메뉴 건너뛰기




Volumn 11, Issue 1 P.447-888, 2006, Pages 699-707

The application of HSP70 as a target for gene therapy

Author keywords

Cerebral ischemia; Gene therapy; Heat shock protein; HSP70; Stroke

Indexed keywords


EID: 32944469304     PISSN: 27686701     EISSN: 27686698     Source Type: Journal    
DOI: 10.2741/1828     Document Type: Review
Times cited : (16)

References (117)
  • 1
    • 32944460485 scopus 로고
    • Chromosome puffs in drosophila induced by ribonuclease
    • Ritossa, F.M. & Vonborstel, R.C.: Chromosome Puffs in Drosophila Induced by Ribonuclease. Science 145, 513-4 (1964)
    • (1964) Science , vol.145 , pp. 513-514
    • Ritossa, F.M.1    Vonborstel, R.C.2
  • 2
    • 0030154255 scopus 로고    scopus 로고
    • Discovery of the heat shock response
    • Ritossa, F.: Discovery of the heat shock response. Cell Stress Chaperones 1, 97-8 (1996)
    • (1996) Cell Stress Chaperones , vol.1 , pp. 97-98
    • Ritossa, F.1
  • 3
    • 0030119429 scopus 로고    scopus 로고
    • Increases in HSF1 translocation and synthesis in human epidermoid A-431 cells: Role of protein kinase C and [Ca2+]i
    • Ding, X.Z., Smallridge, R.C., Galloway, R.J. & Kiang, J.G.: Increases in HSF1 translocation and synthesis in human epidermoid A-431 cells: role of protein kinase C and [Ca2+]i. J Investig Med 44, 144-53 (1996)
    • (1996) J Investig Med , vol.44 , pp. 144-153
    • Ding, X.Z.1    Smallridge, R.C.2    Galloway, R.J.3    Kiang, J.G.4
  • 4
    • 0018841837 scopus 로고
    • Transition series metals and sulfhydryl reagents induce the synthesis of four proteins in eukaryotic cells
    • Levinson, W., Oppermann, H. & Jackson, J.: Transition series metals and sulfhydryl reagents induce the synthesis of four proteins in eukaryotic cells. Biochim Biophys Acta 606, 170-80 (1980)
    • (1980) Biochim Biophys Acta , vol.606 , pp. 170-180
    • Levinson, W.1    Oppermann, H.2    Jackson, J.3
  • 5
    • 0017665008 scopus 로고
    • Induction of two transformation-sensitive membrane polypeptides in normal fibroblasts by a block in glycoprotein synthesis or glucose deprivation
    • Pouyssegur, J., Shiu, R.P. & Pastan, I.: Induction of two transformation-sensitive membrane polypeptides in normal fibroblasts by a block in glycoprotein synthesis or glucose deprivation. Cell 11, 941-7 (1977)
    • (1977) Cell , vol.11 , pp. 941-947
    • Pouyssegur, J.1    Shiu, R.P.2    Pastan, I.3
  • 6
    • 0030154323 scopus 로고    scopus 로고
    • Influence of molecular and chemical chaperones on protein folding
    • Welch, W.J. & Brown, C.R.: Influence of molecular and chemical chaperones on protein folding. Cell Stress Chaperones 1, 109-15 (1996)
    • (1996) Cell Stress Chaperones , vol.1 , pp. 109-115
    • Welch, W.J.1    Brown, C.R.2
  • 7
    • 0020429331 scopus 로고
    • Molecular and cellular effects of heatshock and related treatments of mammalian tissue-culture cells
    • Thomas, G.P., Welch, W.J., Mathews, M.B. & Feramisco, J.R.: Molecular and cellular effects of heatshock and related treatments of mammalian tissue-culture cells. Cold Spring Harb Symp Quant Biol 46 Pt 2, 985-96 (1982)
    • (1982) Cold Spring Harb Symp Quant Biol , vol.46 , Issue.PART 2 , pp. 985-996
    • Thomas, G.P.1    Welch, W.J.2    Mathews, M.B.3    Feramisco, J.R.4
  • 8
    • 0024430704 scopus 로고
    • Mutational analysis of the human HSP70 protein: Distinct domains for nucleolar localization and adenosine triphosphate binding
    • Milarski, K.L. & Morimoto, R.I.: Mutational analysis of the human HSP70 protein: distinct domains for nucleolar localization and adenosine triphosphate binding. J Cell Biol 109, 1947-62 (1989)
    • (1989) J Cell Biol , vol.109 , pp. 1947-1962
    • Milarski, K.L.1    Morimoto, R.I.2
  • 10
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • Bukau, B. & Horwich, A.L.: The Hsp70 and Hsp60 chaperone machines. Cell 92, 351-66 (1998)
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 11
    • 0027308741 scopus 로고
    • Eukaryotic homologues of Escherichia coli dnaJ: A diverse protein family that functions with hsp70 stress proteins
    • Caplan, A.J., Cyr, D.M. & Douglas, M.G.: Eukaryotic homologues of Escherichia coli dnaJ: a diverse protein family that functions with hsp70 stress proteins. Mol Biol Cell 4, 555-63 (1993)
    • (1993) Mol Biol Cell , vol.4 , pp. 555-563
    • Caplan, A.J.1    Cyr, D.M.2    Douglas, M.G.3
  • 12
    • 0000012053 scopus 로고
    • Major heat shock gene of Drosophila and the Escherichia coli heat-inducible dnaK gene are homologous
    • Bardwell, J.C. & Craig, E.A.: Major heat shock gene of Drosophila and the Escherichia coli heat-inducible dnaK gene are homologous. Proc Natl Acad Sci U S A 81, 848-52 (1984)
    • (1984) Proc Natl Acad Sci U S A , vol.81 , pp. 848-852
    • Bardwell, J.C.1    Craig, E.A.2
  • 13
    • 0036084783 scopus 로고    scopus 로고
    • Heat shock proteins: Modifying factors in physiological stress responses and acquired thermotolerance
    • Kregel, K.C.: Heat shock proteins: modifying factors in physiological stress responses and acquired thermotolerance. J Appl Physiol 92, 2177-86 (2002)
    • (2002) J Appl Physiol , vol.92 , pp. 2177-2186
    • Kregel, K.C.1
  • 15
    • 0025153234 scopus 로고
    • Molecular biology of circulatory shock. Part III. Human hepatoblastoma (HepG2) cells demonstrate two patterns of shock-induced gene expression that are independent, exclusive, and prioritized
    • Cabin, D.E. & Buchman, T.G.: Molecular biology of circulatory shock. Part III. Human hepatoblastoma (HepG2) cells demonstrate two patterns of shock-induced gene expression that are independent, exclusive, and prioritized. Surgery 108, 902-12 (1990)
    • (1990) Surgery , vol.108 , pp. 902-912
    • Cabin, D.E.1    Buchman, T.G.2
  • 16
    • 0036944277 scopus 로고    scopus 로고
    • Heat shock proteins and neuroprotection
    • Yenari, M.A.: Heat shock proteins and neuroprotection. Adv Exp Med Biol 513, 281-99 (2002)
    • (2002) Adv Exp Med Biol , vol.513 , pp. 281-299
    • Yenari, M.A.1
  • 18
    • 0023251292 scopus 로고
    • Detection of three protein binding sites in the serum-regulated promoter of the human gene encoding the 70-kDa heat shock protein
    • Wu, B.J., Williams, G.T. & Morimoto, R.I.: Detection of three protein binding sites in the serum-regulated promoter of the human gene encoding the 70-kDa heat shock protein. Proc Natl Acad Sci U S A 84, 2203-7 (1987)
    • (1987) Proc Natl Acad Sci U S A , vol.84 , pp. 2203-2207
    • Wu, B.J.1    Williams, G.T.2    Morimoto, R.I.3
  • 19
    • 0012111663 scopus 로고
    • Human HSP70 promoter contains at least two distinct regulatory domains
    • Wu, B.J., Kingston, R.E. & Morimoto, R.I.: Human HSP70 promoter contains at least two distinct regulatory domains. Proc Natl Acad Sci U S A 83, 629-33 (1986)
    • (1986) Proc Natl Acad Sci U S A , vol.83 , pp. 629-633
    • Wu, B.J.1    Kingston, R.E.2    Morimoto, R.I.3
  • 20
    • 0025300038 scopus 로고
    • In vitro activation of heat shock transcription factor DNA-binding by calcium and biochemical conditions that affect protein conformation
    • Mosser, D.D., Kotzbauer, P.T., Sarge, K.D. & Morimoto, R.I.: In vitro activation of heat shock transcription factor DNA-binding by calcium and biochemical conditions that affect protein conformation. Proc Natl Acad Sci U S A 87, 3748-52 (1990)
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 3748-3752
    • Mosser, D.D.1    Kotzbauer, P.T.2    Sarge, K.D.3    Morimoto, R.I.4
  • 21
    • 0025922155 scopus 로고
    • Ca2+ is essential for multistep activation of the heat shock factor in permeabilized cells
    • Price, B.D. & Calderwood, S.K.: Ca2+ is essential for multistep activation of the heat shock factor in permeabilized cells. Mol Cell Biol 11, 3365-8 (1991)
    • (1991) Mol Cell Biol , vol.11 , pp. 3365-3368
    • Price, B.D.1    Calderwood, S.K.2
  • 22
    • 0028168920 scopus 로고
    • Role of cytosolic Ca2+ and protein kinases in the induction of the hsp70 gene
    • Yamamoto, N., Smith, M.W., Maki, A., Berezesky, I.K. & Trump, B.F.: Role of cytosolic Ca2+ and protein kinases in the induction of the hsp70 gene. Kidney Int 45, 1093-104 (1994)
    • (1994) Kidney Int , vol.45 , pp. 1093-1104
    • Yamamoto, N.1    Smith, M.W.2    Maki, A.3    Berezesky, I.K.4    Trump, B.F.5
  • 23
    • 0028988077 scopus 로고
    • Physiological and pharmacological inhibitors of luteinizing hormone-dependent steroidogenesis induce heat shock protein-70 in rat luteal cells
    • Khanna, A., Aten, R.F. & Behrman, H.R.: Physiological and pharmacological inhibitors of luteinizing hormone-dependent steroidogenesis induce heat shock protein-70 in rat luteal cells. Endocrinology 136, 1775-81 (1995)
    • (1995) Endocrinology , vol.136 , pp. 1775-1781
    • Khanna, A.1    Aten, R.F.2    Behrman, H.R.3
  • 24
    • 0031895617 scopus 로고    scopus 로고
    • Overexpression of HSP-70 inhibits the phosphorylation of HSF1 by activating protein phosphatase and inhibiting protein kinase C activity
    • Ding, X.Z., Tsokos, G.C. & Kiang, J.G.: Overexpression of HSP-70 inhibits the phosphorylation of HSF1 by activating protein phosphatase and inhibiting protein kinase C activity. Faseb J 12, 451-9 (1998)
    • (1998) Faseb J , vol.12 , pp. 451-459
    • Ding, X.Z.1    Tsokos, G.C.2    Kiang, J.G.3
  • 25
    • 0023515282 scopus 로고
    • Mechanisms of heat-shock gene activation in higher eukaryotes
    • Bienz, M. & Pelham, H.R.: Mechanisms of heat-shock gene activation in higher eukaryotes. Adv Genet 24, 31-72 (1987)
    • (1987) Adv Genet , vol.24 , pp. 31-72
    • Bienz, M.1    Pelham, H.R.2
  • 26
    • 0023863121 scopus 로고
    • Germline transformation used to define key features of heat-shock response elements
    • Xiao, H. & Lis, J.T.: Germline transformation used to define key features of heat-shock response elements. Science 239, 1139-42 (1988)
    • (1988) Science , vol.239 , pp. 1139-1142
    • Xiao, H.1    Lis, J.T.2
  • 27
    • 0023694311 scopus 로고
    • Key features of heat shock regulatory elements
    • Amin, J., Ananthan, J. & Voellmy, R.: Key features of heat shock regulatory elements. Mol Cell Biol 8, 3761-9 (1988)
    • (1988) Mol Cell Biol , vol.8 , pp. 3761-3769
    • Amin, J.1    Ananthan, J.2    Voellmy, R.3
  • 28
    • 0027195230 scopus 로고
    • Mouse heat shock transcription factors 1 and 2 prefer a trimeric binding site but interact differently with the HSP70 heat shock element
    • Kroeger, P.E., Sarge, K.D. & Morimoto, R.I.: Mouse heat shock transcription factors 1 and 2 prefer a trimeric binding site but interact differently with the HSP70 heat shock element. Mol Cell Biol 13, 3370-83 (1993)
    • (1993) Mol Cell Biol , vol.13 , pp. 3370-3383
    • Kroeger, P.E.1    Sarge, K.D.2    Morimoto, R.I.3
  • 29
    • 0024282788 scopus 로고
    • Isolation of the gene encoding the S. cerevisiae heat shock transcription factor
    • Wiederrecht, G., Seto, D. & Parker, C.S.: Isolation of the gene encoding the S. cerevisiae heat shock transcription factor. Cell 54, 841-53 (1988)
    • (1988) Cell , vol.54 , pp. 841-853
    • Wiederrecht, G.1    Seto, D.2    Parker, C.S.3
  • 30
    • 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, R.I. & Nagata, K.: HSF4, a new member of the human heat shock factor family which lacks properties of a transcriptional activator. Mol Cell Biol 17, 469-81 (1997)
    • (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
  • 31
    • 0030049318 scopus 로고    scopus 로고
    • The regulatory domain of human heat shock factor 1 is sufficient to sense heat stress
    • Newton, E.M., Knauf, U., Green, M. & Kingston, R.E.: The regulatory domain of human heat shock factor 1 is sufficient to sense heat stress. Mol Cell Biol 16, 839-46 (1996)
    • (1996) Mol Cell Biol , vol.16 , pp. 839-846
    • Newton, E.M.1    Knauf, U.2    Green, M.3    Kingston, R.E.4
  • 33
    • 0025330639 scopus 로고
    • Heat shock proteins
    • Schlesinger, M.J.: Heat shock proteins. J Biol Chem 265, 12111-4 (1990)
    • (1990) J Biol Chem , vol.265 , pp. 12111-12114
    • Schlesinger, M.J.1
  • 34
    • 0031793127 scopus 로고    scopus 로고
    • Heat shock protein 70 kDa: Molecular biology, biochemistry, and physiology
    • Kiang, J.G. & Tsokos, G.C.: Heat shock protein 70 kDa: molecular biology, biochemistry, and physiology. Pharmacol Ther 80, 183-201 (1998)
    • (1998) Pharmacol Ther , vol.80 , pp. 183-201
    • Kiang, J.G.1    Tsokos, G.C.2
  • 35
    • 0027522356 scopus 로고
    • Cells in stress: Transcriptional activation of heat shock genes
    • Morimoto, R.I.: Cells in stress: transcriptional activation of heat shock genes. Science 259, 1409-10 (1993)
    • (1993) Science , vol.259 , pp. 1409-1410
    • Morimoto, R.I.1
  • 36
    • 0027202273 scopus 로고
    • The DNA-binding activity of the human heat shock transcription factor is regulated in vivo by hsp70
    • Mosser, D.D., Duchaine, J. & Massie, B.: The DNA-binding activity of the human heat shock transcription factor is regulated in vivo by hsp70. Mol Cell Biol 13, 5427-38 (1993)
    • (1993) Mol Cell Biol , vol.13 , pp. 5427-5438
    • Mosser, D.D.1    Duchaine, J.2    Massie, B.3
  • 37
    • 0028960212 scopus 로고
    • Heat shock protein hsp70 accelerates the recovery of heat-shocked mammalian cells through its modulation of heat shock transcription factor HSF1
    • Kim, D., Ouyang, H. & Li, G.C.: Heat shock protein hsp70 accelerates the recovery of heat-shocked mammalian cells through its modulation of heat shock transcription factor HSF1. Proc Natl Acad Sci U S A 92, 2126-30 (1995)
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 2126-2130
    • Kim, D.1    Ouyang, H.2    Li, G.C.3
  • 40
    • 0028958602 scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl, F.U. & Martin, J.: Molecular chaperones in cellular protein folding. Curr Opin Struct Biol 5, 92-102 (1995)
    • (1995) Curr Opin Struct Biol , vol.5 , pp. 92-102
    • Hartl, F.U.1    Martin, J.2
  • 41
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: From nascent chain to folded protein
    • Hartl, F.U. & Hayer-Hartl, M.: Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295, 1852-8 (2002)
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 42
    • 0642377466 scopus 로고    scopus 로고
    • More than folding: Localized functions of cytosolic chaperones
    • Young, J.C., Barral, J.M. & Ulrich Hartl, F.: More than folding: localized functions of cytosolic chaperones. Trends Biochem Sci 28, 541-7 (2003)
    • (2003) Trends Biochem Sci , vol.28 , pp. 541-547
    • Young, J.C.1    Barral, J.M.2    Ulrich Hartl, F.3
  • 43
    • 0036343904 scopus 로고    scopus 로고
    • The protein import motor of mitochondria
    • Neupert, W. & Brunner, M.: The protein import motor of mitochondria. Nat Rev Mol Cell Biol 3, 555-65 (2002)
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 555-565
    • Neupert, W.1    Brunner, M.2
  • 44
    • 0037315208 scopus 로고    scopus 로고
    • Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery
    • Pratt, W.B. & Toft, D.O.: Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery. Exp Biol Med (Maywood) 228, 111-33 (2003)
    • (2003) Exp Biol Med (Maywood) , vol.228 , pp. 111-133
    • Pratt, W.B.1    Toft, D.O.2
  • 45
    • 11444271010 scopus 로고    scopus 로고
    • Chaperone-assisted folding of newly synthesized proteins in the cytosol
    • Deuerling, E. & Bukau, B.: Chaperone-assisted folding of newly synthesized proteins in the cytosol. Crit Rev Biochem Mol Biol 39, 261-77 (2004)
    • (2004) Crit Rev Biochem Mol Biol , vol.39 , pp. 261-277
    • Deuerling, E.1    Bukau, B.2
  • 46
    • 17044387386 scopus 로고    scopus 로고
    • Hsp70 chaperones: Cellular functions and molecular mechanism
    • Mayer, M.P. & Bukau, B.: Hsp70 chaperones: cellular functions and molecular mechanism. Cell Mol Life Sci 62, 670-84 (2005)
    • (2005) Cell Mol Life Sci , vol.62 , pp. 670-684
    • Mayer, M.P.1    Bukau, B.2
  • 47
    • 0026687729 scopus 로고
    • An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins
    • Bork, P., Sander, C. & Valencia, A.: An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins. Proc Natl Acad Sci U S A 89, 7290-4 (1992)
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 7290-7294
    • Bork, P.1    Sander, C.2    Valencia, A.3
  • 48
    • 0029038683 scopus 로고
    • The peptide-binding domain of the chaperone protein Hsc70 has an unusual secondary structure topology
    • Morshauser, R.C., Wang, H., Flynn, G.C. & Zuiderweg, E.R.: The peptide-binding domain of the chaperone protein Hsc70 has an unusual secondary structure topology. Biochemistry 34, 6261-6 (1995)
    • (1995) Biochemistry , vol.34 , pp. 6261-6266
    • Morshauser, R.C.1    Wang, H.2    Flynn, G.C.3    Zuiderweg, E.R.4
  • 49
    • 0031030098 scopus 로고    scopus 로고
    • A 16-kDa protein functions as a new regulatory protein for Hsc70 molecular chaperone and is identified as a member of the Nm23/nucleoside diphosphate kinase family
    • Leung, S.M. & Hightower, L.E.: A 16-kDa protein functions as a new regulatory protein for Hsc70 molecular chaperone and is identified as a member of the Nm23/nucleoside diphosphate kinase family. J Biol Chem 272, 2607-14 (1997)
    • (1997) J Biol Chem , vol.272 , pp. 2607-2614
    • Leung, S.M.1    Hightower, L.E.2
  • 50
    • 0025100372 scopus 로고
    • Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein
    • Flaherty, K.M., DeLuca-Flaherty, C. & McKay, D.B.: Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein. Nature 346, 623-8 (1990)
    • (1990) Nature , vol.346 , pp. 623-628
    • Flaherty, K.M.1    DeLuca-Flaherty, C.2    McKay, D.B.3
  • 51
    • 0027433805 scopus 로고
    • Identification of the peptide binding domain of hsc70. 18-Kilodalton fragment located immediately after ATPase domain is sufficient for high affinity binding
    • Wang, T.F., Chang, J.H. & Wang, C.: Identification of the peptide binding domain of hsc70. 18-Kilodalton fragment located immediately after ATPase domain is sufficient for high affinity binding. J Biol Chem 268, 26049-51 (1993)
    • (1993) J Biol Chem , vol.268 , pp. 26049-26051
    • Wang, T.F.1    Chang, J.H.2    Wang, C.3
  • 52
    • 0033936317 scopus 로고    scopus 로고
    • Multistep mechanism of substrate binding determines chaperone activity of Hsp70
    • Mayer, M.P., Schroder, H., Rudiger, S., Paal, K., Laufen, T. & Bukau, B.: Multistep mechanism of substrate binding determines chaperone activity of Hsp70. Nat Struct Biol 7, 586-93 (2000)
    • (2000) Nat Struct Biol , vol.7 , pp. 586-593
    • Mayer, M.P.1    Schroder, H.2    Rudiger, S.3    Paal, K.4    Laufen, T.5    Bukau, B.6
  • 53
    • 0034662746 scopus 로고    scopus 로고
    • The crystal structure of the peptide-binding fragment from the yeast Hsp40 protein Sis1
    • Sha, B., Lee, S. & Cyr, D.M.: The crystal structure of the peptide-binding fragment from the yeast Hsp40 protein Sis1. Structure Fold Des 8, 799-807 (2000)
    • (2000) Structure Fold des , vol.8 , pp. 799-807
    • Sha, B.1    Lee, S.2    Cyr, D.M.3
  • 54
    • 0035119624 scopus 로고    scopus 로고
    • GrpE accelerates peptide binding and release from the high affinity state of DnaK
    • Mally, A. & Witt, S.N.: GrpE accelerates peptide binding and release from the high affinity state of DnaK. Nat Struct Biol 8, 254-7 (2001)
    • (2001) Nat Struct Biol , vol.8 , pp. 254-257
    • Mally, A.1    Witt, S.N.2
  • 55
    • 0037330236 scopus 로고    scopus 로고
    • Interdomain communication in the molecular chaperone DnaK
    • Han, W. & Christen, P.: Interdomain communication in the molecular chaperone DnaK. Biochem J 369, 627-34 (2003)
    • (2003) Biochem J , vol.369 , pp. 627-634
    • Han, W.1    Christen, P.2
  • 56
  • 58
    • 0020771639 scopus 로고
    • Relationship between hyperthermia-induced heat-shock proteins and thermotolerance in Morris hepatoma cells
    • Landry, J. & Chretien, P.: Relationship between hyperthermia-induced heat-shock proteins and thermotolerance in Morris hepatoma cells. Can J Biochem Cell Biol 61, 428-37 (1983)
    • (1983) Can J Biochem Cell Biol , vol.61 , pp. 428-437
    • Landry, J.1    Chretien, P.2
  • 59
    • 0021089337 scopus 로고
    • Heat-induced protection of mice against thermal death
    • Li, G.C., Meyer, J.L., Mak, J.Y. & Hahn, G.M.: Heat-induced protection of mice against thermal death. Cancer Res 43, 5758-60 (1983)
    • (1983) Cancer Res , vol.43 , pp. 5758-5760
    • Li, G.C.1    Meyer, J.L.2    Mak, J.Y.3    Hahn, G.M.4
  • 60
    • 0026642374 scopus 로고
    • Prognostic influence of HSP-27 expression in malignant fibrous histiocytoma: A clinicopathological and immunohistochemical study
    • Tetu, B., Lacasse, B., Bouchard, H.L., Lagace, R., Huot, J. & Landry, J.: Prognostic influence of HSP-27 expression in malignant fibrous histiocytoma: a clinicopathological and immunohistochemical study. Cancer Res 52, 2325-8 (1992)
    • (1992) Cancer Res , vol.52 , pp. 2325-2328
    • Tetu, B.1    Lacasse, B.2    Bouchard, H.L.3    Lagace, R.4    Huot, J.5    Landry, J.6
  • 62
    • 0023231632 scopus 로고
    • Effects of ischemia and perfusion temperature on the synthesis of stress-induced (heat shock) proteins in isolated and perfused rat hearts
    • Currie, R.W.: Effects of ischemia and perfusion temperature on the synthesis of stress-induced (heat shock) proteins in isolated and perfused rat hearts. J Mol Cell Cardiol 19, 795-808 (1987)
    • (1987) J Mol Cell Cardiol , vol.19 , pp. 795-808
    • Currie, R.W.1
  • 63
    • 0022546075 scopus 로고
    • Ischemia of the dog heart induces the appearance of a cardiac mRNA coding for a protein with migration characteristics similar to heat-shock/stress protein 71
    • Dillmann, W.H., Mehta, H.B., Barrieux, A., Guth, B.D., Neeley, W.E. & Ross, J., Jr.: Ischemia of the dog heart induces the appearance of a cardiac mRNA coding for a protein with migration characteristics similar to heat-shock/stress protein 71. Circ Res 59, 110-4 (1986)
    • (1986) Circ Res , vol.59 , pp. 110-114
    • Dillmann, W.H.1    Mehta, H.B.2    Barrieux, A.3    Guth, B.D.4    Neeley, W.E.5    Ross Jr., J.6
  • 65
    • 85047677579 scopus 로고
    • Hypoxic preconditioning of ischaemic myocardium
    • Marber, M.S. & Yellon, D.M.: Hypoxic preconditioning of ischaemic myocardium. Cardiovasc Res 26, 556-7 (1992)
    • (1992) Cardiovasc Res , vol.26 , pp. 556-557
    • Marber, M.S.1    Yellon, D.M.2
  • 68
    • 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, B.K., Stephanou, A., Wagstaff, M.J., Coffin, R.S., Marber, M.S., Engelmann, G. & Latchman, D.S.: 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 31, 135-46 (1999)
    • (1999) J Mol Cell Cardiol , vol.31 , pp. 135-146
    • Brar, B.K.1    Stephanou, A.2    Wagstaff, M.J.3    Coffin, R.S.4    Marber, M.S.5    Engelmann, G.6    Latchman, D.S.7
  • 69
    • 0034862016 scopus 로고    scopus 로고
    • Heat shock proteins and cardiac protection
    • Latchman, D.S.: Heat shock proteins and cardiac protection. Cardiovasc Res 51, 637-46 (2001)
    • (2001) Cardiovasc Res , vol.51 , pp. 637-646
    • Latchman, D.S.1
  • 70
    • 0028932259 scopus 로고
    • Overexpression of the rat inducible 70-kD heat stress protein in a transgenic mouse increases the resistance of the heart to ischemic injury
    • Marber, M.S., Mestril, R., Chi, S.H., Sayen, M.R., Yellon, D.M. & Dillmann, W.H.: Overexpression of the rat inducible 70-kD heat stress protein in a transgenic mouse increases the resistance of the heart to ischemic injury. J Clin Invest 95, 1446-56 (1995)
    • (1995) J Clin Invest , vol.95 , pp. 1446-1456
    • Marber, M.S.1    Mestril, R.2    Chi, S.H.3    Sayen, M.R.4    Yellon, D.M.5    Dillmann, W.H.6
  • 71
    • 0029794271 scopus 로고    scopus 로고
    • Overexpression of heat shock protein 72 in transgenic mice decreases infarct size in vivo
    • Hutter, J.J., Mestril, R., Tam, E.K., Sievers, R.E., Dillmann, W.H. & Wolfe, C.L.: Overexpression of heat shock protein 72 in transgenic mice decreases infarct size in vivo. Circulation 94, 1408-11 (1996)
    • (1996) Circulation , vol.94 , pp. 1408-1411
    • Hutter, J.J.1    Mestril, R.2    Tam, E.K.3    Sievers, R.E.4    Dillmann, W.H.5    Wolfe, C.L.6
  • 74
  • 75
    • 0036357322 scopus 로고    scopus 로고
    • Neuroprotection: Heat shock proteins
    • Kelly, S. & Yenari, M.A.: Neuroprotection: heat shock proteins. Curr Med Res Opin 18 Suppl 2, s55-60 (2002)
    • (2002) Curr Med Res Opin , vol.18 , Issue.SUPPL. 2
    • Kelly, S.1    Yenari, M.A.2
  • 76
    • 0035211413 scopus 로고    scopus 로고
    • Targeted hsp70.1 disruption increases infarction volume after focal cerebral ischemia in mice
    • Lee, S.H., Kim, M., Yoon, B.W., Kim, Y.J., Ma, S.J., Roh, J.K., Lee, J.S. & Seo, J.S.: Targeted hsp70.1 disruption increases infarction volume after focal cerebral ischemia in mice. Stroke 32, 2905-12 (2001)
    • (2001) Stroke , vol.32 , pp. 2905-2912
    • Lee, S.H.1    Kim, M.2    Yoon, B.W.3    Kim, Y.J.4    Ma, S.J.5    Roh, J.K.6    Lee, J.S.7    Seo, J.S.8
  • 77
    • 0348223798 scopus 로고    scopus 로고
    • Many mechanisms for hsp70 protection from cerebral ischemia
    • Giffard, R.G. & Yenari, M.A.: Many mechanisms for hsp70 protection from cerebral ischemia. J Neurosurg Anesthesiol 16, 53-61 (2004)
    • (2004) J Neurosurg Anesthesiol , vol.16 , pp. 53-61
    • Giffard, R.G.1    Yenari, M.A.2
  • 78
    • 0029952943 scopus 로고    scopus 로고
    • DNA fragmentation and HSP70 protein induction in hippocampus and cortex occurs in separate neurons following permanent middle cerebral artery occlusions
    • States, B.A., Honkaniemi, J., Weinstein, P.R. & Sharp, F.R.: DNA fragmentation and HSP70 protein induction in hippocampus and cortex occurs in separate neurons following permanent middle cerebral artery occlusions. J Cereb Blood Flow Metab 16, 1165-75 (1996)
    • (1996) J Cereb Blood Flow Metab , vol.16 , pp. 1165-1175
    • States, B.A.1    Honkaniemi, J.2    Weinstein, P.R.3    Sharp, F.R.4
  • 79
    • 10744224462 scopus 로고    scopus 로고
    • Overexpression of rat heat shock protein 70 reduces neuronal injury after transient focal ischemia, transient global ischemia, or kainic acid-induced seizures
    • Tsuchiya, D., Hong, S., Matsumori, Y., Kayama, T., Swanson, R.A., Dillman, W.H., Liu, J., Panter, S.S. & Weinstein, P.R.: Overexpression of rat heat shock protein 70 reduces neuronal injury after transient focal ischemia, transient global ischemia, or kainic acid-induced seizures. Neurosurgery 53, 1179-87 (2003)
    • (2003) Neurosurgery , vol.53 , pp. 1179-1187
    • Tsuchiya, D.1    Hong, S.2    Matsumori, Y.3    Kayama, T.4    Swanson, R.A.5    Dillman, W.H.6    Liu, J.7    Panter, S.S.8    Weinstein, P.R.9
  • 81
    • 0036329676 scopus 로고    scopus 로고
    • Gene transfer of HSP72 protects cornu ammonis 1 region of the hippocampus neurons from global ischemia: Influence of Bcl-2
    • Kelly, S., Zhang, Z.J., Zhao, H., Xu, L., Giffard, R.G., Sapolsky, R.M., Yenari, M.A. & Steinberg, G.K.: Gene transfer of HSP72 protects cornu ammonis 1 region of the hippocampus neurons from global ischemia: influence of Bcl-2. Ann Neurol 52, 160-7 (2002)
    • (2002) Ann Neurol , vol.52 , pp. 160-167
    • Kelly, S.1    Zhang, Z.J.2    Zhao, H.3    Xu, L.4    Giffard, R.G.5    Sapolsky, R.M.6    Yenari, M.A.7    Steinberg, G.K.8
  • 82
    • 4344571747 scopus 로고    scopus 로고
    • Effects of hsp70.1 gene knockout on the mitochondrial apoptotic pathway after focal cerebral ischemia
    • Lee, S.H., Kwon, H.M., Kim, Y.J., Lee, K.M., Kim, M. & Yoon, B.W.: Effects of hsp70.1 gene knockout on the mitochondrial apoptotic pathway after focal cerebral ischemia. Stroke 35, 2195-9 (2004)
    • (2004) Stroke , vol.35 , pp. 2195-2199
    • Lee, S.H.1    Kwon, H.M.2    Kim, Y.J.3    Lee, K.M.4    Kim, M.5    Yoon, B.W.6
  • 84
    • 0032582562 scopus 로고    scopus 로고
    • Role of Hsp70 in regulation of stress-kinase JNK: Implications in apoptosis and aging
    • Gabai, V.L., Meriin, A.B., Yaglom, J.A., Volloch, V.Z. & Sherman, M.Y.: Role of Hsp70 in regulation of stress-kinase JNK: implications in apoptosis and aging. FEBS Lett 438, 1-4 (1998)
    • (1998) FEBS Lett , vol.438 , pp. 1-4
    • Gabai, V.L.1    Meriin, A.B.2    Yaglom, J.A.3    Volloch, V.Z.4    Sherman, M.Y.5
  • 86
    • 0035182221 scopus 로고    scopus 로고
    • Stress management - Heat shock protein-70 and the regulation of apoptosis
    • Beere, H.M. & Green, D.R.: Stress management - heat shock protein-70 and the regulation of apoptosis. Trends Cell Biol 11, 6-10 (2001)
    • (2001) Trends Cell Biol , vol.11 , pp. 6-10
    • Beere, H.M.1    Green, D.R.2
  • 87
    • 0030601799 scopus 로고    scopus 로고
    • Influence of heat shock protein 70 and metallothionein induction by zinc-bis-(DL-hydrogenaspartate) on the release of inflammatory mediators in a porcine model of recurrent endotoxemia
    • Klosterhalfen, B., Tons, C., Hauptmann, S., Tietze, L., Offner, F.A., Kupper, W. & Kirkpatrick, C.J.: Influence of heat shock protein 70 and metallothionein induction by zinc-bis-(DL-hydrogenaspartate) on the release of inflammatory mediators in a porcine model of recurrent endotoxemia. Biochem Pharmacol 52, 1201-10 (1996)
    • (1996) Biochem Pharmacol , vol.52 , pp. 1201-1210
    • Klosterhalfen, B.1    Tons, C.2    Hauptmann, S.3    Tietze, L.4    Offner, F.A.5    Kupper, W.6    Kirkpatrick, C.J.7
  • 89
    • 0037069397 scopus 로고    scopus 로고
    • Preoperative glutamine administration induces heat-shock protein 70 expression and attenuates cardiopulmonary bypass-induced inflammatory response by regulating nitric oxide synthase activity
    • Hayashi, Y., Sawa, Y., Fukuyama, N., Nakazawa, H. & Matsuda, H.: Preoperative glutamine administration induces heat-shock protein 70 expression and attenuates cardiopulmonary bypass-induced inflammatory response by regulating nitric oxide synthase activity. Circulation 106, 2601-7 (2002)
    • (2002) Circulation , vol.106 , pp. 2601-2607
    • Hayashi, Y.1    Sawa, Y.2    Fukuyama, N.3    Nakazawa, H.4    Matsuda, H.5
  • 90
    • 0035931040 scopus 로고    scopus 로고
    • Over-expression of hsp-70 inhibits bacterial lipopolysaccharide-induced production of cytokines in human monocyte-derived macrophages
    • Ding, X.Z., Fernandez-Prada, C.M., Bhattacharjee, A.K. & Hoover, D.L.: Over-expression of hsp-70 inhibits bacterial lipopolysaccharide-induced production of cytokines in human monocyte-derived macrophages. Cytokine 16, 210-9 (2001)
    • (2001) Cytokine , vol.16 , pp. 210-219
    • Ding, X.Z.1    Fernandez-Prada, C.M.2    Bhattacharjee, A.K.3    Hoover, D.L.4
  • 91
    • 0036738485 scopus 로고    scopus 로고
    • Adenoviral transfer of HSP-70 into pulmonary epithelium ameliorates experimental acute respiratory distress syndrome
    • Weiss, Y.G., Maloyan, A., Tazelaar, J., Raj, N. & Deutschman, C.S.: Adenoviral transfer of HSP-70 into pulmonary epithelium ameliorates experimental acute respiratory distress syndrome. J Clin Invest 110, 801-6 (2002)
    • (2002) J Clin Invest , vol.110 , pp. 801-806
    • Weiss, Y.G.1    Maloyan, A.2    Tazelaar, J.3    Raj, N.4    Deutschman, C.S.5
  • 92
    • 0032984459 scopus 로고    scopus 로고
    • Endotoxin inhibits heat shock protein 70 (HSP70) expression in peripheral blood mononuclear cells of patients with severe sepsis
    • Schroeder, S., Bischoff, J., Lehmann, L.E., Hering, R., von Spiegel, T., Putensen, C., Hoeft, A. & Stuber, F.: Endotoxin inhibits heat shock protein 70 (HSP70) expression in peripheral blood mononuclear cells of patients with severe sepsis. Intensive Care Med 25, 52-7 (1999)
    • (1999) Intensive Care Med , vol.25 , pp. 52-57
    • Schroeder, S.1    Bischoff, J.2    Lehmann, L.E.3    Hering, R.4    Von Spiegel, T.5    Putensen, C.6    Hoeft, A.7    Stuber, F.8
  • 93
    • 0033918085 scopus 로고    scopus 로고
    • Heat shock protein 70 prevents secretagogue-induced cell injury in the pancreas by preventing intracellular trypsinogen activation
    • Bhagat, L., Singh, V.P., Hietaranta, A.J., Agrawal, S., Steer, M.L. & Saluja, A.K.: Heat shock protein 70 prevents secretagogue-induced cell injury in the pancreas by preventing intracellular trypsinogen activation. J Clin Invest 106, 81-9 (2000)
    • (2000) J Clin Invest , vol.106 , pp. 81-89
    • Bhagat, L.1    Singh, V.P.2    Hietaranta, A.J.3    Agrawal, S.4    Steer, M.L.5    Saluja, A.K.6
  • 96
    • 0242367234 scopus 로고    scopus 로고
    • Medicine. Gene therapy - New challenges ahead
    • Williams, D.A. & Baum, C.: Medicine. Gene therapy-new challenges ahead. Science 302, 400-1 (2003)
    • (2003) Science , vol.302 , pp. 400-401
    • Williams, D.A.1    Baum, C.2
  • 97
    • 0037135078 scopus 로고    scopus 로고
    • Tech.Sight. Gene therapy. Hurdles and hopes for cancer treatment
    • Hunt, K.K. & Vorburger, S.A.: Tech.Sight. Gene therapy. Hurdles and hopes for cancer treatment. Science 297, 415-6 (2002)
    • (2002) Science , vol.297 , pp. 415-416
    • Hunt, K.K.1    Vorburger, S.A.2
  • 100
    • 0034943590 scopus 로고    scopus 로고
    • Gene therapy for treatment of cerebral ischemia using defective herpes simplex viral vectors
    • Yenari, M.A., Dumas, T.C., Sapolsky, R.M. & Steinberg, G.K.: Gene therapy for treatment of cerebral ischemia using defective herpes simplex viral vectors. Neurol Res 23, 543-52 (2001)
    • (2001) Neurol Res , vol.23 , pp. 543-552
    • Yenari, M.A.1    Dumas, T.C.2    Sapolsky, R.M.3    Steinberg, G.K.4
  • 102
    • 0034904436 scopus 로고    scopus 로고
    • Targeting expression of hsp70i to discrete neuronal populations using the Lmo-1 promoter: Assessment of the neuroprotective effects of hsp70i in vivo and in vitro
    • Kelly, S., Bieneman, A., Horsburgh, K., Hughes, D., Sofroniew, M.V., McCulloch, J. & Uney, J.B.: Targeting expression of hsp70i to discrete neuronal populations using the Lmo-1 promoter: assessment of the neuroprotective effects of hsp70i in vivo and in vitro. J Cereb Blood Flow Metab 21, 972-81 (2001)
    • (2001) J Cereb Blood Flow Metab , vol.21 , pp. 972-981
    • Kelly, S.1    Bieneman, A.2    Horsburgh, K.3    Hughes, D.4    Sofroniew, M.V.5    McCulloch, J.6    Uney, J.B.7
  • 104
    • 0031020041 scopus 로고    scopus 로고
    • Defective herpes simplex virus vectors expressing the rat brain stress-inducible heat shock protein 72 protect cultured neurons from severe heat shock
    • Fink, S.L., Chang, L.K., Ho, D.Y. & Sapolsky, R.M.: Defective herpes simplex virus vectors expressing the rat brain stress-inducible heat shock protein 72 protect cultured neurons from severe heat shock. J Neurochem 68, 961-9 (1997)
    • (1997) J Neurochem , vol.68 , pp. 961-969
    • Fink, S.L.1    Chang, L.K.2    Ho, D.Y.3    Sapolsky, R.M.4
  • 105
    • 0036319568 scopus 로고    scopus 로고
    • Geldanamycin induces heat shock proteins in brain and protects against focal cerebral ischemia
    • Lu, A., Ran, R., Parmentier-Batteur, S., Nee, A. & Sharp, F.R.: Geldanamycin induces heat shock proteins in brain and protects against focal cerebral ischemia. J Neurochem 81, 355-64 (2002)
    • (2002) J Neurochem , vol.81 , pp. 355-364
    • Lu, A.1    Ran, R.2    Parmentier-Batteur, S.3    Nee, A.4    Sharp, F.R.5
  • 106
    • 0034984898 scopus 로고    scopus 로고
    • Nonviral gene delivery to the lateral ventricles in rat brain: Initial evidence for widespread distribution and expression in the central nervous system
    • Hecker, J.G., Hall, L.L. & Irion, V.R.: Nonviral gene delivery to the lateral ventricles in rat brain: initial evidence for widespread distribution and expression in the central nervous system. Mol Ther 3, 375-84 (2001)
    • (2001) Mol Ther , vol.3 , pp. 375-384
    • Hecker, J.G.1    Hall, L.L.2    Irion, V.R.3
  • 107
    • 22244440491 scopus 로고    scopus 로고
    • Selectively increasing inducible heat shock protein 70 via TAT-protein transduction protects neurons from nitrosative stress and excitotoxicity
    • Lai, Y., Du, L., Dunsmore, K.E., Jenkins, L.W., Wong, H.R. & Clark, R.S.: Selectively increasing inducible heat shock protein 70 via TAT-protein transduction protects neurons from nitrosative stress and excitotoxicity. J Neurochem 94, 360-6 (2005)
    • (2005) J Neurochem , vol.94 , pp. 360-366
    • Lai, Y.1    Du, L.2    Dunsmore, K.E.3    Jenkins, L.W.4    Wong, H.R.5    Clark, R.S.6
  • 110
    • 0036829818 scopus 로고    scopus 로고
    • Intravenous TAT-Bcl-Xl is protective after middle cerebral artery occlusion in mice
    • Kilic, E., Dietz, O.P., Hermann, D.M. & Bahr, M.: Intravenous TAT-Bcl-Xl is protective after middle cerebral artery occlusion in mice. Ann Neurol 52, 611-22 (2002)
    • (2002) Ann Neurol , vol.52 , pp. 611-622
    • Kilic, E.1    Dietz, O.P.2    Hermann, D.M.3    Bahr, M.4
  • 111
    • 5444265882 scopus 로고    scopus 로고
    • Gene therapy in Parkinson's disease
    • Eberhardt, O. & Schulz, J.B.: Gene therapy in Parkinson's disease. Cell Tissue Res 318, 243-60 (2004)
    • (2004) Cell Tissue Res , vol.318 , pp. 243-260
    • Eberhardt, O.1    Schulz, J.B.2
  • 112
    • 5444270967 scopus 로고    scopus 로고
    • Neuronal pathology in Parkinson's disease
    • Schulz, J.B. & Falkenburger, B.H.: Neuronal pathology in Parkinson's disease. Cell Tissue Res 318, 135-47 (2004)
    • (2004) Cell Tissue Res , vol.318 , pp. 135-147
    • Schulz, J.B.1    Falkenburger, B.H.2
  • 113
    • 17644383748 scopus 로고    scopus 로고
    • Heat shock protein 70 inhibits alpha-synuclein fibril formation via preferential binding to prefibrillar species
    • Dedmon, M.M., Christodoulou, J., Wilson, M.R. & Dobson, C.M.: Heat shock protein 70 inhibits alpha-synuclein fibril formation via preferential binding to prefibrillar species. J Biol Chem 280, 14733-40 (2005)
    • (2005) J Biol Chem , vol.280 , pp. 14733-14740
    • Dedmon, M.M.1    Christodoulou, J.2    Wilson, M.R.3    Dobson, C.M.4
  • 114
    • 2942620074 scopus 로고    scopus 로고
    • Hsp70 reduces alpha-synuclein aggregation and toxicity
    • Klucken, J., Shin, Y., Masliah, E., Hyman, B.T. & McLean, P.J.: Hsp70 Reduces alpha-Synuclein Aggregation and Toxicity. J Biol Chem 279, 25497-502 (2004)
    • (2004) J Biol Chem , vol.279 , pp. 25497-25502
    • Klucken, J.1    Shin, Y.2    Masliah, E.3    Hyman, B.T.4    McLean, P.J.5
  • 115
    • 7444256611 scopus 로고    scopus 로고
    • A single amino acid substitution differentiates Hsp70-dependent effects on alpha-synuclein degradation and toxicity
    • Klucken, J., Shin, Y., Hyman, B.T. & McLean, P.J.: A single amino acid substitution differentiates Hsp70-dependent effects on alpha-synuclein degradation and toxicity. Biochem Biophys Res Commun 325, 367-73 (2004)
    • (2004) Biochem Biophys Res Commun , vol.325 , pp. 367-373
    • Klucken, J.1    Shin, Y.2    Hyman, B.T.3    McLean, P.J.4
  • 116
    • 10944241135 scopus 로고    scopus 로고
    • Hsp70 gene transfer by adeno-associated virus inhibits MPTP-induced nigrostriatal degeneration in the mouse model of Parkinson disease
    • Dong, Z., Wolfer, D.P., Lipp, H.P. & Bueler, H.: Hsp70 gene transfer by adeno-associated virus inhibits MPTP-induced nigrostriatal degeneration in the mouse model of Parkinson disease. Mol Ther 11, 80-8 (2005)
    • (2005) Mol Ther , vol.11 , pp. 80-88
    • Dong, Z.1    Wolfer, D.P.2    Lipp, H.P.3    Bueler, H.4
  • 117
    • 4344569643 scopus 로고    scopus 로고
    • Geldanamycin induces Hsp70 and prevents alpha-synuclein aggregation and toxicity in vitro
    • McLean, P.J., Klucken, J., Shin, Y. & Hyman, B.T.: Geldanamycin induces Hsp70 and prevents alpha-synuclein aggregation and toxicity in vitro. Biochem Biophys Res Commun 321, 665-9 (2004)
    • (2004) Biochem Biophys Res Commun , vol.321 , pp. 665-669
    • McLean, P.J.1    Klucken, J.2    Shin, Y.3    Hyman, B.T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.