Sakai, M.3
  • 28
    • 0033584258 scopus 로고    scopus 로고
    • The molecular chaperone alphaB-crystallin enhances amyloid beta neurotoxicity
    • Stege G.J., Renkawek K., Overkamp P.S., et al. The molecular chaperone alphaB-crystallin enhances amyloid beta neurotoxicity. Biochem Biophys Res Commun 262 (1999) 152-156
    • (1999) Biochem Biophys Res Commun , vol.262 , pp. 152-156
    • Stege, G.J.1    Renkawek, K.2    Overkamp, P.S.3
  • 29
    • 4944229684 scopus 로고    scopus 로고
    • Transglutaminase catalyzes differential crosslinking of small heat shock proteins and amyloid-β
    • Boros S., Kamps B., Wunderink L., de Bruijin W., de Jong W.W., and Boelens W.C. Transglutaminase catalyzes differential crosslinking of small heat shock proteins and amyloid-β. FEBS Lett 576 (2004) 57-62
    • (2004) FEBS Lett , vol.576 , pp. 57-62
    • Boros, S.1    Kamps, B.2    Wunderink, L.3    de Bruijin, W.4    de Jong, W.W.5    Boelens, W.C.6
  • 30
    • 17344361902 scopus 로고    scopus 로고
    • A missense mutation in the alphaB-crystallin chaperone gene causes a desmin-related myopathy
    • Vicart P., Caron A., Guicheney P., et al. A missense mutation in the alphaB-crystallin chaperone gene causes a desmin-related myopathy. Nat Genet 20 (1998) 92-95
    • (1998) Nat Genet , vol.20 , pp. 92-95
    • Vicart, P.1    Caron, A.2    Guicheney, P.3
  • 31
    • 26444486021 scopus 로고    scopus 로고
    • Reversal of amyloid-induced heart disease in desmin-related cardiomyopathy
    • Sanbe A., Osinska H., Villa C., et al. Reversal of amyloid-induced heart disease in desmin-related cardiomyopathy. Proc Natl Acad Sci USA 102 (2005) 13592-13597
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 13592-13597
    • Sanbe, A.1    Osinska, H.2    Villa, C.3
  • 32
    • 0036239489 scopus 로고    scopus 로고
    • Inhibition of proteasomes induces accumulation, phosphorylation, and recruitment of HSP27 and alphaB-crystallin to aggresomes
    • Ito H., Kamei K., Iwamoto I., et al. Inhibition of proteasomes induces accumulation, phosphorylation, and recruitment of HSP27 and alphaB-crystallin to aggresomes. J Biochem (Tokyo) 131 (2002) 593-603
    • (2002) J Biochem (Tokyo) , vol.131 , pp. 593-603
    • Ito, H.1    Kamei, K.2    Iwamoto, I.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.