메뉴 건너뛰기




Volumn 1173, Issue , 2009, Pages 463-469

A dual role for HSP90 and HSP70 in the inflammatory myopathies: From muscle fiber protection to active invasion by macrophages

Author keywords

Heat shock proteins; Inflammatory myopathy; Myocytotoxicity; Myoprotection

Indexed keywords

CHAPERONE; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; INDUCIBLE NITRIC OXIDE SYNTHASE;

EID: 70049097249     PISSN: 00778923     EISSN: 17496632     Source Type: Book Series    
DOI: 10.1111/j.1749-6632.2009.04812.x     Document Type: Conference Paper
Times cited : (17)

References (33)
  • 1
    • 0027328535 scopus 로고
    • Heat-shock proteins-Molecular chaperones of protein biogenesis
    • Craig, E.A., B.D. Gambill & R.J. Nelson. 1993. Heat-shock proteins-Molecular chaperones of protein biogenesis. Moll. Cell. Biol. 13: 5637-5646.
    • (1993) Moll. Cell. Biol. , vol.13 , pp. 5637-5646
    • Craig, E.A.1    Gambill, B.D.2    Nelson, R.J.3
  • 2
    • 0030112681 scopus 로고    scopus 로고
    • A hitchhiker's guide to the human Hsp70
    • Tavaria, M. et al. 1996. A hitchhiker's guide to the human Hsp70. Cell. Stress Chaperon. 1: 23-28.
    • (1996) Cell. Stress Chaperon. , vol.1 , pp. 23-28
    • Tavaria, M.1
  • 3
    • 0031793127 scopus 로고    scopus 로고
    • Heat shock protein 70 kDa: Molecular biology, biochemistry, and physiology
    • Kiang, J.G. & G.C. 1998. Heat shock protein 70 kDa: Molecular biology, biochemistry, and physiology. Pharmacol. Ther. 80: 183-201.
    • (1998) Pharmacol. Ther. , vol.80 , pp. 183-201
    • Kiang, J.G.1
  • 4
    • 0028940309 scopus 로고
    • Transient interaction of Hsp90 with early unfolding intermediates of citrate synthase: Implications for heat shock in vivo
    • Jacob, U. et al. 1995. Transient interaction of Hsp90 with early unfolding intermediates of citrate synthase: Implications for heat shock in vivo. J. Biol. Chem. 270: 7288-7294.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7288-7294
    • Jacob, U.1
  • 5
    • 0034892432 scopus 로고    scopus 로고
    • Hsp90: Chaperoning signal transduction
    • Richter, K. & J. Buchner. 2001. Hsp90: chaperoning signal transduction. J. Cell. Physiol. 188: 281-290.
    • (2001) J. Cell. Physiol. , vol.188 , pp. 281-290
    • Richter, K.1    Buchner, J.2
  • 6
    • 0034608387 scopus 로고    scopus 로고
    • Cross-presentation of gly-coprotein 96-associated antigens on major histocom-patibility complex class i molecules requires receptor-mediated endocytosis
    • Singh-Jasuja, H. et al. 2000. Cross-presentation of gly-coprotein 96-associated antigens on major histocom-patibility complex class I molecules requires receptor-mediated endocytosis. J. Exp. Med. 191: 1965-1974.
    • (2000) J. Exp. Med. , vol.191 , pp. 1965-1974
    • Singh-Jasuja, H.1
  • 7
    • 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. et al. 2001. 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. 31: 1602-1609.
    • (2001) Eur. J. Immunol. , vol.31 , pp. 1602-1609
    • Kuppner, M.C.1
  • 8
    • 0034113617 scopus 로고    scopus 로고
    • HSP70 stimulates cytokine production through a CD14-dependent pathway, demonstrating its dual role as a chaperone and cy-tokine
    • Asea, A. et al. 2000. HSP70 stimulates cytokine production through a CD14-dependent pathway, demonstrating its dual role as a chaperone and cy-tokine. Nat. Med. 6: 435-442.
    • (2000) Nat. Med. , vol.6 , pp. 435-442
    • Asea, A.1
  • 9
    • 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. 2002. Interaction of heat shock proteins with peptides and antigen presenting cells: chaperoning of the innate and adaptive immune responses. Annu. Rev. Immunol. 20: 395-425.
    • (2002) Annu. Rev. Immunol. , vol.20 , pp. 395-425
    • Srivastava, P.1
  • 10
    • 27944442354 scopus 로고    scopus 로고
    • The heat shock protein Hsp70 enhances antigen-specific proliferation of human CD4+ memory T cells
    • Haug, M. et al. 2005. The heat shock protein Hsp70 enhances antigen-specific proliferation of human CD4+ memory T cells. Eur. J. Immunol. 35: 3163-3172.
    • (2005) Eur. J. Immunol. , vol.35 , pp. 3163-3172
    • Haug, M.1
  • 11
    • 24744442576 scopus 로고    scopus 로고
    • Heat shock protein 60 activates B cells via the TLR4-MyD88 pathway
    • Cohen-Sfady, M. et al. 2005. Heat shock protein 60 activates B cells via the TLR4-MyD88 pathway. J. Immunol. 175: 3594-3602.
    • (2005) J. Immunol. , vol.175 , pp. 3594-3602
    • Cohen-Sfady, M.1
  • 12
    • 34948816592 scopus 로고    scopus 로고
    • Inclusion-body myositis, a multifactorial muscle disease associated with aging: Current concepts of pathogenesis
    • Askanas, V. & W.K. Engel. 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
  • 13
    • 32644472178 scopus 로고    scopus 로고
    • The idio-pathic inflammatory myopathies
    • De Bleecker, J.L. & B. De Paepe. 2003. The idio-pathic inflammatory myopathies. Adv. Clin. Neurosc. 13: 353-378.
    • (2003) Adv. Clin. Neurosc. , vol.13 , pp. 353-378
    • De Bleecker, L.J.1    De Paepe, B.2
  • 14
    • 0029926776 scopus 로고    scopus 로고
    • Heat shock protein 90 and ubiquitin: Developmental regulation during myogenesis
    • Bornmann, L., B.S. Polla & G.S. Gericke. 1996. Heat shock protein 90 and ubiquitin: developmental regulation during myogenesis. Muscle Nerve 19: 574-580.
    • (1996) Muscle Nerve , vol.19 , pp. 574-580
    • Bornmann, L.1    Polla, B.S.2    Gericke, G.S.3
  • 15
    • 70049118677 scopus 로고
    • Expression of heat-shock/stress proteins in Duchenne muscular dystrophy
    • Bornmann, L. et al. 1995. Expression of heat-shock/stress proteins in Duchenne muscular dystrophy. Muscle Nerve 19: 574-580.
    • (1995) Muscle Nerve , vol.19 , pp. 574-580
    • Bornmann, L.1
  • 16
    • 24144489814 scopus 로고    scopus 로고
    • Proteasome inhibition and ag-gresome formation in sporadic inclusion-body myosi-tis and in amyloid-b precursor protein-overexpressing cultured human muscle fibers
    • Fratta, P. et al. 2005. Proteasome inhibition and ag-gresome formation in sporadic inclusion-body myosi-tis and in amyloid-b 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
  • 17
    • 0029593556 scopus 로고
    • Expression of the heat shock protein 70 in inflammatory myopathies
    • Ibi, T. et al. 1995. Expression of the heat shock protein 70 in inflammatory myopathies. Rinsho Shinkeigaku 35: 1163-1166.
    • (1995) Rinsho Shinkeigaku , vol.35 , pp. 1163-1166
    • Ibi, T.1
  • 18
    • 70049107335 scopus 로고    scopus 로고
    • HSP70 inhibits NFkB activation and IkB phosphorylation following experimental stroke
    • Zheng, Z. et al. 2005. HSP70 inhibits NFkB activation and IkB phosphorylation following experimental stroke. Neurology 64: A180.
    • (2005) Neurology , vol.64
    • Zheng, Z.1
  • 19
    • 67349116153 scopus 로고    scopus 로고
    • The distribution of NF-κB and its inhibitor in the idiopathic inflammatory myopathies
    • III/10
    • De Bleecker, J.L., K.K. Creus & B. De Paepe. 2007. The distribution of NF-κB and its inhibitor in the idiopathic inflammatory myopathies. J. Neurol. 254: III/10.
    • (2007) J. Neurol. , vol.254
    • De Bleecker, J.L.1    Creus, K.K.2    De Paepe, B.3
  • 20
    • 0034921488 scopus 로고    scopus 로고
    • Geldanamycin inhibits NF-kappaB activation and interleukin-8 gene expression in cultured human respiratory epithelium
    • Malhotra, V. et al. 2001. Geldanamycin inhibits NF-kappaB activation and interleukin-8 gene expression in cultured human respiratory epithelium. Am. J. Respir. Cell. Mol. Biol. 25: 92-97.
    • (2001) Am. J. Respir. Cell. Mol. Biol. , vol.25 , pp. 92-97
    • Malhotra, V.1
  • 21
    • 10044259729 scopus 로고    scopus 로고
    • Heat shock protein 70 confers cardiovascular protection during endotoxemia via inhibition of nuclear factor-kB activation and in-ducible nitric oxide synthase expression in the rostral ventrolateral medulla
    • Chan, J.Y.H. et al. 2004. Heat shock protein 70 confers cardiovascular protection during endotoxemia via inhibition of nuclear factor-kB activation and in-ducible nitric oxide synthase expression in the rostral ventrolateral medulla. Circulation 110: 3560-3566.
    • (2004) Circulation , vol.110 , pp. 3560-3566
    • Chan, J.Y.H.1
  • 22
    • 0141480200 scopus 로고    scopus 로고
    • Heat shock protein 90 as an endogenous protein enhancer of inducible nitric-oxide synthase
    • Yoshida, M. & Y. Xia. 2003. Heat shock protein 90 as an endogenous protein enhancer of inducible nitric-oxide synthase. J. Biol. Chem. 278: 36953-36958.
    • (2003) J. Biol. Chem. , vol.278 , pp. 36953-36958
    • Yoshida, M.1    Xia, Y.2
  • 23
    • 0037013152 scopus 로고    scopus 로고
    • Domain mapping studies reveal that the M domain of hsp90 serves as a molecular scaffold to regulate Akt-dependent phosphorylation of endothelial nitric oxide synthase and NO release
    • Fontana, J. et al. 2002. Domain mapping studies reveal that the M domain of hsp90 serves as a molecular scaffold to regulate Akt-dependent phosphorylation of endothelial nitric oxide synthase and NO release. Circ. Res. 90: 866-873.
    • (2002) Circ. Res. , vol.90 , pp. 866-873
    • Fontana, J.1
  • 24
    • 0035871194 scopus 로고    scopus 로고
    • Determination of the enhancing action of HSP90 on neuronal nitric oxide synthase by EPR spectroscopy
    • Song, Y., J.L. Zweier & Y. Xia. 2001. Determination of the enhancing action of HSP90 on neuronal nitric oxide synthase by EPR spectroscopy. Biochem. J. 355: 357-360.
    • (2001) Biochem. J. , vol.355 , pp. 357-360
    • Song, Y.1    Zweier, J.L.2    Xia, Y.3
  • 25
    • 0031800036 scopus 로고    scopus 로고
    • Cell death and oxidative damage in inflammatory myopathies
    • Tews, D.S. & H.H. Goebel. 1998. Cell death and oxidative damage in inflammatory myopathies. Clin. Immunol. Immunopathol. 87: 240-247.
    • (1998) Clin. Immunol. Immunopathol. , vol.87 , pp. 240-247
    • Tews, D.S.1    Goebel, H.H.2
  • 26
    • 3242681674 scopus 로고    scopus 로고
    • Expression and distribution of the nitric oxide synthases in idiopathic inflammatory myopathies
    • De Paepe, B. et al. 2004. Expression and distribution of the nitric oxide synthases in idiopathic inflammatory myopathies. Acta Neuropathol. 108: 37-42.
    • (2004) Acta Neuropathol. , vol.108 , pp. 37-42
    • De Paepe, B.1
  • 27
    • 38449097099 scopus 로고    scopus 로고
    • Chemokines in idiopathic inflammatory myopathies
    • De Paepe, B., K.K. Creus & J.L. De Bleecker. 2008. Chemokines in idiopathic inflammatory myopathies. Front. Biosci. 13: 2548-2577.
    • (2008) Front. Biosci. , vol.13 , pp. 2548-2577
    • De Paepe, B.1    Creus, K.K.2    Bleecker De, J.L.3
  • 28
    • 23844442104 scopus 로고    scopus 로고
    • CXC chemokines: A new family of heat-shock proteins?
    • Nagarsekar, A. & J.D. Hasday, I.S. 2005. CXC chemokines: a new family of heat-shock proteins? Immunol. Invest. 34: 381-398.
    • (2005) Immunol. Invest. , vol.34 , pp. 381-398
    • Nagarsekar, A.1    Hasday, J.D.2
  • 29
    • 22144433678 scopus 로고    scopus 로고
    • Alpha-chemokine receptors CXCR1-3 and their ligands in idiopathic inflammatory myopathies
    • De Paepe, B. et al. 2005. Alpha-chemokine receptors CXCR1-3 and their ligands in idiopathic inflammatory myopathies. Acta Neuropathol. 109: 576-582.
    • (2005) Acta Neuropathol. , vol.109 , pp. 576-582
    • De Paepe, B.1
  • 30
    • 34347380341 scopus 로고    scopus 로고
    • Inhibition of Hsp90 attenuates inflammation in endotoxin-induced uveitis
    • Poulaki, V. et al. 2007. Inhibition of Hsp90 attenuates inflammation in endotoxin-induced uveitis. FA S E B J. 21: 2113-2123.
    • (2007) FASEBJ. , vol.21 , pp. 2113-2123
    • Poulaki, V.1
  • 31
    • 33746724745 scopus 로고    scopus 로고
    • Modulation of Hsp90 function in neurodegenerative disorders: A molecular-targeted therapy against disease-causing protein
    • Waza, M. et al. 2006. Modulation of Hsp90 function in neurodegenerative disorders: a molecular-targeted therapy against disease-causing protein. J. Mol. Med. 84: 635-646.
    • (2006) J. Mol. Med. , vol.84 , pp. 635-646
    • Waza, M.1
  • 32
    • 0025744556 scopus 로고
    • Uehara Y, Yamamoto C, Fukazawa H, Mizuno S. Induction of hsp72/73 by herbimycin A, an inhibitor of transformation by tyro-sine kinase oncogenes
    • Murakami, Y. et al. 1991. Uehara Y, Yamamoto C, Fukazawa H, Mizuno S. Induction of hsp72/73 by herbimycin A, an inhibitor of transformation by tyro-sine kinase oncogenes. Exp. Cell. Res. 195: 338-344.
    • (1991) Exp. Cell. Res. , vol.195 , pp. 338-344
    • Murakami, Y.1
  • 33
    • 1442290124 scopus 로고    scopus 로고
    • Overexpression of HSP70 in mouse skeletal muscle protects against muscle damage and age-related muscle dysfunction
    • McArdle, A. et al. 2004. Overexpression of HSP70 in mouse skeletal muscle protects against muscle damage and age-related muscle dysfunction. FA S E B J. 18: 355-357.
    • (2004) FASEBJ. , vol.18 , pp. 355-357
    • McArdle, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.