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Volumn 141, Issue 1, 1996, Pages 330-339

Expression of the 25-kDa heat-shock protein (HSP27) correlates with resistance to the toxicity of cadmium chloride, mercuric chloride, cis-platinum(II)-diammine dichloride, or sodium arsenite in mouse embryonic stem cells transfected with sense or antisense HSP27 cDNA

Author keywords

[No Author keywords available]

Indexed keywords

ARSENITE SODIUM; CADMIUM CHLORIDE; CISPLATIN; COMPLEMENTARY DNA; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 27; MERCURIC CHLORIDE; VIRUS VECTOR;

EID: 0030297011     PISSN: 0041008X     EISSN: None     Source Type: Journal    
DOI: 10.1006/taap.1996.0290     Document Type: Article
Times cited : (58)

References (35)
  • 1
    • 0002241311 scopus 로고
    • Expression and function of the low-molecular weight heat shock proteins
    • R. I. Morimoto, A. Tissieres, and C. Georgopoulos, Eds. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Arrigo, A. P., and Landry, J. (1994). Expression and function of the low-molecular weight heat shock proteins. In Biology of Heat Shock Proteins and Molecular Chaperones (R. I. Morimoto, A. Tissieres, and C. Georgopoulos, Eds.), pp. 335-373. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1994) Biology of Heat Shock Proteins and Molecular Chaperones , pp. 335-373
    • Arrigo, A.P.1    Landry, J.2
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0023201025 scopus 로고
    • Heat shock proteins in thermotolerance and other cellular processes
    • Carper, S. W., Duffy, J. J., and Cerner, E. W. (1987). Heat shock proteins in thermotolerance and other cellular processes. Cancer Res. 47, 5249-5255.
    • (1987) Cancer Res. , vol.47 , pp. 5249-5255
    • Carper, S.W.1    Duffy, J.J.2    Cerner, E.W.3
  • 7
    • 85030283888 scopus 로고
    • GenBank, Accession No. M86389
    • Gilmont, R. R., and Welsh, M. J. (1992). GenBank, Accession No. M86389.
    • (1992)
    • Gilmont, R.R.1    Welsh, M.J.2
  • 9
    • 0030069517 scopus 로고    scopus 로고
    • Hsp27 phosphorylation-mediated resistance against actin fragmentation and cell death induced by oxidative stress
    • Huot, J., Houle, F., Spitz, D. R., and Landry, J. (1996). Hsp27 phosphorylation-mediated resistance against actin fragmentation and cell death induced by oxidative stress. Cancer Res. 56, 273-279.
    • (1996) Cancer Res. , vol.56 , pp. 273-279
    • Huot, J.1    Houle, F.2    Spitz, D.R.3    Landry, J.4
  • 10
    • 0021802765 scopus 로고
    • Review of the health effects of methylmercury
    • Inskip, M. J., and Piotrowski, J. K. (1985). Review of the health effects of methylmercury. J. Appl. Toxicol. 5, 113-133.
    • (1985) J. Appl. Toxicol. , vol.5 , pp. 113-133
    • Inskip, M.J.1    Piotrowski, J.K.2
  • 11
    • 0027391629 scopus 로고
    • Small heat shock proteins are molecular chaperones
    • Jakob, U., Gaestel, M., Engel, K., and Buchner, J. (1993). Small heat shock proteins are molecular chaperones. J. Biol. Chem. 268, 1517-1520.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1517-1520
    • Jakob, U.1    Gaestel, M.2    Engel, K.3    Buchner, J.4
  • 12
    • 0023605264 scopus 로고
    • Heat-induced nuclear protein binding and its relation to thermal cytotoxicity
    • Kampinga, H. H., Luppes, J. G., and Konings, A. W. (1987). Heat-induced nuclear protein binding and its relation to thermal cytotoxicity. Int. J. Hyperthermia 3, 459-465.
    • (1987) Int. J. Hyperthermia , vol.3 , pp. 459-465
    • Kampinga, H.H.1    Luppes, J.G.2    Konings, A.W.3
  • 13
    • 0024345716 scopus 로고
    • Heat shock resistance conferred by expression of the human HSP27 gene in rodent cells
    • Landry, J., Chretien, P., Lambert, J., Hickey, E., and Weber, L. A. (1989). Heat shock resistance conferred by expression of the human HSP27 gene in rodent cells. J. Cell Biol. 109, 7-15.
    • (1989) J. Cell Biol. , vol.109 , pp. 7-15
    • Landry, J.1    Chretien, P.2    Lambert, J.3    Hickey, E.4    Weber, L.A.5
  • 14
    • 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, J. N., Gingras-Breton, G., Tanguay, M., and Landry, J. (1993a). 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-Breton, G.2    Tanguay, M.3    Landry, J.4
  • 15
    • 0027482463 scopus 로고
    • Modulation of actin microfilament dynamics and fluid phase pinocytosis by phosphorylation of heat shock protein 27
    • Lavoie, J. N., Hickey, E., Weber, L. A., and Landry, J. (1993b). Modulation of actin microfilament dynamics and fluid phase pinocytosis by phosphorylation of heat shock protein 27. J. Biol. Chem. 268, 24210-24214.
    • (1993) J. Biol. Chem. , vol.268 , pp. 24210-24214
    • Lavoie, J.N.1    Hickey, E.2    Weber, L.A.3    Landry, J.4
  • 16
    • 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, J. N., Lambert, H., Hickey, E., Weber, L. A., and Landry, J. (1995). Modulation of cellular thermoresistance and actin filament stability accompanies phosphorylation-induced changes in the oligomeric structure of heat shock protein 27. Mol. Cell. Biol. 15, 505-516.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 505-516
    • Lavoie, J.N.1    Lambert, H.2    Hickey, E.3    Weber, L.A.4    Landry, J.5
  • 17
    • 0020130877 scopus 로고
    • Correlation between synthesis of heat shock proteins and development of thermotolerance in Chinese hamster fibroblasts
    • Li, G. C., and Werb, Z. (1982). Correlation between synthesis of heat shock proteins and development of thermotolerance in Chinese hamster fibroblasts. Proc. Natl. Acad. Sci. USA 79, 3218-3222.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 3218-3222
    • Li, G.C.1    Werb, Z.2
  • 18
    • 0022555843 scopus 로고
    • The heat-shock response
    • Lindquist, S. (1986). The heat-shock response. Annu. Rev. Biochem. 55, 1151-1191.
    • (1986) Annu. Rev. Biochem. , vol.55 , pp. 1151-1191
    • Lindquist, S.1
  • 19
    • 0027991697 scopus 로고
    • The application of TXFR in instrumental multielement analysis of plants, demonstrated with species of moss
    • Markert, B., Reus, U., and Herpin, U. (1994). The application of TXFR in instrumental multielement analysis of plants, demonstrated with species of moss. Sci. Total Environ. 152, 213-220.
    • (1994) Sci. Total Environ. , vol.152 , pp. 213-220
    • Markert, B.1    Reus, U.2    Herpin, U.3
  • 20
    • 0028817419 scopus 로고
    • Constitutive expression of human hsp27, Drosophila hsp27, or human aB-crystallin confers resistance to TNF-and oxidative stress-induced cytotoxicity in stably transfected murine L929 fibroblasts
    • Mehlen, P., Preville, X., Chareyron, P., Briolay, J., Klemenz, R., and Arrigo, A.-P. (1995). Constitutive expression of human hsp27, Drosophila hsp27, or human aB-crystallin confers resistance to TNF-and oxidative stress-induced cytotoxicity in stably transfected murine L929 fibroblasts. J. Immunol. 154, 363-374.
    • (1995) J. Immunol. , vol.154 , pp. 363-374
    • Mehlen, P.1    Preville, X.2    Chareyron, P.3    Briolay, J.4    Klemenz, R.5    Arrigo, A.-P.6
  • 21
    • 0029933741 scopus 로고    scopus 로고
    • Human hsp27, Drosophila hsp27 and human αB-crystallin expression-mediated increase in glutathione is essential for the protective activity of these proteins against TNFα-induced cell death
    • Mehlen, P., Kretz-Remy, C., Preville, X., and Arrigo, A.-P. (1996). Human hsp27, Drosophila hsp27 and human αB-crystallin expression-mediated increase in glutathione is essential for the protective activity of these proteins against TNFα-induced cell death. EMBO J. 15, 2695-2706.
    • (1996) EMBO J. , vol.15 , pp. 2695-2706
    • Mehlen, P.1    Kretz-Remy, C.2    Preville, X.3    Arrigo, A.-P.4
  • 22
    • 0025813543 scopus 로고
    • A 25-kD inhibitor of actin polymerization is a low molecular mass heat shock protein
    • Miron, T., Vancompernolle, K., Vandekerckhove, J., Wilchek, M., and Geiger, B. (1991). A 25-kD inhibitor of actin polymerization is a low molecular mass heat shock protein. J. Cell Biol. 114, 255-261.
    • (1991) J. Cell Biol. , vol.114 , pp. 255-261
    • Miron, T.1    Vancompernolle, K.2    Vandekerckhove, J.3    Wilchek, M.4    Geiger, B.5
  • 23
    • 0001824746 scopus 로고
    • Progress and perspectives on the biology of heat shock proteins and molecular chaperones
    • R. I. Morimoto, A. Tissieres, and C. Georgopoulos, Eds. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Morimoto, R. I., Tissieres, A., and Georgopoulos, C. (1994). Progress and perspectives on the biology of heat shock proteins and molecular chaperones. In Biology of Heat Shock Proteins and Molecular Chaperones (R. I. Morimoto, A. Tissieres, and C. Georgopoulos, Eds.), pp. 335-373. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1994) Biology of Heat Shock Proteins and Molecular Chaperones , pp. 335-373
    • Morimoto, R.I.1    Tissieres, A.2    Georgopoulos, C.3
  • 24
    • 84988130977 scopus 로고
    • Experimental studies upon lymphocytes
    • Pappenheimer, A. M. (1917). Experimental studies upon lymphocytes. J. Exp. Med. 25, 633-650.
    • (1917) J. Exp. Med. , vol.25 , pp. 633-650
    • Pappenheimer, A.M.1
  • 25
    • 0000675009 scopus 로고
    • Heat-shock protein and stress tolerance
    • R. I. Morimoto, A. Tissieres, and C. Georgopoulos, Eds. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Parsell, D. A., and Lindquist, S. (1994). Heat-shock protein and stress tolerance. In The Biology of Heat Shock Proteins and Molecular Chaperones (R. I. Morimoto, A. Tissieres, and C. Georgopoulos, Eds.), pp. 457-494. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1994) The Biology of Heat Shock Proteins and Molecular Chaperones , pp. 457-494
    • Parsell, D.A.1    Lindquist, S.2
  • 27
    • 0027407468 scopus 로고
    • Heat shock and recovery protects renal allografts from warm ischemic injury and enhances hsp72 production
    • Perdrizet, G. A., Kaneko, H., Buckley, T. M., Fishman, M. S., Pleau, M., Bow, L., and Schweizer, R. T. (1993). Heat shock and recovery protects renal allografts from warm ischemic injury and enhances hsp72 production. Transplant. Proc. 25, 1670-1673.
    • (1993) Transplant. Proc. , vol.25 , pp. 1670-1673
    • Perdrizet, G.A.1    Kaneko, H.2    Buckley, T.M.3    Fishman, M.S.4    Pleau, M.5    Bow, L.6    Schweizer, R.T.7
  • 28
    • 0003048995 scopus 로고
    • An analyst's approach to total reflection XFR: Features and applications
    • Reus, U., and Prange, A. (1993). An analyst's approach to total reflection XFR: Features and applications. Spectroscopy Eur. 5, 26-33.
    • (1993) Spectroscopy Eur. , vol.5 , pp. 26-33
    • Reus, U.1    Prange, A.2
  • 29
    • 0026691949 scopus 로고
    • Expression of Drosophila's 27kDa heat shock protein into rodent cells confers thermal resistance
    • Rollet, E., Lavoie, J. N., Landry, J., and Tanguay, R. M. (1992). Expression of Drosophila's 27kDa heat shock protein into rodent cells confers thermal resistance. Biochem. Biophys. Res. Commun. 185, 116-120.
    • (1992) Biochem. Biophys. Res. Commun. , vol.185 , pp. 116-120
    • Rollet, E.1    Lavoie, J.N.2    Landry, J.3    Tanguay, R.M.4
  • 30
    • 0025186226 scopus 로고
    • Antisense inhibition of glial S100β production results in alterations in cell morphology, cytoskeletal organization, and cell proliferation
    • Selinfreund, R. H., Barger, S. W., Welsh, M. J., and Van Eldik, L. J. (1990). Antisense inhibition of glial S100β production results in alterations in cell morphology, cytoskeletal organization, and cell proliferation. J. Cell Biol. 111, 2021-2028.
    • (1990) J. Cell Biol. , vol.111 , pp. 2021-2028
    • Selinfreund, R.H.1    Barger, S.W.2    Welsh, M.J.3    Van Eldik, L.J.4
  • 31
    • 0029788715 scopus 로고    scopus 로고
    • Variation in expression of HSP27 messenger RNA during the cycle of the seminiferous epithelium and co-localization of HSP27 and microfilaments in Sertoli cells of the rat
    • Welsh, M. J., Wu, W., Parvinen, M., and Gilmont, R. R. (1996). Variation in expression of HSP27 messenger RNA during the cycle of the seminiferous epithelium and co-localization of HSP27 and microfilaments in Sertoli cells of the rat. Biol. Reprod. 55, 141-151.
    • (1996) Biol. Reprod. , vol.55 , pp. 141-151
    • Welsh, M.J.1    Wu, W.2    Parvinen, M.3    Gilmont, R.R.4
  • 32
    • 0029047573 scopus 로고
    • A method for purification of DNA species by high speed centrifugation of agarose gel slices
    • Wu, W., and Welsh, M. J. (1995). A method for purification of DNA species by high speed centrifugation of agarose gel slices. Anal. Biochem. 229, 350-352.
    • (1995) Anal. Biochem. , vol.229 , pp. 350-352
    • Wu, W.1    Welsh, M.J.2
  • 33
    • 0011832641 scopus 로고
    • Inhibition of gene expression by antisense DNA and RNA
    • P. B. Kaufman, W. Wu, D. Kim, and L. J. Cseke, Eds. CRC Press, Inc., Boca Raton, FL
    • Wu, W. (1995a). Inhibition of gene expression by antisense DNA and RNA. In Handbook of Molecular and Cellular Methods in Biology and Medicine (P. B. Kaufman, W. Wu, D. Kim, and L. J. Cseke, Eds.), pp. 289-304. CRC Press, Inc., Boca Raton, FL.
    • (1995) Handbook of Molecular and Cellular Methods in Biology and Medicine , pp. 289-304
    • Wu, W.1
  • 34
    • 0011912985 scopus 로고
    • Electrophoresis, blotting and hybridization
    • P. B. Kaufman, W. Wu, D. Kim, and L. J. Cseke, Eds. CRC Press, Inc., Boca Raton, FL
    • Wu, W. (1995b). Electrophoresis, blotting and hybridization. In Handbook of Molecular and Cellular Methods in Biology and Medicine (P. B. Kaufman, W. Wu, D. Kim, and L. J. Cseke, Eds.), pp. 87-122. CRC Press, Inc., Boca Raton, FL.
    • (1995) Handbook of Molecular and Cellular Methods in Biology and Medicine , pp. 87-122
    • Wu, W.1
  • 35
    • 0011910353 scopus 로고
    • Isolation and purification of RNA
    • P. B. Kaufman, W. Wu, D. Kim, and L. J. Cseke, Eds. CRC Press, Inc., Boca Raton, FL
    • Wu, W. (1995c). Isolation and purification of RNA. In Handbook of Molecular and Cellular Methods in Biology and Medicine (P. B. Kaufman, W. Wu, D. Kim, and L. J. Cseke, Eds.), pp. 27-40. CRC Press, Inc., Boca Raton, FL.
    • (1995) Handbook of Molecular and Cellular Methods in Biology and Medicine , pp. 27-40
    • Wu, W.1


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