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Volumn 594, Issue , 2007, Pages 14-26

The cellular "networking" of mammalian Hsp27 and its functions in the control of protein folding, redox state and apoptosis

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; HEAT SHOCK PROTEIN 27; MESSENGER RNA;

EID: 84934439863     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-0-387-39975-1_2     Document Type: Review
Times cited : (179)

References (122)
  • 1
    • 0016373748 scopus 로고
    • Protein synthesis in salivary glands of Drosophila melanogaster: Relation to chromosome puffs
    • Tissieres A, Mitchell H, Tracy U. Protein synthesis in salivary glands of Drosophila melanogaster: Relation to chromosome puffs. J Mol Biol 1974; 84:389-398.
    • (1974) J Mol Biol , vol.84 , pp. 389-398
    • Tissieres, A.1    Mitchell, H.2    Tracy, U.3
  • 2
    • 0027472047 scopus 로고    scopus 로고
    • de Jong W, Leunissen J, Voorter C. Evolution of the alpha-crystallin/ small heat-shock protein family. Moi Biol Evol 1993; 10:103-126.
    • de Jong W, Leunissen J, Voorter C. Evolution of the alpha-crystallin/ small heat-shock protein family. Moi Biol Evol 1993; 10:103-126.
  • 3
    • 0032077156 scopus 로고    scopus 로고
    • Genealogy of the alpha-crystallin - small heat-shock protein superfamily
    • de Jong WW, Gaspers GJ, Leunissen JA. Genealogy of the alpha-crystallin - small heat-shock protein superfamily. Int J Biol Macromol 1998; 22:151-162.
    • (1998) Int J Biol Macromol , vol.22 , pp. 151-162
    • de Jong, W.W.1    Gaspers, G.J.2    Leunissen, J.A.3
  • 4
    • 0035973873 scopus 로고    scopus 로고
    • Characterization of two novel human small heat shock proteins: Protein kinase-related HspB8 and testis-specific HspB9
    • Kappe G, Verschuure P, Philipsen RL et al. Characterization of two novel human small heat shock proteins: Protein kinase-related HspB8 and testis-specific HspB9. Biochim Biophys Acta 2001; 1520:1-6.
    • (2001) Biochim Biophys Acta , vol.1520 , pp. 1-6
    • Kappe, G.1    Verschuure, P.2    Philipsen, R.L.3
  • 5
    • 0036359595 scopus 로고    scopus 로고
    • Evolution and diversity of prokaryotic small heat shock proteins
    • Kappe G, Leunissen J A, de Jong WW. Evolution and diversity of prokaryotic small heat shock proteins. Prog Mol Subcell Biol 2002; 28:1-17.
    • (2002) Prog Mol Subcell Biol , vol.28 , pp. 1-17
    • Kappe, G.1    Leunissen, J.A.2    de Jong, W.W.3
  • 6
    • 0037358061 scopus 로고    scopus 로고
    • The human genome encodes 10 alpha-crystallin-related small heat shock proteins: HspB1-10
    • Kappe G, Franck E, Verschuure P et al. The human genome encodes 10 alpha-crystallin-related small heat shock proteins: HspB1-10. Cell Stress Chaperones 2003; 8:53-61.
    • (2003) Cell Stress Chaperones , vol.8 , pp. 53-61
    • Kappe, G.1    Franck, E.2    Verschuure, P.3
  • 7
    • 0003720391 scopus 로고
    • Morimoto RI, Tissieres A, Georgopoulos C, eds, Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Arrigo AP, Landry J. In: Morimoto RI, Tissieres A, Georgopoulos C, eds. The Biology of Heat Shock Proteins and Molecular Chaperones. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press, 1994:335-373.
    • (1994) The Biology of Heat Shock Proteins and Molecular Chaperones , pp. 335-373
    • Arrigo, A.P.1    Landry, J.2
  • 8
    • 0024345716 scopus 로고
    • Heat shock resistance confered by expression of the human HSP 27 gene in rodent cells
    • Landry J, Chretien P, Lambert H et al. Heat shock resistance confered by expression of the human HSP 27 gene in rodent cells. J Cell Biol 1989; 109:7-15.
    • (1989) J Cell Biol , vol.109 , pp. 7-15
    • Landry, J.1    Chretien, P.2    Lambert, H.3
  • 9
    • 0031962486 scopus 로고    scopus 로고
    • Small stress proteins: Chaperones that act as regulators of intracellular redox state and programmed cell death
    • Arrigo AP. Small stress proteins: Chaperones that act as regulators of intracellular redox state and programmed cell death. Biol Chem 1998; 379:19-26.
    • (1998) Biol Chem , vol.379 , pp. 19-26
    • Arrigo, A.P.1
  • 10
    • 0000177546 scopus 로고    scopus 로고
    • ed, Handbook of Experimental Pharmacology. Springer
    • Arrigo AP, Préville X. In: Latchman DS, ed. Stress Proteins, Vol. 136, Handbook of Experimental Pharmacology. Springer, 1999:101-132.
    • (1999) Stress Proteins , vol.136 , pp. 101-132
    • Arrigo, A.P.1    Préville, X.2
  • 11
    • 0036186869 scopus 로고    scopus 로고
    • Hsp27: Novel regulator of intracellular redox state
    • Arrigo AP. Hsp27: Novel regulator of intracellular redox state. IUBMB Life 2001; 52:303-307.
    • (2001) IUBMB Life , vol.52 , pp. 303-307
    • Arrigo, A.P.1
  • 12
    • 0036359558 scopus 로고    scopus 로고
    • Small stress proteins: Modulation of intracellular redox state and protection against oxidative stress
    • Arrigo AP, Paul C, Ducasse C et al. Small stress proteins: Modulation of intracellular redox state and protection against oxidative stress. Prog Mol Subcell Biol 2002; 28:171-184.
    • (2002) Prog Mol Subcell Biol , vol.28 , pp. 171-184
    • Arrigo, A.P.1    Paul, C.2    Ducasse, C.3
  • 13
    • 0025988318 scopus 로고
    • Increased survival after treatments with anticancer agents of Chinese hamster cells expressing the human Mr 27,000 heat shock protein
    • Huot J, Roy G, Lambert H et al. Increased survival after treatments with anticancer agents of Chinese hamster cells expressing the human Mr 27,000 heat shock protein. Cancer Res 1991; 51:5245-5252.
    • (1991) Cancer Res , vol.51 , pp. 5245-5252
    • Huot, J.1    Roy, G.2    Lambert, H.3
  • 15
    • 0034081704 scopus 로고    scopus 로고
    • sHsp as novel regulators of programmed cell death and tumorigenicity
    • Arrigo AP. sHsp as novel regulators of programmed cell death and tumorigenicity. Pathol Biol (Paris) 2000; 48:280-288.
    • (2000) Pathol Biol (Paris) , vol.48 , pp. 280-288
    • Arrigo, A.P.1
  • 16
    • 0034812599 scopus 로고    scopus 로고
    • Heat shock proteins: Endogenous modulators of apoptotic cell death
    • Garrido C, Gurbuxani S, Ravagnan L et al. Heat shock proteins: Endogenous modulators of apoptotic cell death. Biochem Biophys Res Commun 2001; 286:433-442.
    • (2001) Biochem Biophys Res Commun , vol.286 , pp. 433-442
    • Garrido, C.1    Gurbuxani, S.2    Ravagnan, L.3
  • 17
    • 0036366524 scopus 로고    scopus 로고
    • Small stress proteins: Novel negative modulators of apoptosis induced independently of reactive oxygen species
    • Arrigo AP, Paul C, Ducasse C et al. Small stress proteins: Novel negative modulators of apoptosis induced independently of reactive oxygen species. Prog Mol Subcell Biol 2002; 28:185-204.
    • (2002) Prog Mol Subcell Biol , vol.28 , pp. 185-204
    • Arrigo, A.P.1    Paul, C.2    Ducasse, C.3
  • 18
    • 0037246247 scopus 로고    scopus 로고
    • On the role of Hsp27 in regulating apoptosis
    • Concannon CG, Gorman AM, Samali A. On the role of Hsp27 in regulating apoptosis. Apoptosis 2003; 8:61-70.
    • (2003) Apoptosis , vol.8 , pp. 61-70
    • Concannon, C.G.1    Gorman, A.M.2    Samali, A.3
  • 19
    • 23344434147 scopus 로고    scopus 로고
    • HSP27 and cell survival in neurones
    • Latchman DS. HSP27 and cell survival in neurones. Int J Hyperthermia 2005; 21:393-402.
    • (2005) Int J Hyperthermia , vol.21 , pp. 393-402
    • Latchman, D.S.1
  • 20
    • 0027391629 scopus 로고
    • Small heat shock proteins are molecular chaperones
    • Jakob U, Gaestel M, Engels K et al. Small heat shock proteins are molecular chaperones. J Biol Chem 1993; 268:1517-1520.
    • (1993) J Biol Chem , vol.268 , pp. 1517-1520
    • Jakob, U.1    Gaestel, M.2    Engels, K.3
  • 21
    • 0028284571 scopus 로고
    • Assisting spontaneity: The role of Hsp90 and small Hsps as molecular chaperones
    • Jakob U, Buchner J. Assisting spontaneity: The role of Hsp90 and small Hsps as molecular chaperones. Trends Biochem Sci 1994; 19:205-211.
    • (1994) Trends Biochem Sci , vol.19 , pp. 205-211
    • Jakob, U.1    Buchner, J.2
  • 22
    • 0031454881 scopus 로고    scopus 로고
    • hsp27 as a switch between differentiation and apoptosis in murine embryonic stem cells
    • Mehlen P, Mehlen A, Godet J et al. hsp27 as a switch between differentiation and apoptosis in murine embryonic stem cells. J Biol Chem 1997; 272:31657-31665.
    • (1997) J Biol Chem , vol.272 , pp. 31657-31665
    • Mehlen, P.1    Mehlen, A.2    Godet, J.3
  • 23
    • 0032404094 scopus 로고    scopus 로고
    • Heat shock protein 27 enhances the tumorigenicity of immunogenic rat colon carcinoma cell clones
    • Garrido C, Fromentin A, Bonnotte B et al. Heat shock protein 27 enhances the tumorigenicity of immunogenic rat colon carcinoma cell clones. Cancer Res 1998; 58:5495-5499.
    • (1998) Cancer Res , vol.58 , pp. 5495-5499
    • Garrido, C.1    Fromentin, A.2    Bonnotte, B.3
  • 24
    • 0026457201 scopus 로고
    • Identification of MAPKAP kinase 2 as a major enzyme responsible for the phosphorylation of the small mammalian heat shock proteins
    • Stokoe D, Engel K, Campbell D et al. Identification of MAPKAP kinase 2 as a major enzyme responsible for the phosphorylation of the small mammalian heat shock proteins. FEBS Lett 1992; 313:307-313.
    • (1992) FEBS Lett , vol.313 , pp. 307-313
    • Stokoe, D.1    Engel, K.2    Campbell, D.3
  • 25
    • 0026330838 scopus 로고
    • Immunological evidence for the identity between the hsp27 estrogen-regulated heat shock protein and the p29 estrogen receptor-associated protein in breast and endometrial cancer
    • Ciocca DR, Luque EH. Immunological evidence for the identity between the hsp27 estrogen-regulated heat shock protein and the p29 estrogen receptor-associated protein in breast and endometrial cancer. Breast Cancer Res Treat 1991; 20:33-42.
    • (1991) Breast Cancer Res Treat , vol.20 , pp. 33-42
    • Ciocca, D.R.1    Luque, E.H.2
  • 26
    • 0032535245 scopus 로고    scopus 로고
    • Regulation of the heat shock transcriptional response: Cross talk between a family of heat shock factors, molecular chaperones, and negative regulators
    • Morimoto RI. Regulation of the heat shock transcriptional response: Cross talk between a family of heat shock factors, molecular chaperones, and negative regulators. Genes Dev 1998; 12:3788-3796.
    • (1998) Genes Dev , vol.12 , pp. 3788-3796
    • Morimoto, R.I.1
  • 27
    • 0028022750 scopus 로고
    • A novel kinase cascade triggered by stress and heat shock that stimulates MAPKAP kinase-2 and phosphorylation of the small heat shock proteins
    • Rouse J et al. A novel kinase cascade triggered by stress and heat shock that stimulates MAPKAP kinase-2 and phosphorylation of the small heat shock proteins. Cell 1994; 78:1027-1037.
    • (1994) Cell , vol.78 , pp. 1027-1037
    • Rouse, J.1
  • 28
    • 0023656751 scopus 로고
    • Characterization and purification of the small 28,000-dalton mammalian heat shock protein
    • Arrigo AP, Welch W. Characterization and purification of the small 28,000-dalton mammalian heat shock protein. J Biol Chem 1987; 262:15359-15369.
    • (1987) J Biol Chem , vol.262 , pp. 15359-15369
    • Arrigo, A.P.1    Welch, W.2
  • 29
    • 0023697402 scopus 로고
    • Dynamic changes in the structure and intracellular locale of the mammalian low-molecular-weight heat shock protein
    • Arrigo AP, Suhan JP, Welch WJ. Dynamic changes in the structure and intracellular locale of the mammalian low-molecular-weight heat shock protein. Mol Cell Biol 1988; 8:5059-5071.
    • (1988) Mol Cell Biol , vol.8 , pp. 5059-5071
    • Arrigo, A.P.1    Suhan, J.P.2    Welch, W.J.3
  • 30
    • 0028346451 scopus 로고
    • Dissociation as a result of phosphorylation of an aggregated form of the small stress protein, hsp27
    • Kato K, Hasegawa K, Goto S et al. Dissociation as a result of phosphorylation of an aggregated form of the small stress protein, hsp27. J Biol Chem 1994; 269:11274-11278.
    • (1994) J Biol Chem , vol.269 , pp. 11274-11278
    • Kato, K.1    Hasegawa, K.2    Goto, S.3
  • 31
    • 0031148195 scopus 로고    scopus 로고
    • Overexpression of the small heat shock protein, hsp27, confers resistance to hyperthermia, but not to oxidative stress and UV-induced cell death, in a stably transfected squamous cell carcinoma cell line
    • Trautinger F, Kokesch C, Herbacek I et al. Overexpression of the small heat shock protein, hsp27, confers resistance to hyperthermia, but not to oxidative stress and UV-induced cell death, in a stably transfected squamous cell carcinoma cell line. J Photochem Photobiol 1997; 39:90-95.
    • (1997) J Photochem Photobiol , vol.39 , pp. 90-95
    • Trautinger, F.1    Kokesch, C.2    Herbacek, I.3
  • 32
    • 0026691949 scopus 로고
    • Expression of Drosophila's 27 kDa heat shock protein into rodent cells confers thermal resistance
    • Rollet E, Lavoie J, Landry J et al. Expression of Drosophila's 27 kDa heat shock protein into rodent cells confers thermal resistance. Biochem Biophys Res Commun 1992; 185:116-120.
    • (1992) Biochem Biophys Res Commun , vol.185 , pp. 116-120
    • Rollet, E.1    Lavoie, J.2    Landry, J.3
  • 33
    • 21244489544 scopus 로고    scopus 로고
    • HspB8, a small heat shock protein mutated in human neuromuscular disorders, has in vivo chaperone activity in cultured cells
    • Carra S, Sivilotti M, Chavez Zobel AT et al. HspB8, a small heat shock protein mutated in human neuromuscular disorders, has in vivo chaperone activity in cultured cells. Hum Mol Genet 2005; 14:1659-1669.
    • (2005) Hum Mol Genet , vol.14 , pp. 1659-1669
    • Carra, S.1    Sivilotti, M.2    Chavez Zobel, A.T.3
  • 34
    • 0027999593 scopus 로고
    • Cells overexpressing Hsp27 show accelerated recovery from heat-induced nuclear protein aggregation
    • Kampinga HH, Brunsting JF, Stege GJ et al. Cells overexpressing Hsp27 show accelerated recovery from heat-induced nuclear protein aggregation. Biochem Biophys Res Commun 1994; 204:1170-1177.
    • (1994) Biochem Biophys Res Commun , vol.204 , pp. 1170-1177
    • Kampinga, H.H.1    Brunsting, J.F.2    Stege, G.J.3
  • 35
    • 0034659505 scopus 로고    scopus 로고
    • Chaperone Hsp27 inhibits translation during heat shock by binding eIF4G and facilitating dissociation of cap-initiation complexes
    • Cuesta R, Laroia G, Schneider RJ. Chaperone Hsp27 inhibits translation during heat shock by binding eIF4G and facilitating dissociation of cap-initiation complexes. Genes Dev 2000; 14:1460-1470.
    • (2000) Genes Dev , vol.14 , pp. 1460-1470
    • Cuesta, R.1    Laroia, G.2    Schneider, R.J.3
  • 36
    • 0030802907 scopus 로고    scopus 로고
    • Heat shock protein 27 stimulates recovery of RNA and protein synthesis following a heat shock
    • Carper SW, Rocheleau TA, Cimino D et al. Heat shock protein 27 stimulates recovery of RNA and protein synthesis following a heat shock. J Cell Biochem 1997; 66:153-164.
    • (1997) J Cell Biochem , vol.66 , pp. 153-164
    • Carper, S.W.1    Rocheleau, T.A.2    Cimino, D.3
  • 37
    • 85069257024 scopus 로고    scopus 로고
    • Hsp27 enhances recovery of splicing as well as rephosphorylation of SRp38 after heat shock
    • Marin-Vinader L, Shin C, Onnekink C et al. Hsp27 enhances recovery of splicing as well as rephosphorylation of SRp38 after heat shock. Mol Biol Cell 2005; 7:7-17.
    • (2005) Mol Biol Cell , vol.7 , pp. 7-17
    • Marin-Vinader, L.1    Shin, C.2    Onnekink, C.3
  • 38
    • 0030069517 scopus 로고    scopus 로고
    • HSP27 phosphorylation-mediated resistance against actin fragmentation and cell death induced by oxidative stress
    • Huot J, Houle F, Spitz DR et al, HSP27 phosphorylation-mediated resistance against actin fragmentation and cell death induced by oxidative stress. Cancer Res 1996; 56:273-279.
    • (1996) Cancer Res , vol.56 , pp. 273-279
    • Huot, J.1    Houle, F.2    Spitz, D.R.3
  • 39
    • 0028924759 scopus 로고
    • Modulation of cellular thermoresistance and actin filament stability accompanies phosphorylation- induced changes in the oligomeric structure of heat shock protein 27
    • Lavoie JN, Lambert H, Hickey E et al. Modulation of cellular thermoresistance and actin filament stability accompanies phosphorylation- induced changes in the oligomeric structure of heat shock protein 27. Mol Cell Biol 1995; 15:505-516.
    • (1995) Mol Cell Biol , vol.15 , pp. 505-516
    • Lavoie, J.N.1    Lambert, H.2    Hickey, E.3
  • 40
    • 0033591453 scopus 로고    scopus 로고
    • The dynamics of hsp25 quaternary structure. Structure and function of different oligomeric species
    • Ehrnsperger M, Lilie H, Gaestel M et al. The dynamics of hsp25 quaternary structure. Structure and function of different oligomeric species. J Biol Chem 1999; 274:14867-14874.
    • (1999) J Biol Chem , vol.274 , pp. 14867-14874
    • Ehrnsperger, M.1    Lilie, H.2    Gaestel, M.3
  • 41
    • 0343742639 scopus 로고    scopus 로고
    • Binding of nonnative protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation
    • Ehrnsperger M, Graber S, Gaestel M et al. Binding of nonnative protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation. EMBO J 1997; 16:221-229.
    • (1997) EMBO J , vol.16 , pp. 221-229
    • Ehrnsperger, M.1    Graber, S.2    Gaestel, M.3
  • 42
    • 0031024691 scopus 로고    scopus 로고
    • Small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state
    • Lee GJ, Roseman AM, Saibil HR et al. Small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state. EMBO J 1997; 16:659-671.
    • (1997) EMBO J , vol.16 , pp. 659-671
    • Lee, G.J.1    Roseman, A.M.2    Saibil, H.R.3
  • 43
    • 0038043235 scopus 로고    scopus 로고
    • Analysis of the interaction of small heat shock proteins with unfolding proteins
    • Stromer T, Ehrnsperger M, Gaestel M et al. Analysis of the interaction of small heat shock proteins with unfolding proteins. J Biol Chem 2003; 278:18015-18021.
    • (2003) J Biol Chem , vol.278 , pp. 18015-18021
    • Stromer, T.1    Ehrnsperger, M.2    Gaestel, M.3
  • 44
    • 27144448839 scopus 로고    scopus 로고
    • Some like it hot: The structure and function of small heat-shock proteins
    • Haslbeck M, Franzmann T, Weinfurtner D et al. Some like it hot: The structure and function of small heat-shock proteins. Nat Struct Mol Biol 2005; 12:842-846.
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 842-846
    • Haslbeck, M.1    Franzmann, T.2    Weinfurtner, D.3
  • 45
  • 46
    • 0033516660 scopus 로고    scopus 로고
    • Regulation of Hsp27 oligomerization, chaperone function, and protective activity against oxidative stress/tumor necrosis factor alpha by phosphorylation
    • Rogalla T, Ehrnsperger M, Preville X et al. Regulation of Hsp27 oligomerization, chaperone function, and protective activity against oxidative stress/tumor necrosis factor alpha by phosphorylation. J Biol Chem 1999; 274:18947-18956.
    • (1999) J Biol Chem , vol.274 , pp. 18947-18956
    • Rogalla, T.1    Ehrnsperger, M.2    Preville, X.3
  • 47
    • 0028071812 scopus 로고
    • Phosphorylation and supramolecular organization of murine small heat shock protein HSP25 abolish its actin polymerization-inhibiting activity
    • Benndorf R, Hayess K, Ryazantsev S et al. Phosphorylation and supramolecular organization of murine small heat shock protein HSP25 abolish its actin polymerization-inhibiting activity. J Biol Chem 1994; 269:20780-20784.
    • (1994) J Biol Chem , vol.269 , pp. 20780-20784
    • Benndorf, R.1    Hayess, K.2    Ryazantsev, S.3
  • 48
    • 0031056783 scopus 로고    scopus 로고
    • Regulation of actin filament dynamics by p38 map kinase-mediated phosphorylation of heat shock protein 27
    • Guay J, Lambert H, GingrasBreton G et al. Regulation of actin filament dynamics by p38 map kinase-mediated phosphorylation of heat shock protein 27. J Cell Sci 1997; 110:357-368.
    • (1997) J Cell Sci , vol.110 , pp. 357-368
    • Guay, J.1    Lambert, H.2    GingrasBreton, G.3
  • 49
    • 0036556697 scopus 로고    scopus 로고
    • Actin cytoskeleton and small heat shock proteins: How do they interact?
    • Mounier N, Arrigo AP. Actin cytoskeleton and small heat shock proteins: How do they interact? Cell Stress Chaperones 2002; 7:167-176.
    • (2002) Cell Stress Chaperones , vol.7 , pp. 167-176
    • Mounier, N.1    Arrigo, A.P.2
  • 50
    • 18844417388 scopus 로고    scopus 로고
    • Effects of small heat shock proteins on the thermal denaturation and aggregation of F-actin
    • Pivovarova AV, Mikhailova VV , Chernik IS et al. Effects of small heat shock proteins on the thermal denaturation and aggregation of F-actin. Biochem Biophys Res Commun 2005; 331:1548-1553.
    • (2005) Biochem Biophys Res Commun , vol.331 , pp. 1548-1553
    • Pivovarova, A.V.1    Mikhailova, V.V.2    Chernik, I.S.3
  • 51
    • 0031722160 scopus 로고    scopus 로고
    • Tobacco smoke induces both apoptosis and necrosis in mammalian cells: Differential effects of HSP70
    • Vayssier M, Banzet N, Francois D et al. Tobacco smoke induces both apoptosis and necrosis in mammalian cells: Differential effects of HSP70. Am J Physiol 1998; 275:771-779.
    • (1998) Am J Physiol , vol.275 , pp. 771-779
    • Vayssier, M.1    Banzet, N.2    Francois, D.3
  • 52
    • 0001421693 scopus 로고    scopus 로고
    • Glutathione depletion in fibroblasts is the basis for apoptosis-induction by endogenous reactive oxygen species
    • Zucker B, Hanusch J, Bauer G. Glutathione depletion in fibroblasts is the basis for apoptosis-induction by endogenous reactive oxygen species. Cell Death and Diff 1997; 4:388-395.
    • (1997) Cell Death and Diff , vol.4 , pp. 388-395
    • Zucker, B.1    Hanusch, J.2    Bauer, G.3
  • 53
    • 0033524857 scopus 로고    scopus 로고
    • A comparative study of apoptosis and necrosis in HepG2 cells: Oxidant-induced caspase inactivation leads to necrosis
    • Samali A, Nordgren H, Zhivotovsky B et al. A comparative study of apoptosis and necrosis in HepG2 cells: Oxidant-induced caspase inactivation leads to necrosis. Biochem Biophys Res Commun 1999; 255:6-11.
    • (1999) Biochem Biophys Res Commun , vol.255 , pp. 6-11
    • Samali, A.1    Nordgren, H.2    Zhivotovsky, B.3
  • 54
    • 0029873387 scopus 로고    scopus 로고
    • Reactive oxygen species and programmed cell death
    • Jacobson MD. Reactive oxygen species and programmed cell death. Trends Biochem Sci 1996; 21:83-86.
    • (1996) Trends Biochem Sci , vol.21 , pp. 83-86
    • Jacobson, M.D.1
  • 55
    • 0028824707 scopus 로고
    • Redox signalling and the control of cell growth and death
    • Powis G, Briehl M, Oblong J. Redox signalling and the control of cell growth and death. Pharmacol Ther 1995; 68:149-173.
    • (1995) Pharmacol Ther , vol.68 , pp. 149-173
    • Powis, G.1    Briehl, M.2    Oblong, J.3
  • 56
    • 0027485461 scopus 로고
    • Bcl-2 functions in an antioxidant pathway to prevent apoptosis
    • Hockenbery DM, Oltvai ZN, Yin XM et al. Bcl-2 functions in an antioxidant pathway to prevent apoptosis. Cell 1993; 75:241-251.
    • (1993) Cell , vol.75 , pp. 241-251
    • Hockenbery, D.M.1    Oltvai, Z.N.2    Yin, X.M.3
  • 57
    • 0027717968 scopus 로고
    • Bcl-2 inhibition of neural death: Decreased generation of reactive oxygen species
    • Kane DJ, Sarafian TA, Anton R et al. Bcl-2 inhibition of neural death: Decreased generation of reactive oxygen species. Science 1993; 262:1274-1277.
    • (1993) Science , vol.262 , pp. 1274-1277
    • Kane, D.J.1    Sarafian, T.A.2    Anton, R.3
  • 58
    • 0027293201 scopus 로고
    • Analysis of the resistance to heat and hydrogen peroxide stresses in COS cells transiently expressing wid type or deletion mutants of the Drosophila 27-kDa heat-shock protein
    • Mehlen P, Briolay J, Smith L et al. Analysis of the resistance to heat and hydrogen peroxide stresses in COS cells transiently expressing wid type or deletion mutants of the Drosophila 27-kDa heat-shock protein. Eur J Biochem 1993; 215:277-284.
    • (1993) Eur J Biochem , vol.215 , pp. 277-284
    • Mehlen, P.1    Briolay, J.2    Smith, L.3
  • 59
    • 0029933741 scopus 로고    scopus 로고
    • Human hsp27, Drosophila hsp27 and human aB-crystallin expression-mediated increase in glutathione is essential for the protective activity of these protein against TNFα-induced cell death
    • Mehlen P, Préville X, Kretz-Remy C et al. Human hsp27, Drosophila hsp27 and human aB-crystallin expression-mediated increase in glutathione is essential for the protective activity of these protein against TNFα-induced cell death. EMBO J 1996; 15:2695-2706.
    • (1996) EMBO J , vol.15 , pp. 2695-2706
    • Mehlen, P.1    Préville, X.2    Kretz-Remy, C.3
  • 60
    • 0345410965 scopus 로고    scopus 로고
    • Mammalian small stress proteins protect against oxidative stress through their ability to increase glucose-6-phosphate dehydrogenase activity and by maintaining optimal cellular detoxifying machinery
    • Preville X, Salvemin F, Giraud S et al. Mammalian small stress proteins protect against oxidative stress through their ability to increase glucose-6-phosphate dehydrogenase activity and by maintaining optimal cellular detoxifying machinery. Exp Cell Res 1999; 247:61-78.
    • (1999) Exp Cell Res , vol.247 , pp. 61-78
    • Preville, X.1    Salvemin, F.2    Giraud, S.3
  • 61
    • 0028817419 scopus 로고
    • Constitutive expression of human hsp27, Drosophila hsp27, or human alpha B-crystallin confers resistance to TNF- and oxidative stress-induced cytotoxicity in stably transfected murine L929 fibroblasts
    • Mehlen P, Préville X, Chareyron P et al. Constitutive expression of human hsp27, Drosophila hsp27, or human alpha B-crystallin confers resistance to TNF- and oxidative stress-induced cytotoxicity in stably transfected murine L929 fibroblasts. J Immunol 1995; 154:363-374.
    • (1995) J Immunol , vol.154 , pp. 363-374
    • Mehlen, P.1    Préville, X.2    Chareyron, P.3
  • 63
    • 0031961844 scopus 로고    scopus 로고
    • Overexpression of HSP25 reduces the level of TNF alpha-induced oxidative DNA damage biomarker, 8-hydroxy-2′- deoxyguanosine, in L929 cells
    • Park YM, Han MY, Blackburn RV et al. Overexpression of HSP25 reduces the level of TNF alpha-induced oxidative DNA damage biomarker, 8-hydroxy-2′- deoxyguanosine, in L929 cells. J Cell Physiol 1998; 174:27-34.
    • (1998) J Cell Physiol , vol.174 , pp. 27-34
    • Park, Y.M.1    Han, M.Y.2    Blackburn, R.V.3
  • 64
    • 0007404243 scopus 로고    scopus 로고
    • Large unphosphorylated aggregates as the active form of hsp27 which controls intracellular reactive oxygen species and glutathione levels and generates a protection against TNFα in NIH-3T3-ras cells
    • Mehlen P, Hickey E, Weber L et al. Large unphosphorylated aggregates as the active form of hsp27 which controls intracellular reactive oxygen species and glutathione levels and generates a protection against TNFα in NIH-3T3-ras cells. Biochem Biophys Res Comm 1997; 241:187-192.
    • (1997) Biochem Biophys Res Comm , vol.241 , pp. 187-192
    • Mehlen, P.1    Hickey, E.2    Weber, L.3
  • 65
    • 0030785821 scopus 로고    scopus 로고
    • HSP27 as a mediator of confluence-dependent resistance to cell death induced by anticancer drugs
    • Garrido C, Ottavi P, Fromentin A et al. HSP27 as a mediator of confluence-dependent resistance to cell death induced by anticancer drugs. Cancer Res 1997; 57:2661-2667.
    • (1997) Cancer Res , vol.57 , pp. 2661-2667
    • Garrido, C.1    Ottavi, P.2    Fromentin, A.3
  • 66
    • 0031057892 scopus 로고    scopus 로고
    • Oxidative stress-induced actin reorganization mediated by the p38 mitogen-activated protein kinase/heat shock protein 27 pathway in vascular endothelial cells
    • Huot J, Houle F, Marceau F et al. Oxidative stress-induced actin reorganization mediated by the p38 mitogen-activated protein kinase/heat shock protein 27 pathway in vascular endothelial cells. Circ Res 1997; 80:383-392.
    • (1997) Circ Res , vol.80 , pp. 383-392
    • Huot, J.1    Houle, F.2    Marceau, F.3
  • 67
    • 0031715855 scopus 로고    scopus 로고
    • Phosphorylation is not essential for protection of L929 cells by Hsp25 against H2O2-mediated disruption actin cytoskeleton, a protection which appears related to the redox change mediated by Hsp25
    • Préville X, Gaestel M, Arrigo AP. Phosphorylation is not essential for protection of L929 cells by Hsp25 against H2O2-mediated disruption actin cytoskeleton, a protection which appears related to the redox change mediated by Hsp25. Cell Stress Chaperones 1998; 3:177-187.
    • (1998) Cell Stress Chaperones , vol.3 , pp. 177-187
    • Préville, X.1    Gaestel, M.2    Arrigo, A.P.3
  • 69
    • 0034054731 scopus 로고    scopus 로고
    • Role of small heat shock protein HSP25 in radioresistance and glutathione-redox cycle
    • Baek SH, Min JN, Park EM et al. Role of small heat shock protein HSP25 in radioresistance and glutathione-redox cycle. J Cell Physiol 2000; 183:100-107.
    • (2000) J Cell Physiol , vol.183 , pp. 100-107
    • Baek, S.H.1    Min, J.N.2    Park, E.M.3
  • 70
    • 0033784408 scopus 로고    scopus 로고
    • Comparison of the protective activities generated by two survival proteins: Bcl-2 and Hsp27 in L929 murine fibroblasts exposed to menadione or staurosporine
    • Paul C, Arrigo AP. Comparison of the protective activities generated by two survival proteins: Bcl-2 and Hsp27 in L929 murine fibroblasts exposed to menadione or staurosporine. Exp Gerontol 2000; 35:757-766.
    • (2000) Exp Gerontol , vol.35 , pp. 757-766
    • Paul, C.1    Arrigo, A.P.2
  • 71
    • 11844257596 scopus 로고    scopus 로고
    • Cytotoxic effects induced by oxidative stress in cultured mammalian cells and protection provided by Hsp27 expression
    • Arrigo AP, Firdaus WJ, Mellier G et al. Cytotoxic effects induced by oxidative stress in cultured mammalian cells and protection provided by Hsp27 expression. Methods 2005; 35:126-138.
    • (2005) Methods , vol.35 , pp. 126-138
    • Arrigo, A.P.1    Firdaus, W.J.2    Mellier, G.3
  • 72
    • 14044259324 scopus 로고    scopus 로고
    • Substitution of the unique cysteine residue of murine hsp25 interferes with the protective activity of this stress protein through inhibition of dimer formation
    • Diaz-Latoud C, Buache E, Javouhey E et al. Substitution of the unique cysteine residue of murine hsp25 interferes with the protective activity of this stress protein through inhibition of dimer formation. Antioxid Redox Signal 2005; 7:436-445.
    • (2005) Antioxid Redox Signal , vol.7 , pp. 436-445
    • Diaz-Latoud, C.1    Buache, E.2    Javouhey, E.3
  • 73
    • 0029068086 scopus 로고
    • Tumor necrosis factor-a induces changes in the phosphorylation, cellular localization, and oligomerization of human hsp27, a stress protein that confers cellular resistance to this cytokine
    • Mehlen P, Mehlen A, Guillet D et al. Tumor necrosis factor-a induces changes in the phosphorylation, cellular localization, and oligomerization of human hsp27, a stress protein that confers cellular resistance to this cytokine. J Cell Biochem 1995; 58:248-259.
    • (1995) J Cell Biochem , vol.58 , pp. 248-259
    • Mehlen, P.1    Mehlen, A.2    Guillet, D.3
  • 74
    • 0029610424 scopus 로고
    • Intracellular reactive oxygen species as apparent modulators of heat-shock protein 27 (hsp27) structural organization and phosphorylation in basal and tumour necrosis factor alpha-treated T47D human carcinoma cells
    • Mehlen P, Kretz-Remy C, Briolay J et al. Intracellular reactive oxygen species as apparent modulators of heat-shock protein 27 (hsp27) structural organization and phosphorylation in basal and tumour necrosis factor alpha-treated T47D human carcinoma cells. Biochem J 1995; 312:367-375.
    • (1995) Biochem J , vol.312 , pp. 367-375
    • Mehlen, P.1    Kretz-Remy, C.2    Briolay, J.3
  • 75
    • 0032438035 scopus 로고    scopus 로고
    • Proteasome-dependent degradation of oxidized proteins in MRC-5 fibroblasts
    • Sitte N, Merker K, Grune T. Proteasome-dependent degradation of oxidized proteins in MRC-5 fibroblasts. FEBS Lett 1998; 440:399-402.
    • (1998) FEBS Lett , vol.440 , pp. 399-402
    • Sitte, N.1    Merker, K.2    Grune, T.3
  • 76
    • 0029043135 scopus 로고
    • Effects of the overexpression of the small heat shock protein, Hsp27, on the sensitivity of human fibroblast cells exposed to oxidative stress
    • Arata S, Hamaguchi S, Nose K. Effects of the overexpression of the small heat shock protein, Hsp27, on the sensitivity of human fibroblast cells exposed to oxidative stress. J Cell Physiol 1995; 163:458-465.
    • (1995) J Cell Physiol , vol.163 , pp. 458-465
    • Arata, S.1    Hamaguchi, S.2    Nose, K.3
  • 77
    • 0031795906 scopus 로고    scopus 로고
    • Expression of HSP27 results in increased sensitivity to tumor necrosis factor, etoposide, and H2O2 in an oxidative stress-resistant cell line
    • Mairesse N, Bernaert D, Del Bino G et al. Expression of HSP27 results in increased sensitivity to tumor necrosis factor, etoposide, and H2O2 in an oxidative stress-resistant cell line. J Cell Physiol 1998; 177:606-617.
    • (1998) J Cell Physiol , vol.177 , pp. 606-617
    • Mairesse, N.1    Bernaert, D.2    Del Bino, G.3
  • 79
    • 0032575750 scopus 로고    scopus 로고
    • Caspases: Enemies within
    • Thornberry NA, Lazebnik Y. Caspases: Enemies within. Science 1998; 281:1312-1316.
    • (1998) Science , vol.281 , pp. 1312-1316
    • Thornberry, N.A.1    Lazebnik, Y.2
  • 80
    • 0032536771 scopus 로고    scopus 로고
    • Two CD95 (APO-1/Fas) signaling pathways
    • Scaffidi C, Fulda S, Srinivasan A et al. Two CD95 (APO-1/Fas) signaling pathways. Embo J 1998; 17:1675-1687.
    • (1998) Embo J , vol.17 , pp. 1675-1687
    • Scaffidi, C.1    Fulda, S.2    Srinivasan, A.3
  • 81
    • 0030782177 scopus 로고    scopus 로고
    • Cytochrome c: Can't live with it - can't live without it
    • Reed JC. Cytochrome c: Can't live with it - can't live without it. Cell 1997; 91:559-562.
    • (1997) Cell , vol.91 , pp. 559-562
    • Reed, J.C.1
  • 82
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • Green DR, Reed JC. Mitochondria and apoptosis. Science 1998; 281:1309-1312.
    • (1998) Science , vol.281 , pp. 1309-1312
    • Green, D.R.1    Reed, J.C.2
  • 83
    • 0035072246 scopus 로고    scopus 로고
    • Hsp27 protects mitochondria of thermotolerant cells against apoptotic stimuli
    • Samali A, Robertson JD, Peterson E et al. Hsp27 protects mitochondria of thermotolerant cells against apoptotic stimuli. Cell Stress Chaperones 2001; 6:49-58.
    • (2001) Cell Stress Chaperones , vol.6 , pp. 49-58
    • Samali, A.1    Robertson, J.D.2    Peterson, E.3
  • 84
    • 0030041936 scopus 로고    scopus 로고
    • Heat shock proteins increase resistance to apoptosis
    • Samali A, Cotter TG. Heat shock proteins increase resistance to apoptosis. Exp Cell Res 1996; 223:163-170.
    • (1996) Exp Cell Res , vol.223 , pp. 163-170
    • Samali, A.1    Cotter, T.G.2
  • 85
    • 0032440847 scopus 로고    scopus 로고
    • Heat shock proteins: Regulators of stress response and apoptosis
    • Samali A, Orrenius S. Heat shock proteins: Regulators of stress response and apoptosis. Cell Stress Chaperones 1998; 3:228-236.
    • (1998) Cell Stress Chaperones , vol.3 , pp. 228-236
    • Samali, A.1    Orrenius, S.2
  • 86
    • 30344459150 scopus 로고    scopus 로고
    • In situ trapping of activated initiator caspases reveals a role for caspase-2 in heat shock-induced apoptosis
    • Tu S, McStay GP, Boucher LM et al. In situ trapping of activated initiator caspases reveals a role for caspase-2 in heat shock-induced apoptosis. Nat Cell Biol 2006; 8:72-77.
    • (2006) Nat Cell Biol , vol.8 , pp. 72-77
    • Tu, S.1    McStay, G.P.2    Boucher, L.M.3
  • 87
    • 29144463145 scopus 로고    scopus 로고
    • The multidomain proapoptotic molecules Bax and Bak are directly activated by heat
    • Pagliari LJ, Kuwana T, Bonzon C et al. The multidomain proapoptotic molecules Bax and Bak are directly activated by heat. Proc Natl Acad Sci USA 2005; 102:17975-17980.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 17975-17980
    • Pagliari, L.J.1    Kuwana, T.2    Bonzon, C.3
  • 88
    • 0030014643 scopus 로고    scopus 로고
    • Mehlen P, Schulze-Osthoff K, Arrigo AP. Small stress proteins as novel regulators of apoptosis. Heat shock protein 27 blocks Fas/APO-1- and staurosporine-induced cell death. The J Biol Chem 1996; 271:16510-16514.
    • Mehlen P, Schulze-Osthoff K, Arrigo AP. Small stress proteins as novel regulators of apoptosis. Heat shock protein 27 blocks Fas/APO-1- and staurosporine-induced cell death. The J Biol Chem 1996; 271:16510-16514.
  • 89
    • 0032722324 scopus 로고    scopus 로고
    • HSP27 inhibits cytochrome c-dependent activation of procaspase-9
    • Garrido C, Bruey JM, Fromentin A et al. HSP27 inhibits cytochrome c-dependent activation of procaspase-9. Faseb J 1999; 13:2061-2070.
    • (1999) Faseb J , vol.13 , pp. 2061-2070
    • Garrido, C.1    Bruey, J.M.2    Fromentin, A.3
  • 90
    • 0029979079 scopus 로고    scopus 로고
    • Inconstant association between 27-kDa heat-shock protein (Hsp27) content and doxorubicin resistance in human colon cancer cells. The doxorubicin-protecting effect of Hsp27
    • Garrido C, Mehlen P, Fromentin A et al. Inconstant association between 27-kDa heat-shock protein (Hsp27) content and doxorubicin resistance in human colon cancer cells. The doxorubicin-protecting effect of Hsp27. Eur J Biochem 1996; 237:653-659.
    • (1996) Eur J Biochem , vol.237 , pp. 653-659
    • Garrido, C.1    Mehlen, P.2    Fromentin, A.3
  • 91
    • 0032747966 scopus 로고    scopus 로고
    • Hsp27 overexpression inhibits doxorubicin-induced apoptosis in human breast cancer cells
    • Hansen RK, Parra I, Lemieux P et al. Hsp27 overexpression inhibits doxorubicin-induced apoptosis in human breast cancer cells. Breast Cancer Res Treat 1999; 56:187-196.
    • (1999) Breast Cancer Res Treat , vol.56 , pp. 187-196
    • Hansen, R.K.1    Parra, I.2    Lemieux, P.3
  • 92
    • 0345073285 scopus 로고    scopus 로고
    • Bcl-2 and Hsp27 act at different levels to suppress programmed cell death
    • Guenal I, Sidoti-de Fraisse C, Gaumer S et al. Bcl-2 and Hsp27 act at different levels to suppress programmed cell death. Oncogene 1997; 15:347-360.
    • (1997) Oncogene , vol.15 , pp. 347-360
    • Guenal, I.1    Sidoti-de Fraisse, C.2    Gaumer, S.3
  • 93
    • 0031803216 scopus 로고    scopus 로고
    • A role for heat shock protein 27 in CTL-mediated cell death
    • Beresford PJ, Jaju M, Friedman RS et al. A role for heat shock protein 27 in CTL-mediated cell death. J Immunol 1998; 161:161-167.
    • (1998) J Immunol , vol.161 , pp. 161-167
    • Beresford, P.J.1    Jaju, M.2    Friedman, R.S.3
  • 94
    • 77957095102 scopus 로고    scopus 로고
    • Differential protective activity of αA- and {alpha}B-crystallin in lens epithelial cells
    • Andley UP, Song Z, Wawrousek EF et al. Differential protective activity of αA- and {alpha}B-crystallin in lens epithelial cells. J Biol Chem 2000; 30:30-40.
    • (2000) J Biol Chem , vol.30 , pp. 30-40
    • Andley, U.P.1    Song, Z.2    Wawrousek, E.F.3
  • 95
    • 0033796051 scopus 로고    scopus 로고
    • Inhibition of daxx-mediated apoptosis by heat shock protein 27
    • Charette SJ, Lavoie JN, Lambert H et al. Inhibition of daxx-mediated apoptosis by heat shock protein 27. Mol Cell Biol 2000; 20:7602-7612.
    • (2000) Mol Cell Biol , vol.20 , pp. 7602-7612
    • Charette, S.J.1    Lavoie, J.N.2    Lambert, H.3
  • 96
    • 0036143720 scopus 로고    scopus 로고
    • Hsp27 as a negative regulator of cytochrome C release
    • Paul C, Manero F, Gonin S et al. Hsp27 as a negative regulator of cytochrome C release. Mol Cell Biol 2002; 22:816-834.
    • (2002) Mol Cell Biol , vol.22 , pp. 816-834
    • Paul, C.1    Manero, F.2    Gonin, S.3
  • 97
    • 0142245588 scopus 로고    scopus 로고
    • Hsp27 inhibits release of mitochondrial protein Smac in multiple myeloma cells and confers dexamethasone resistance
    • Chauhan D, Li G, Hideshima T et al. Hsp27 inhibits release of mitochondrial protein Smac in multiple myeloma cells and confers dexamethasone resistance. Blood 2003; 102:3379-3386.
    • (2003) Blood , vol.102 , pp. 3379-3386
    • Chauhan, D.1    Li, G.2    Hideshima, T.3
  • 98
    • 0034282104 scopus 로고    scopus 로고
    • Hsp27 negatively regulates cell death by interacting with cytochrome c
    • Bruey JM, Ducasse C, Bonniaud P et al. Hsp27 negatively regulates cell death by interacting with cytochrome c. Nat Cell Biol 2000; 2:645-652.
    • (2000) Nat Cell Biol , vol.2 , pp. 645-652
    • Bruey, J.M.1    Ducasse, C.2    Bonniaud, P.3
  • 99
    • 14044250859 scopus 로고    scopus 로고
    • Hsp27 consolidates intracellular redox homeostasis by upholding glutathione in its reduced form and by decreasing iron intracellular levels
    • Arrigo AP, Virot S, Chaufour S et al. Hsp27 consolidates intracellular redox homeostasis by upholding glutathione in its reduced form and by decreasing iron intracellular levels. Antioxid Redox Signal 2005; 7:414-422.
    • (2005) Antioxid Redox Signal , vol.7 , pp. 414-422
    • Arrigo, A.P.1    Virot, S.2    Chaufour, S.3
  • 100
    • 0034643424 scopus 로고    scopus 로고
    • Hsp27 functions as a negative regulator of cytochrome c-dependent activation of procaspase-3
    • Pandey P, Farber R, Nakazawa A et al. Hsp27 functions as a negative regulator of cytochrome c-dependent activation of procaspase-3. Oncogene 2000; 19:1975-1981.
    • (2000) Oncogene , vol.19 , pp. 1975-1981
    • Pandey, P.1    Farber, R.2    Nakazawa, A.3
  • 101
    • 0029587039 scopus 로고
    • Expression of stress genes during development
    • Arrigo AP. Expression of stress genes during development. Neuropathol and Applied Neurobiol 1995; 21:488-491.
    • (1995) Neuropathol and Applied Neurobiol , vol.21 , pp. 488-491
    • Arrigo, A.P.1
  • 102
    • 18444366777 scopus 로고    scopus 로고
    • In search of the molecular mechanism by which small stress proteins counteract apoptosis during cellular differentiation
    • Arrigo AP. In search of the molecular mechanism by which small stress proteins counteract apoptosis during cellular differentiation. J Cell Biochem 2005; 94:241-246.
    • (2005) J Cell Biochem , vol.94 , pp. 241-246
    • Arrigo, A.P.1
  • 103
    • 0030322999 scopus 로고    scopus 로고
    • Transient accumulation, phosphorylation and changes in the oligomerization of Hsp27 during retinoic acid-induced differentiation of HL-60 cells: Possible role in the control of cellular growth and differentiation
    • Chaufour S, Mehlen P, Arrigo AP. Transient accumulation, phosphorylation and changes in the oligomerization of Hsp27 during retinoic acid-induced differentiation of HL-60 cells: Possible role in the control of cellular growth and differentiation. Cell Stress Chaperones 1996; 1:225-235.
    • (1996) Cell Stress Chaperones , vol.1 , pp. 225-235
    • Chaufour, S.1    Mehlen, P.2    Arrigo, A.P.3
  • 105
    • 0033014730 scopus 로고    scopus 로고
    • Small stress protein Hsp27 accumulation during dopamine-mediated differentiation of rat olfactory neurons counteracts apoptosis
    • Mehlen P, Coronas V, Ljubic-Thibal V et al. Small stress protein Hsp27 accumulation during dopamine-mediated differentiation of rat olfactory neurons counteracts apoptosis. Cell Death Differ 1999; 6:227-233.
    • (1999) Cell Death Differ , vol.6 , pp. 227-233
    • Mehlen, P.1    Coronas, V.2    Ljubic-Thibal, V.3
  • 106
    • 0032990851 scopus 로고    scopus 로고
    • Heat shock proteins delivered with a virus vector can protect cardiac cells against apoptosis as well as against thermal or hypoxic stress
    • Brar BK, Stephanou A, Wagstaff MJ et al. Heat shock proteins delivered with a virus vector can protect cardiac cells against apoptosis as well as against thermal or hypoxic stress. J Mol Cell Cardiol 1999; 31:135-146.
    • (1999) J Mol Cell Cardiol , vol.31 , pp. 135-146
    • Brar, B.K.1    Stephanou, A.2    Wagstaff, M.J.3
  • 107
    • 0026642374 scopus 로고
    • Prognostic influence of HSP-27 expression in malignant fibrous histiocytoma: A clinicopathological and immunohistochemical study
    • Têtu B, Têtu BB, Lacasse HL et al. Prognostic influence of HSP-27 expression in malignant fibrous histiocytoma: A clinicopathological and immunohistochemical study. Cancer Res 1992; 52:2325-2328.
    • (1992) Cancer Res , vol.52 , pp. 2325-2328
    • Têtu, B.1    Têtu, B.B.2    Lacasse, H.L.3
  • 108
    • 0027423102 scopus 로고
    • Biological and clinical implications of heat shock proteins 27000 (Hsp27): A review
    • Ciocca DR, Oesterreich S, Chamnes GC et al. Biological and clinical implications of heat shock proteins 27000 (Hsp27): A review. J Natl Cancer Inst 1993; 85:1558-1570.
    • (1993) J Natl Cancer Inst , vol.85 , pp. 1558-1570
    • Ciocca, D.R.1    Oesterreich, S.2    Chamnes, G.C.3
  • 109
    • 21744445069 scopus 로고    scopus 로고
    • Heat shock proteins in cancer: Diagnostic, prognostic, predictive, and treatment implications
    • Ciocca DR, Calderwood SK. Heat shock proteins in cancer: Diagnostic, prognostic, predictive, and treatment implications. Cell Stress Chaperones 2005; 10:86-103.
    • (2005) Cell Stress Chaperones , vol.10 , pp. 86-103
    • Ciocca, D.R.1    Calderwood, S.K.2
  • 110
    • 28244456529 scopus 로고    scopus 로고
    • Increased Hsp27 after androgen ablation facilitates androgen-independent progression in prostate cancer via signal transducers and activators of transcription 3-mediated suppression of apoptosis
    • Rocchi P, Beraldi E, Ettinger S et al. Increased Hsp27 after androgen ablation facilitates androgen-independent progression in prostate cancer via signal transducers and activators of transcription 3-mediated suppression of apoptosis. Cancer Res 2005; 65:11083-11093.
    • (2005) Cancer Res , vol.65 , pp. 11083-11093
    • Rocchi, P.1    Beraldi, E.2    Ettinger, S.3
  • 111
    • 0037195845 scopus 로고    scopus 로고
    • Modulation of heat-shock protein 27 (Hsp27) anti-apoptotic activity by methylglyoxal modification
    • Sakamoto H, Mashima T, Yamamoto K et al. Modulation of heat-shock protein 27 (Hsp27) anti-apoptotic activity by methylglyoxal modification. J Biol Chem 2002; 277:45770-45775.
    • (2002) J Biol Chem , vol.277 , pp. 45770-45775
    • Sakamoto, H.1    Mashima, T.2    Yamamoto, K.3
  • 112
    • 85069250612 scopus 로고    scopus 로고
    • Argpyrimidine-modified Heat Shock Protein 27 in human nonsmail cell lung cancer: A possible mechanism for evasion of apoptosis
    • Heijst JW, Niessen HW, Musters RJ et al. Argpyrimidine-modified Heat Shock Protein 27 in human nonsmail cell lung cancer: A possible mechanism for evasion of apoptosis. Cancer Lett 2005; 5:5-15.
    • (2005) Cancer Lett , vol.5 , pp. 5-15
    • Heijst, J.W.1    Niessen, H.W.2    Musters, R.J.3
  • 113
    • 0031750178 scopus 로고    scopus 로고
    • Antibodies to heat-shock protein 27 are associated with improved survival in patients with breast cancer
    • Conroy SE, Sasieni PD, Amin V et al. Antibodies to heat-shock protein 27 are associated with improved survival in patients with breast cancer. Br J Cancer 1998; 77:1875-1879.
    • (1998) Br J Cancer , vol.77 , pp. 1875-1879
    • Conroy, S.E.1    Sasieni, P.D.2    Amin, V.3
  • 114
    • 0034657707 scopus 로고    scopus 로고
    • The mechanisms of hsp27 antibody-mediated apoptosis in retinal neuronal cells
    • Tezel G, Wax MB. The mechanisms of hsp27 antibody-mediated apoptosis in retinal neuronal cells. J Neurosci 2000; 20:3552-3562.
    • (2000) J Neurosci , vol.20 , pp. 3552-3562
    • Tezel, G.1    Wax, M.B.2
  • 115
    • 33644876626 scopus 로고    scopus 로고
    • Hsp27 may allow prediction of the response to single-agent vinorelbine chemotherapy in nonsmall cell lung cancer
    • Berrieman HK, Cawkwell L, O'Kane SL et al. Hsp27 may allow prediction of the response to single-agent vinorelbine chemotherapy in nonsmall cell lung cancer. Oncol Rep 2006; 15:283-286.
    • (2006) Oncol Rep , vol.15 , pp. 283-286
    • Berrieman, H.K.1    Cawkwell, L.2    O'Kane, S.L.3
  • 116
    • 28444451204 scopus 로고    scopus 로고
    • Heat-shock protein 27: A potential biomarker for hepatocellular carcinoma identified by serum proteome analysis
    • Feng JT, Liu YK, Song HY et al. Heat-shock protein 27: A potential biomarker for hepatocellular carcinoma identified by serum proteome analysis. Proteomics 2005; 5:4581-4588.
    • (2005) Proteomics , vol.5 , pp. 4581-4588
    • Feng, J.T.1    Liu, Y.K.2    Song, H.Y.3
  • 117
    • 29244479188 scopus 로고    scopus 로고
    • Blocking tumor cell migration and invasion with biphenyl isoxazole derivative KRIBB3, a synthetic molecule that inhibits Hsp27 phosphorylation
    • Shin KD, Lee MY, Shin DS et al. Blocking tumor cell migration and invasion with biphenyl isoxazole derivative KRIBB3, a synthetic molecule that inhibits Hsp27 phosphorylation. J Biol Chem 2005; 280:41439-41448.
    • (2005) J Biol Chem , vol.280 , pp. 41439-41448
    • Shin, K.D.1    Lee, M.Y.2    Shin, D.S.3
  • 118
    • 26944481201 scopus 로고    scopus 로고
    • Differential expression of alphaB-crystallin and Hsp27-1 in anaplastic thyroid carcinomas because of tumor-specific alphaB-crystallin gene (CRYAB) silencing
    • Mineva I, Gartne W, Hauser P et al. Differential expression of alphaB-crystallin and Hsp27-1 in anaplastic thyroid carcinomas because of tumor-specific alphaB-crystallin gene (CRYAB) silencing. Cell Stress Chaperones 2005; 10:171-184.
    • (2005) Cell Stress Chaperones , vol.10 , pp. 171-184
    • Mineva, I.1    Gartne, W.2    Hauser, P.3
  • 119
    • 21244480134 scopus 로고    scopus 로고
    • Heat shock protein 27 is associated with decreased survival in node-negative breast cancer patients
    • Thanner F, Sutterlin MW, Kapp M et al. Heat shock protein 27 is associated with decreased survival in node-negative breast cancer patients. Anticancer Res 2005; 25:1649-1653.
    • (2005) Anticancer Res , vol.25 , pp. 1649-1653
    • Thanner, F.1    Sutterlin, M.W.2    Kapp, M.3
  • 120
    • 20944432903 scopus 로고    scopus 로고
    • Heat shock protein 27 expression in patients with chronic liver damage
    • Federico A, Tuccillo C, Terracciano F et al. Heat shock protein 27 expression in patients with chronic liver damage. Immunobiology 2005; 209:729-735.
    • (2005) Immunobiology , vol.209 , pp. 729-735
    • Federico, A.1    Tuccillo, C.2    Terracciano, F.3
  • 121
    • 0036666144 scopus 로고    scopus 로고
    • Heat shock protein-27 protects human bronchial epithelial cells against oxidative stress-mediated apoptosis: Possible implication in asthma
    • Merendino AM, Paul C, Costa MA et al. Heat shock protein-27 protects human bronchial epithelial cells against oxidative stress-mediated apoptosis: Possible implication in asthma. Cell Stress Chaperones 2002; 7:269-280.
    • (2002) Cell Stress Chaperones , vol.7 , pp. 269-280
    • Merendino, A.M.1    Paul, C.2    Costa, M.A.3
  • 122
    • 26944453184 scopus 로고    scopus 로고
    • Small heat shock proteins in inherited peripheral neuropathies
    • Dierick I, Irobi J, De Jonghe P et al. Small heat shock proteins in inherited peripheral neuropathies. Ann Med 2005; 37:413-422.
    • (2005) Ann Med , vol.37 , pp. 413-422
    • Dierick, I.1    Irobi, J.2    De Jonghe, P.3


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