메뉴 건너뛰기




Volumn 4, Issue 1, 1999, Pages 8-18

Modulation of tolerance by mutant heat shock transcription factors

Author keywords

[No Author keywords available]

Indexed keywords

CYCLOPHOSPHAMIDE; HEAT SHOCK PROTEIN; TRANSCRIPTION FACTOR;

EID: 0032898588     PISSN: 13558145     EISSN: None     Source Type: Journal    
DOI: 10.1054/csac.1998.0113     Document Type: Article
Times cited : (40)

References (40)
  • 1
    • 0026750001 scopus 로고
    • Heat shock gene regulation by nascent polypeptides and denatured proteins: Hsp70 as a potential autoregulatory factor
    • Baler R, Welch WJ and Voellmy R (1992) Heat shock gene regulation by nascent polypeptides and denatured proteins: hsp70 as a potential autoregulatory factor. J Cell Biol 117: 1151-1159.
    • (1992) J Cell Biol , vol.117 , pp. 1151-1159
    • Baler, R.1    Welch, W.J.2    Voellmy, R.3
  • 2
    • 0027474909 scopus 로고
    • Activation of human heat shock genes is accompanied by oligomerization, modification, and rapid translocation of heat shock transcription factor Hsf1
    • Baler R, Dahl G and Voellmy R (1993) Activation of human heat shock genes is accompanied by oligomerization, modification, and rapid translocation of heat shock transcription factor Hsf1. Mol Cell Biol 13: 2486-2496.
    • (1993) Mol Cell Biol , vol.13 , pp. 2486-2496
    • Baler, R.1    Dahl, G.2    Voellmy, R.3
  • 3
    • 0029852803 scopus 로고    scopus 로고
    • Chaperone function of Hap90-associated proteins
    • Bose S, Weikl T, Buegl H and Buchner J (1996) Chaperone function of Hap90-associated proteins. Science 274: 1715-1717.
    • (1996) Science , vol.274 , pp. 1715-1717
    • Bose, S.1    Weikl, T.2    Buegl, H.3    Buchner, J.4
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of proteins utilizing the principle of protein-dye binding
    • Bradford M (1976) A rapid and sensitive method for the quantitation of microgram quantities of proteins utilizing the principle of protein-dye binding. Analyt Biochem 72: 248-254.
    • (1976) Analyt Biochem , vol.72 , pp. 248-254
    • Bradford, M.1
  • 5
    • 0027463072 scopus 로고
    • Heat shock response and limitation of tissue necrosis during occlusion/reperfusion in rabbit hearts
    • Currie RW, Tanguay RM and Kingma JG (1993) Heat shock response and limitation of tissue necrosis during occlusion/reperfusion in rabbit hearts. Circulation 87: 963-971.
    • (1993) Circulation , vol.87 , pp. 963-971
    • Currie, R.W.1    Tanguay, R.M.2    Kingma, J.G.3
  • 6
    • 0020409205 scopus 로고
    • The heat shock response is self-regulated at both the transcriptional and posttranscriptional levels
    • DiDomenico BJ, Bugaisky GE and Lindquist S (1982a) The heat shock response is self-regulated at both the transcriptional and posttranscriptional levels. Cell 31: 593-603.
    • (1982) Cell , vol.31 , pp. 593-603
    • Didomenico, B.J.1    Bugaisky, G.E.2    Lindquist, S.3
  • 7
    • 0344122872 scopus 로고
    • Heat shock and recovery are mediated by different translational mechanisms
    • DiDomenico BJ, Bugaisky GE and Lindquist S (1982b) Heat shock and recovery are mediated by different translational mechanisms. Proc Natl Acad Sci USA 79: 6181-6185.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 6181-6185
    • DiDomenico, B.J.1    Bugaisky, G.E.2    Lindquist, S.3
  • 8
    • 0026570622 scopus 로고
    • Heat shock protein induction in rat hearts. A role for improved myocardial salvage after ichemia and reperfusion?
    • Donelly TJ, Sievers RE, Vissern FL, Welch WJ and Wolfe CL (1992) Heat shock protein induction in rat hearts. A role for improved myocardial salvage after ichemia and reperfusion? Circulation 85: 769-778.
    • (1992) Circulation , vol.85 , pp. 769-778
    • Donelly, T.J.1    Sievers, R.E.2    Vissern, F.L.3    Welch, W.J.4    Wolfe, C.L.5
  • 9
    • 0020435972 scopus 로고
    • Recombinant genomes which express chloramphenicol acetyltransferase in mammalian cells
    • Gorman CM, Moffat LF and Howard BH (1982) Recombinant genomes which express chloramphenicol acetyltransferase in mammalian cells. Mol Cell Biol 2: 1044-1051.
    • (1982) Mol Cell Biol , vol.2 , pp. 1044-1051
    • Gorman, C.M.1    Moffat, L.F.2    Howard, B.H.3
  • 11
    • 0020451771 scopus 로고
    • Thermotolerance and heat shock proteins in mammalian cells
    • Hahn G and Li GC (1982) Thermotolerance and heat shock proteins in mammalian cells. Radiation Res 92: 452-457.
    • (1982) Radiation Res , vol.92 , pp. 452-457
    • Hahn, G.1    Li, G.C.2
  • 13
    • 0030985251 scopus 로고    scopus 로고
    • Multiple functions of Drosophila heat shock transcription factor in vivo
    • Jedlicka P, Mortin MA and Wu C (1997) Multiple functions of Drosophila heat shock transcription factor in vivo. EMBO J 16: 2452-2462.
    • (1997) EMBO J , vol.16 , pp. 2452-2462
    • Jedlicka, P.1    Mortin, M.A.2    Wu, C.3
  • 14
    • 0001392321 scopus 로고
    • Heat stress protects against coronary endothelial dysfunction after myocardial ischemia and reperfusion in rats
    • Kaeffer N, Richard V and Thuillez C (1995) Heat stress protects against coronary endothelial dysfunction after myocardial ischemia and reperfusion in rats. Circulation 92: I-653.
    • (1995) Circulation , vol.92
    • Kaeffer, N.1    Richard, V.2    Thuillez, C.3
  • 15
    • 0029082019 scopus 로고
    • Thermal protein denaturation and protein aggregation in cells made thermotolerant by various chemicals: Role of heat shock proteins
    • Kampinga HH, Brunsting JF, Stege GJJ, Burgman PWJJ and Konings AWT (1995) Thermal protein denaturation and protein aggregation in cells made thermotolerant by various chemicals: role of heat shock proteins. Exp Cell Res 219: 536-546.
    • (1995) Exp Cell Res , vol.219 , pp. 536-546
    • Kampinga, H.H.1    Brunsting, J.F.2    Stege, G.J.J.3    Pwjj, B.4    Konings, A.W.T.5
  • 16
    • 0025845010 scopus 로고
    • Hyperthermia-induced protection against ischemic injury in gerbils
    • Kitigawa K, Matsumoto M, Kuwabara K et al (1991) Hyperthermia-induced protection against ischemic injury in gerbils. J Cereb Blood Flow Metab 11: 449-452.
    • (1991) J Cereb Blood Flow Metab , vol.11 , pp. 449-452
    • Kitigawa, K.1    Matsumoto, M.2    Kuwabara, K.3
  • 18
    • 0027417852 scopus 로고
    • Induction of chinese hamster hsp27 gene expression in mouse cells confers resistance to heat shock. Hsp27 stabilization of the microfilament organization
    • Lavoie JN, Gingras-Bretori G, Tanguay RM and Landry J (1993) Induction of Chinese hamster hsp27 gene expression in mouse cells confers resistance to heat shock. Hsp27 stabilization of the microfilament organization. J Biol Chem 268: 3420-3429.
    • (1993) J Biol Chem , vol.268 , pp. 3420-3429
    • Lavoie, J.N.1    Gingras-Bretori, G.2    Tanguay, R.M.3    Landry, J.4
  • 19
    • 0344057656 scopus 로고    scopus 로고
    • Heat shock and recovery prevents paraplegia in a model of acute spinal cord ischemia
    • Lena CJ, Shapiro DS and Perdrizet G (1996) Heat shock and recovery prevents paraplegia in a model of acute spinal cord ischemia. Surg Forum 47: 270-271.
    • (1996) Surg Forum , vol.47 , pp. 270-271
    • Lena, C.J.1    Shapiro, D.S.2    Perdrizet, G.3
  • 20
    • 0027199872 scopus 로고
    • Protein denaturation in intact hepatocytes and isolated cellular organelles during heat shock
    • Lepock JR, Frey HE and Ritchie KP (1993) Protein denaturation in intact hepatocytes and isolated cellular organelles during heat shock. J Cell Biol 122: 1267-1276.
    • (1993) J Cell Biol , vol.122 , pp. 1267-1276
    • Lepock, J.R.1    Frey, H.E.2    Ritchie, K.P.3
  • 21
    • 0028958828 scopus 로고
    • Effects of expressing human hsp70 and its deletion derivatives on heat killing and on RNA and protein synthesis
    • Li L, Shen G and Li GC (1995) Effects of expressing human hsp70 and its deletion derivatives on heat killing and on RNA and protein synthesis. Exp Cell Res 217: 460-468.
    • (1995) Exp Cell Res , vol.217 , pp. 460-468
    • Li, L.1    Shen, G.2    Li, G.C.3
  • 22
    • 0026734257 scopus 로고
    • Expression of human hsp70 in rat fibroblasts enhances cell survival and facilitates recovery from translational and transcriptional inhibition following heat shock
    • Liu RY, Li X, Li L and Li GC (1992) Expression of human hsp70 in rat fibroblasts enhances cell survival and facilitates recovery from translational and transcriptional inhibition following heat shock. Cancer Res 52: 3667-3673.
    • (1992) Cancer Res , vol.52 , pp. 3667-3673
    • Liu, R.Y.1    Li, X.2    Li, L.3    Li, G.C.4
  • 23
    • 0027973005 scopus 로고
    • Heat shock proteins hsp90 and hsp70 protect neuronal cells from thermal stress but not from programmed cell death
    • Mailhos C, Howard MK and Latchman DS (1994) Heat shock proteins hsp90 and hsp70 protect neuronal cells from thermal stress but not from programmed cell death. J Neurochem 63: 1787-1795.
    • (1994) J Neurochem , vol.63 , pp. 1787-1795
    • Mailhos, C.1    Howard, M.K.2    Latchman, D.S.3
  • 24
    • 0027163384 scopus 로고
    • Cardiac stress protein elevation 24 hours after brief ischemia or heat stress is associated with resistance to myocardial infarction
    • Marber MS, Latchman DS, Walker JM and Yellon DM (1993) Cardiac stress protein elevation 24 hours after brief ischemia or heat stress is associated with resistance to myocardial infarction. Circulation 88: 1264-1272.
    • (1993) Circulation , vol.88 , pp. 1264-1272
    • Marber, M.S.1    Latchman, D.S.2    Walker, J.M.3    Yellon, D.M.4
  • 25
    • 0028932259 scopus 로고
    • Overexpression of the rat inducible 70-kD heat stress protein in a transgemc mouse increases the resistance of the heart to ischemic injury
    • Marber MS, Mestril R, Chu SH, Sayen MR, Yellon DM and Dillmann WH (1995) Overexpression of the rat inducible 70-kD heat stress protein in a transgemc mouse increases the resistance of the heart to ischemic injury. J Clin Invest 95: 1446-1456.
    • (1995) J Clin Invest , vol.95 , pp. 1446-1456
    • Marber, M.S.1    Mestril, R.2    Chu, S.H.3    Sayen, M.R.4    Yellon, D.M.5    Dillmann, W.H.6
  • 26
    • 0028293462 scopus 로고
    • Expression of inducible stress protein 70 in rat heart rnyogenic cells confers protection against simulated ischemia-induced injury
    • Mestril R, Chi S-H, Sayen MR, O'Reilly K and Dillmann WH (1994) Expression of inducible stress protein 70 in rat heart rnyogenic cells confers protection against simulated ischemia-induced injury. J Clin Invest 93: 759-767.
    • (1994) J Clin Invest , vol.93 , pp. 759-767
    • Mestril, R.1    Chi, S.-H.2    Sayen, M.R.3    O'Reilly, K.4    Dillmann, W.H.5
  • 27
    • 0031032550 scopus 로고    scopus 로고
    • Hsf4, a new member of the human heat shock factor family which lacks properties of a transcriptional activator
    • Nakai A, Tanabe M, Kawazoe Y, Inazawa J, Morimoto, RI and Nagata K (1997) Hsf4, a new member of the human heat shock factor family which lacks properties of a transcriptional activator. Mol Cell Biol 17: 469-481.
    • (1997) Mol Cell Biol , vol.17 , pp. 469-481
    • Nakai, A.1    Tanabe, M.2    Kawazoe, Y.3    Inazawa, J.4    Morimoto, R.I.5    Nagata, K.6
  • 28
    • 0027135501 scopus 로고
    • The function of heat-shock proteins in stress tolerance: Degradation and reactivation of damaged proteins
    • Parsell DA and Lindquist S (1993) The function of heat-shock proteins in stress tolerance: degradation and reactivation of damaged proteins. Annu Rev Genet 27: 437-496.
    • (1993) Annu Rev Genet , vol.27 , pp. 437-496
    • Parsell, D.A.1    Lindquist, S.2
  • 30
    • 0025864313 scopus 로고
    • Molecular cloning and expression of a human heat shock transcription factor, Hsf1
    • Rabindran SK, Giorgi J, Clos J and Wu C (1991) Molecular cloning and expression of a human heat shock transcription factor, Hsf1. Proc Natl Acad Sci USA 88: 6906-6910.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 6906-6910
    • Rabindran, S.K.1    Giorgi, J.2    Clos, J.3    Wu, C.4
  • 31
    • 0028357297 scopus 로고
    • Induction of the heat shock response reduces mortality rate and organ damage in a sepsis-induced acute lung injury model
    • Ribeiro SP, Villar J, Downey GP, Edelson JD and Slutsky AS (1994) Induction of the heat shock response reduces mortality rate and organ damage in a sepsis-induced acute lung injury model. Crit Care Med 22: 914-921.
    • (1994) Crit Care Med , vol.22 , pp. 914-921
    • Ribeiro, S.P.1    Villar, J.2    Downey, G.P.3    Edelson, J.D.4    Slutsky, A.S.5
  • 32
    • 0029737693 scopus 로고    scopus 로고
    • Regulation of mRNA export in response to stress in Saccharomyces cerevisiae
    • Saavedra C, Tung K-S, Amberg DC, Hopper AK and Cole CN (1996) Regulation of mRNA export in response to stress in Saccharomyces cerevisiae. Genes Dev 10: 1608-1620.
    • (1996) Genes Dev , vol.10 , pp. 1608-1620
    • Saavedra, C.1    Tung, K.-S.2    Amberg, D.C.3    Hopper, A.K.4    Cole, C.N.5
  • 33
    • 0030297274 scopus 로고    scopus 로고
    • Induction of hsp70 in HepG2 cells in response to hepatotoxicants
    • Salminen WF, Voellmy R and Roberts SM (1996) Induction of hsp70 in HepG2 cells in response to hepatotoxicants. Toxicol Appl Pharmacol 141: 117-123.
    • (1996) Toxicol Appl Pharmacol , vol.141 , pp. 117-123
    • Salminen, W.F.1    Voellmy, R.2    Roberts, S.M.3
  • 34
    • 0031405439 scopus 로고    scopus 로고
    • Protection against hepatotoxicity by a single dose of amphetamine: The potential role of heat shock protein induction
    • Salminen WF, Voellmy R and Roberts SM (1997) Protection against hepatotoxicity by a single dose of amphetamine: the potential role of heat shock protein induction. Toxicol Appl Pharmacol 147: 247-258.
    • (1997) Toxicol Appl Pharmacol , vol.147 , pp. 247-258
    • Salminen, W.F.1    Voellmy, R.2    Roberts, S.M.3
  • 35
    • 0025989349 scopus 로고
    • Cloning and characterization of two mouse heat shock factors with distinct inducible and constitutive DNA-binding ability
    • Sarge KD, Zimarino V, Holm K, Wu C and Morimoto RI (1991) Cloning and characterization of two mouse heat shock factors with distinct inducible and constitutive DNA-binding ability. Genes Dev 5: 1902-1911.
    • (1991) Genes Dev , vol.5 , pp. 1902-1911
    • Sarge, K.D.1    Zimarino, V.2    Holm, K.3    Wu, C.4    Morimoto, R.I.5
  • 36
    • 0027461364 scopus 로고
    • Activation of heat shock gene transcription by heat shock factor 1 involves oligomerization, acquisition of DNA-binding activity, and nuclear translocation and can occur in the absence of stress
    • Sarge KD, Murphy SP and Morimoto RI (1993) Activation of heat shock gene transcription by heat shock factor 1 involves oligomerization, acquisition of DNA-binding activity, and nuclear translocation and can occur in the absence of stress. Mol Cell Biol 13: 1392-1407.
    • (1993) Mol Cell Biol , vol.13 , pp. 1392-1407
    • Sarge, K.D.1    Murphy, S.P.2    Morimoto, R.I.3
  • 38
    • 0028966256 scopus 로고
    • Transduction of the stress signal and mechanisms of transcriptional regulation of heat shock/stress protein expression in higher eukaryotes
    • Voellmy R (1994) Transduction of the stress signal and mechanisms of transcriptional regulation of heat shock/stress protein expression in higher eukaryotes. Crit Rev Eukaryotic Gene Expr 4: 357-401.
    • (1994) Crit Rev Eukaryotic Gene Expr , vol.4 , pp. 357-401
    • Voellmy, R.1
  • 39
    • 0028150986 scopus 로고
    • Activation of the DNA-binding ability of human heat shock transcription factor may involve the transition from an intramolecular to an intermolecular triple-stranded coiled-coil structure
    • Zuo J, Baler R, Dahl G and Voellmy R (1994) Activation of the DNA-binding ability of human heat shock transcription factor may involve the transition from an intramolecular to an intermolecular triple-stranded coiled-coil structure. Mol Cell Biol 14: 7557-7568.
    • (1994) Mol Cell Biol , vol.14 , pp. 7557-7568
    • Zuo, J.1    Baler, R.2    Dahl, G.3    Voellmy, R.4
  • 40
    • 0029055176 scopus 로고
    • Multiple layers of regulation of human heat shock transcription factor 1
    • Zuo J, Rungger D and Voellmy R (1995) Multiple layers of regulation of human heat shock transcription factor 1. Mol Cell Biol 15: 4319-4330.
    • (1995) Mol Cell Biol , vol.15 , pp. 4319-4330
    • Zuo, J.1    Rungger, D.2    Voellmy, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.