메뉴 건너뛰기




Volumn 22, Issue 1, 2012, Pages 26-33

Heat shock protein families 70 and 90 in Duchenne muscular dystrophy and inflammatory myopathy: Balancing muscle protection and destruction

Author keywords

Duchenne muscular dystrophy; Heat shock proteins; Inflammatory myopathy

Indexed keywords

CHAPERONE; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90;

EID: 84855987288     PISSN: 09608966     EISSN: 18732364     Source Type: Journal    
DOI: 10.1016/j.nmd.2011.07.007     Document Type: Article
Times cited : (31)

References (38)
  • 1
    • 0027328535 scopus 로고
    • Heat-shock proteins: molecular chaperones of protein biogenesis
    • Craig E.A., Gambill B.D., Nelson R.J. Heat-shock proteins: molecular chaperones of protein biogenesis. Mol Cell Biol 1993, 13:5637-5646.
    • (1993) Mol Cell Biol , vol.13 , pp. 5637-5646
    • Craig, E.A.1    Gambill, B.D.2    Nelson, R.J.3
  • 2
    • 11244306423 scopus 로고    scopus 로고
    • Exercise raises serum heat-shock protein 70 (Hsp70) levels
    • Banfi G., Dolci A., Verna R., et al. Exercise raises serum heat-shock protein 70 (Hsp70) levels. Clin Chem Lab Med 2004, 42:1445-1446.
    • (2004) Clin Chem Lab Med , vol.42 , pp. 1445-1446
    • Banfi, G.1    Dolci, A.2    Verna, R.3
  • 3
    • 24744442576 scopus 로고    scopus 로고
    • Heat shock protein 60 activates B cells via the TLR4-MyD88 pathway
    • Cohen-Sfady M., Nussbaum G., Pevsner-Fischer M., et al. Heat shock protein 60 activates B cells via the TLR4-MyD88 pathway. J Immunol 2005, 175:3594-3602.
    • (2005) J Immunol , vol.175 , pp. 3594-3602
    • Cohen-Sfady, M.1    Nussbaum, G.2    Pevsner-Fischer, M.3
  • 4
    • 27944442354 scopus 로고    scopus 로고
    • The heat shock protein Hsp70 enhances antigen-specific proliferation of human CD4+ memory T cells
    • Haug M., Dannecker L., Schepp C.P., et al. The heat shock protein Hsp70 enhances antigen-specific proliferation of human CD4+ memory T cells. Eur J Immunol 2005, 35:3163-3172.
    • (2005) Eur J Immunol , vol.35 , pp. 3163-3172
    • Haug, M.1    Dannecker, L.2    Schepp, C.P.3
  • 5
    • 0035007710 scopus 로고    scopus 로고
    • The role of heat shock protein (hsp70) in dendritic cell maturation: hsp70 induces the maturation of immature dendritic cells but reduces DC differentiation from monocyte precursors
    • Kuppner M.C., Gastpar R., Gelwer S., et al. The role of heat shock protein (hsp70) in dendritic cell maturation: hsp70 induces the maturation of immature dendritic cells but reduces DC differentiation from monocyte precursors. Eur J Immunol 2001, 31:1602-1609.
    • (2001) Eur J Immunol , vol.31 , pp. 1602-1609
    • Kuppner, M.C.1    Gastpar, R.2    Gelwer, S.3
  • 6
    • 0034608387 scopus 로고    scopus 로고
    • Cross-presentation of glycoprotein 96-associated antigens on major histocompatibility complex class I molecules requires receptor-mediated endocytosis
    • Singh-Jasuja H. Cross-presentation of glycoprotein 96-associated antigens on major histocompatibility complex class I molecules requires receptor-mediated endocytosis. J Exp Med 2000, 191:1965-1974.
    • (2000) J Exp Med , vol.191 , pp. 1965-1974
    • Singh-Jasuja, H.1
  • 7
    • 0036214288 scopus 로고    scopus 로고
    • Interaction of heat shock proteins with peptides and antigen presenting cells: chaperoning of the innate and adaptive immune responses
    • Srivastava P. Interaction of heat shock proteins with peptides and antigen presenting cells: chaperoning of the innate and adaptive immune responses. Annu Rev Immunol 2002, 20:395-425.
    • (2002) Annu Rev Immunol , vol.20 , pp. 395-425
    • Srivastava, P.1
  • 8
    • 0034113617 scopus 로고    scopus 로고
    • HSP70 stimulates cytokine production through a CD14-dependent pathway, demonstrating its dual role as a chaperone and cytokine
    • Asea A., Kraeft S.K., Kurt-Jones E.A., et al. HSP70 stimulates cytokine production through a CD14-dependent pathway, demonstrating its dual role as a chaperone and cytokine. Nat Med 2000, 6:435-442.
    • (2000) Nat Med , vol.6 , pp. 435-442
    • Asea, A.1    Kraeft, S.K.2    Kurt-Jones, E.A.3
  • 9
    • 61549130869 scopus 로고    scopus 로고
    • Heat-shock proteins can promote as well as regulate autoimmunity
    • Rajaiah R., Moudgil K.D. Heat-shock proteins can promote as well as regulate autoimmunity. Autoimm Rev 2009, 8:388-393.
    • (2009) Autoimm Rev , vol.8 , pp. 388-393
    • Rajaiah, R.1    Moudgil, K.D.2
  • 10
  • 11
    • 0031793127 scopus 로고    scopus 로고
    • Heat shock protein 70kDa: molecular biology, biochemistry, and physiology
    • 183-20
    • Kiang J.G., Tsokos G.C. Heat shock protein 70kDa: molecular biology, biochemistry, and physiology. Pharmacol Ther 1998, 80. 183-20.
    • (1998) Pharmacol Ther , vol.80
    • Kiang, J.G.1    Tsokos, G.C.2
  • 12
  • 13
    • 0031873752 scopus 로고    scopus 로고
    • The 90-kDa molecular chaperone family: structure, function, and clinical applications. A comprehensive review
    • Csermely P., Schnaider T., Soti C., et al. The 90-kDa molecular chaperone family: structure, function, and clinical applications. A comprehensive review. Pharmacol Ther 1998, 79:129-168.
    • (1998) Pharmacol Ther , vol.79 , pp. 129-168
    • Csermely, P.1    Schnaider, T.2    Soti, C.3
  • 14
    • 0034892432 scopus 로고    scopus 로고
    • Hsp90: chaperoning signal transduction
    • Richter K., Buchner J. Hsp90: chaperoning signal transduction. J Cell Physiol 2001, 188:281-290.
    • (2001) J Cell Physiol , vol.188 , pp. 281-290
    • Richter, K.1    Buchner, J.2
  • 15
    • 33947258069 scopus 로고    scopus 로고
    • Pathophysiology of Duchenne muscular dystrophy: current hypotheses
    • Deconinck N., Dan B. Pathophysiology of Duchenne muscular dystrophy: current hypotheses. Pediatr Neurol 2007, 36:1-7.
    • (2007) Pediatr Neurol , vol.36 , pp. 1-7
    • Deconinck, N.1    Dan, B.2
  • 16
    • 0025081106 scopus 로고
    • Nature of the mononuclear infiltrate and the mechanism of muscle damage in juvenile dermatomyositis and Duchenne muscular dystrophy
    • McDouall R.M., Dunn M.J., Dubowitz V. Nature of the mononuclear infiltrate and the mechanism of muscle damage in juvenile dermatomyositis and Duchenne muscular dystrophy. J Neurol Sci 1990, 99:199-217.
    • (1990) J Neurol Sci , vol.99 , pp. 199-217
    • McDouall, R.M.1    Dunn, M.J.2    Dubowitz, V.3
  • 17
    • 66949145779 scopus 로고    scopus 로고
    • Inclusion body myositis: a degenerative muscle disease associated with intra-muscle fiber multi-protein aggregates, proteasome inhibition, endoplasmic reticulum stress and decreased lysosomal degradation
    • Askanas V., Engel W.K., 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 2009, 19:493-506.
    • (2009) Brain Pathol , vol.19 , pp. 493-506
    • Askanas, V.1    Engel, W.K.2    Nogalska, A.3
  • 18
    • 0034646141 scopus 로고    scopus 로고
    • Alpha-B-crystallin immunolocalization yields new insights into inclusion body myositis
    • Banwell B.L., Engel A.G. Alpha-B-crystallin immunolocalization yields new insights into inclusion body myositis. Neurology 2000, 54:1033-1041.
    • (2000) Neurology , vol.54 , pp. 1033-1041
    • Banwell, B.L.1    Engel, A.G.2
  • 19
    • 0026451989 scopus 로고
    • Expression of 65-kd heat shock proteins in the inflammatory myopathies
    • Hohlfeld R., Engel A.G. Expression of 65-kd heat shock proteins in the inflammatory myopathies. Ann Neurol 1992, 32:821-823.
    • (1992) Ann Neurol , vol.32 , pp. 821-823
    • Hohlfeld, R.1    Engel, A.G.2
  • 20
    • 0029593556 scopus 로고
    • Expression of the heat shock protein 70 in inflammatory myopathies
    • Ibi T. Expression of the heat shock protein 70 in inflammatory myopathies. Rinsho Shinkeigaku 1995, 35:1163-1166.
    • (1995) Rinsho Shinkeigaku , vol.35 , pp. 1163-1166
    • Ibi, T.1
  • 21
    • 0029926776 scopus 로고    scopus 로고
    • Heat shock protein 90 and ubiquitin: developmental regulation during myogenesis
    • Bornmann L., Polla B.S., Gericke G.S. Heat shock protein 90 and ubiquitin: developmental regulation during myogenesis. Muscle Nerve 1996, 19:574-580.
    • (1996) Muscle Nerve , vol.19 , pp. 574-580
    • Bornmann, L.1    Polla, B.S.2    Gericke, G.S.3
  • 22
    • 0028813406 scopus 로고
    • Expression of heat-shock/stress proteins in Duchenne muscular dystrophy
    • Bornmann L., Gericke G.S., Polla B.S., et al. Expression of heat-shock/stress proteins in Duchenne muscular dystrophy. Muscle Nerve 1995, 18:23-31.
    • (1995) Muscle Nerve , vol.18 , pp. 23-31
    • Bornmann, L.1    Gericke, G.S.2    Polla, B.S.3
  • 23
    • 85044098375 scopus 로고    scopus 로고
    • A dual role for HSP90 and HSP70 in the inflammatory myopathies: from muscle fiber protection to active invasion by macrophages
    • De Paepe B., Creus K.K., Martin J.J., et al. A dual role for HSP90 and HSP70 in the inflammatory myopathies: from muscle fiber protection to active invasion by macrophages. Ann NY Acad Sci 2009, 1109:441-453.
    • (2009) Ann NY Acad Sci , vol.1109 , pp. 441-453
    • De Paepe, B.1    Creus, K.K.2    Martin, J.J.3
  • 24
    • 0141651951 scopus 로고    scopus 로고
    • Polymyositis and dermatomyositis
    • Dalakas M.C., Hohlfeld R. Polymyositis and dermatomyositis. Lancet 2003, 362:971-982.
    • (2003) Lancet , vol.362 , pp. 971-982
    • Dalakas, M.C.1    Hohlfeld, R.2
  • 25
    • 0024462566 scopus 로고
    • Diminished heat-shock protein synthesis following mitogen stimulation of lymphocytes from aged donors
    • Faasen A.E. Diminished heat-shock protein synthesis following mitogen stimulation of lymphocytes from aged donors. Exp Cell Res 1989, 183:326-334.
    • (1989) Exp Cell Res , vol.183 , pp. 326-334
    • Faasen, A.E.1
  • 26
    • 34547665165 scopus 로고    scopus 로고
    • Heat shock proteins and chemokine/cytokine secretion profile in ageing and inflammation
    • Njemini R., Bautmans I., Lambert M., et al. Heat shock proteins and chemokine/cytokine secretion profile in ageing and inflammation. Mech Age Develop 2007, 128:450-454.
    • (2007) Mech Age Develop , vol.128 , pp. 450-454
    • Njemini, R.1    Bautmans, I.2    Lambert, M.3
  • 27
    • 33845918172 scopus 로고    scopus 로고
    • Heat shock proteins 70 and 90 inhibit early stages of amyloid beta-(1-42) aggregation in vitro
    • Evans C.G., Wisen S., Gestwicki J.E. Heat shock proteins 70 and 90 inhibit early stages of amyloid beta-(1-42) aggregation in vitro. J Biol Chem 2006, 281:33182-33191.
    • (2006) J Biol Chem , vol.281 , pp. 33182-33191
    • Evans, C.G.1    Wisen, S.2    Gestwicki, J.E.3
  • 29
    • 3242681674 scopus 로고    scopus 로고
    • Expression and distribution of the nitric oxide synthases in idiopathic inflammatory myopathies
    • De Paepe B., Racz G.Z., Schröder J.M., et al. Expression and distribution of the nitric oxide synthases in idiopathic inflammatory myopathies. Acta Neuropathol 2004, 108:37-42.
    • (2004) Acta Neuropathol , vol.108 , pp. 37-42
    • De Paepe, B.1    Racz, G.Z.2    Schröder, J.M.3
  • 30
    • 0141480200 scopus 로고    scopus 로고
    • Heat shock protein 90 as an endogenous protein enhancer of inducible nitric-oxide synthase
    • Yoshida M., Xia Y. Heat shock protein 90 as an endogenous protein enhancer of inducible nitric-oxide synthase. J Biol Chem 2003, 278:36953-36958.
    • (2003) J Biol Chem , vol.278 , pp. 36953-36958
    • Yoshida, M.1    Xia, Y.2
  • 31
    • 0037172893 scopus 로고    scopus 로고
    • Differential expression of chemokines in inflammatory myopathies
    • De Bleecker J.L., De Paepe B., Vanwalleghem I.E., et al. Differential expression of chemokines in inflammatory myopathies. Neurology 2002, 58:1779-1785.
    • (2002) Neurology , vol.58 , pp. 1779-1785
    • De Bleecker, J.L.1    De Paepe, B.2    Vanwalleghem, I.E.3
  • 32
    • 23844442104 scopus 로고    scopus 로고
    • CXC chemokines: a new family of heat-shock proteins?
    • Nagarsekar A., Hasday J.D., Singh I.S. CXC chemokines: a new family of heat-shock proteins?. Immunol Invest 2005, 34:381-398.
    • (2005) Immunol Invest , vol.34 , pp. 381-398
    • Nagarsekar, A.1    Hasday, J.D.2    Singh, I.S.3
  • 33
    • 22144433678 scopus 로고    scopus 로고
    • Alpha-chemokine receptors CXCR1-3 and their ligands in idiopathic inflammatory myopathies
    • De Paepe B., De Keyzer K., Martin J.J., et al. Alpha-chemokine receptors CXCR1-3 and their ligands in idiopathic inflammatory myopathies. Acta Neuropathol 2005, 109:576-582.
    • (2005) Acta Neuropathol , vol.109 , pp. 576-582
    • De Paepe, B.1    De Keyzer, K.2    Martin, J.J.3
  • 34
    • 62949238913 scopus 로고    scopus 로고
    • New developments in hsp90 inhibitors as anti-cancer therapeutics: mechanisms, clinical perspective and more potential
    • Li Y., Zhang T., Schwartz S.J. New developments in hsp90 inhibitors as anti-cancer therapeutics: mechanisms, clinical perspective and more potential. Drug Resist Updates 2009, 19:17-27.
    • (2009) Drug Resist Updates , vol.19 , pp. 17-27
    • Li, Y.1    Zhang, T.2    Schwartz, S.J.3
  • 35
    • 34848829167 scopus 로고    scopus 로고
    • Heat shock protein 90 inhibitors prolong survival, attenuate inflammation, and reduce lung injury in murine sepsis
    • Chatterjee A., Dimitropoulou C., Drakopanayiotakis F., et al. Heat shock protein 90 inhibitors prolong survival, attenuate inflammation, and reduce lung injury in murine sepsis. Am J Respir Crit Care Med 2007, 176:667-675.
    • (2007) Am J Respir Crit Care Med , vol.176 , pp. 667-675
    • Chatterjee, A.1    Dimitropoulou, C.2    Drakopanayiotakis, F.3
  • 36
    • 33750945303 scopus 로고    scopus 로고
    • The heat shock protein 90 inhibitor 17-allylamino-17-demethoxygeldanamycin suppresses glial inflammatory responses and ameliorates experimental autoimmune encephalomyelitis
    • Dello Russo C., Polak P.E., Mercado P.R., et al. The heat shock protein 90 inhibitor 17-allylamino-17-demethoxygeldanamycin suppresses glial inflammatory responses and ameliorates experimental autoimmune encephalomyelitis. J Neurochem 2006, 99:1351-1362.
    • (2006) J Neurochem , vol.99 , pp. 1351-1362
    • Dello Russo, C.1    Polak, P.E.2    Mercado, P.R.3
  • 37
    • 0034921488 scopus 로고    scopus 로고
    • Geldanamycin inhibits NF-kappaB activation and interleukin-8 gene expression in cultured human respiratory epithelium
    • Malhotra V., Shanley T.P., Pittet J.F., et al. Geldanamycin inhibits NF-kappaB activation and interleukin-8 gene expression in cultured human respiratory epithelium. Am J Respir Cell Mol Biol 2001, 25:92-97.
    • (2001) Am J Respir Cell Mol Biol , vol.25 , pp. 92-97
    • Malhotra, V.1    Shanley, T.P.2    Pittet, J.F.3
  • 38
    • 15044350606 scopus 로고    scopus 로고
    • Hsp90 inhibitor geldanamycin increases hsp70 mRNA stabilization but fails to activate HSF1 in cells exposed to hydrostatic pressure
    • Elo M.A., Kaarniranta K., Helminen H.J., et al. Hsp90 inhibitor geldanamycin increases hsp70 mRNA stabilization but fails to activate HSF1 in cells exposed to hydrostatic pressure. Biochim Biophys Acta 2005, 1743:115-119.
    • (2005) Biochim Biophys Acta , vol.1743 , pp. 115-119
    • Elo, M.A.1    Kaarniranta, K.2    Helminen, H.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.