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Volumn 12, Issue 14, 1998, Pages 1571-1579

Cytoprotection and regulation of heat shock proteins induced by heat shock in human breast cancer T47-D cells: Role of [Ca2+](i) and protein kinases

Author keywords

Heat; Protein kinase A; Protein kinase C; Viability

Indexed keywords

HEAT SHOCK PROTEIN; PROTEIN KINASE;

EID: 0031790564     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fasebj.12.14.1571     Document Type: Article
Times cited : (23)

References (44)
  • 1
    • 0031793127 scopus 로고    scopus 로고
    • Heat shock protein 70 kDa: Molecular biology, biochemistry, and physiology
    • In press
    • Klang. J. G., and Tsokos, G. C. (1998) Heat shock protein 70 kDa: molecular biology, biochemistry, and physiology. Pharrnacol, Ther. In press
    • (1998) Pharrnacol. Ther.
    • Klang, J.G.1    Tsokos, G.C.2
  • 2
    • 0030498355 scopus 로고    scopus 로고
    • Cell signaling and heat shock protein expression
    • Kiang, J. G., and Tsokos, G. C. (1996) Cell signaling and heat shock protein expression. J. Biomed. Science 3, 379-388
    • (1996) J. Biomed. Science , vol.3 , pp. 379-388
    • Kiang, J.G.1    Tsokos, G.C.2
  • 3
    • 0028357297 scopus 로고
    • Induction of heat shock response reduces mortality rate and organ damage in a sepsis-induced acute lung injury model
    • Villar, J., Edelson, J. D., Post, M., and Slutsky, A. S. (1994) Induction of 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
    • Villar, J.1    Edelson, J.D.2    Post, M.3    Slutsky, A.S.4
  • 5
    • 0027463072 scopus 로고
    • Heatshock response and limitation of tissue necrosis during occlusion/reperfusion in rabbit hearts
    • Currie, R. W., Tanguay, R. M., and Kingma, J. K. (1993) Heatshock 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.K.3
  • 6
    • 0029101723 scopus 로고
    • Induction of heat shock protein72 protects against ischemia/reperfusion injury in rat small intestine
    • Stojadinovic, A., Kiang, J. G., Smallridge, R. C., Galloway, R.J., and Shea-Donohue, T. (1995) Induction of heat shock protein72 protects against ischemia/reperfusion injury in rat small intestine. Gastroentrology 109, 505-515
    • (1995) Gastroentrology , vol.109 , pp. 505-515
    • Stojadinovic, A.1    Kiang, J.G.2    Smallridge, R.C.3    Galloway, R.J.4    Shea-Donohue, T.5
  • 7
    • 0031029847 scopus 로고    scopus 로고
    • Induction of the heat shock response limits tissue injury during acute inflammation of the rat ileum
    • Stojadinovic, A, Kiang, J. G., Smallridge, R. C., Galloway, R. J., and Shea-Donahue, T. (1996) Induction of the heat shock response limits tissue injury during acute inflammation of the rat ileum. Crit. Care Med. 25, 309-317
    • (1996) Crit. Care Med. , vol.25 , pp. 309-317
    • Stojadinovic, A.1    Kiang, J.G.2    Smallridge, R.C.3    Galloway, R.J.4    Shea-Donahue, T.5
  • 8
    • 0023732689 scopus 로고
    • Hyperthermia protects against light damage in the rat retina
    • Barbe, M. F., Tytell, M., Gower, D. J., and Welch, W. J. (1988) Hyperthermia protects against light damage in the rat retina. Science 241, 1817-1820
    • (1988) Science , vol.241 , pp. 1817-1820
    • Barbe, M.F.1    Tytell, M.2    Gower, D.J.3    Welch, W.J.4
  • 10
    • 0030041936 scopus 로고    scopus 로고
    • Heat shock proteins increase resistance to apoptosis
    • Samali. A., and Cotter, T. G. (1996) Heat shock proteins increase resistance to apoptosis. Exp. Cell Res. 223, 163-170
    • (1996) Exp. Cell Res. , vol.223 , pp. 163-170
    • Samali, A.1    Cotter, T.G.2
  • 11
    • 0025856948 scopus 로고
    • Induction of heat shock proteins and their implication in protection against ethanol-induced damage in cultured guinea pig gastric mucosal cells
    • Nakamura, K., Rokutan, K., Marui, N., Aoike, A., and Kawai, K. (1991) Induction of heat shock proteins and their implication in protection against ethanol-induced damage in cultured guinea pig gastric mucosal cells. Gastroenterology 101, 161-166
    • (1991) Gastroenterology , vol.101 , pp. 161-166
    • Nakamura, K.1    Rokutan, K.2    Marui, N.3    Aoike, A.4    Kawai, K.5
  • 13
    • 0029958183 scopus 로고    scopus 로고
    • Heat shock inhibits the hypoxia-induced effects on iodide uptake, signal transduction, and cell viability in rat thyroid FRTL-5 cells
    • Kiang, J. G., Wang, X. D., Ding, X. Z., Gist, I. D., and Smallridge, R. C. (1996) Heat shock inhibits the hypoxia-induced effects on iodide uptake, signal transduction, and cell viability in rat thyroid FRTL-5 cells. Thyroid 6, 475-483
    • (1996) Thyroid , vol.6 , pp. 475-483
    • Kiang, J.G.1    Wang, X.D.2    Ding, X.Z.3    Gist, I.D.4    Smallridge, R.C.5
  • 14
    • 0031592996 scopus 로고    scopus 로고
    • I7β-estradiolinduced increases in glucose-regulated proteins 78 kD and 94 kD protect human breast cancer T47-D cells from thermal injury
    • Kiang, J. G., Gist, I. D., and Tsokos, G. C. (1997) I7β-estradiolinduced increases in glucose-regulated proteins 78 kD and 94 kD protect human breast cancer T47-D cells from thermal injury. Chin. J. Physiol. 40, 213-219
    • (1997) Chin. J. Physiol. , vol.40 , pp. 213-219
    • Kiang, J.G.1    Gist, I.D.2    Tsokos, G.C.3
  • 15
    • 0030078322 scopus 로고    scopus 로고
    • i and HSP72 synthesis but not heat-induced intracellular acidification in human a-431 cells
    • i and HSP72 synthesis but not heat-induced intracellular acidification in human a-431 cells. J. Invest. Med. 44, 53-63
    • (1996) J. Invest. Med. , vol.44 , pp. 53-63
    • Klang, J.G.1    Ding, X.Z.2    McChiin, D.E.3
  • 16
    • 0022531458 scopus 로고
    • RNA splicing is interrupted by heat shock and is reduced by heat shock protein synthesis
    • Yost, H. J., and Lindquist, S. (1986) RNA splicing is interrupted by heat shock and is reduced by heat shock protein synthesis. Cell 45, 185-193
    • (1986) Cell , vol.45 , pp. 185-193
    • Yost, H.J.1    Lindquist, S.2
  • 18
    • 0013002289 scopus 로고
    • Hyperthermia to enhance drug delivery
    • Chabner, S., ed, Alan R. Liss, New York
    • Hahn, G. M. (1983) Hyperthermia to enhance drug delivery. In Rational Basis for Chemotherapy (Chabner, S., ed) pp. 427-436, Alan R. Liss, New York
    • (1983) Rational Basis for Chemotherapy , pp. 427-436
    • Hahn, G.M.1
  • 19
    • 0023617135 scopus 로고
    • Modulation of adriamycin transport by hyperthermia as measured by fluorescence-activated cell sorting
    • Rice, G. C., and Hahn, G. M. (1987) Modulation of adriamycin transport by hyperthermia as measured by fluorescence-activated cell sorting. Cancer Chemother. Pharmacol. 20, 183-187
    • (1987) Cancer Chemother. Pharmacol. , vol.20 , pp. 183-187
    • Rice, G.C.1    Hahn, G.M.2
  • 20
    • 0003157260 scopus 로고
    • Thermotolerance, thermoresistance, and thermosensitization
    • Morimoto, R. I., and Georgopoulos, C., eds, Cold Spring Harbor Laboratory Press, New York
    • Hahn, G. M., and Li, G. C. (1990) Thermotolerance, thermoresistance, and thermosensitization. In Stress Proteins in Biology and Medicine (Morimoto, R. I., and Georgopoulos, C., eds) pp. 79-100, Cold Spring Harbor Laboratory Press, New York
    • (1990) Stress Proteins in Biology and Medicine , pp. 79-100
    • Hahn, G.M.1    Li, G.C.2
  • 21
    • 0022458173 scopus 로고
    • Adriamycin resistance, heat resistance and radiation response in Chinese hamster fibroblasts
    • Wallner, K., and Li, G. C. (1986) Adriamycin resistance, heat resistance and radiation response in Chinese hamster fibroblasts. Int. J. Radiat. Oncol. Biol. Phys. 12, 829-833
    • (1986) Int. J. Radiat. Oncol. Biol. Phys. , vol.12 , pp. 829-833
    • Wallner, K.1    Li, G.C.2
  • 22
    • 0020393599 scopus 로고
    • Immunohistochemical detection of an estrogen-regulated protein by monoclonal antibodies
    • Ciocca, D. R., Adams, D. J., Bjercke, R. J., Edwards, D. P., and McGuire, W. L. (1982) Immunohistochemical detection of an estrogen-regulated protein by monoclonal antibodies. Cancer Res. 42, 4256-4258
    • (1982) Cancer Res. , vol.42 , pp. 4256-4258
    • Ciocca, D.R.1    Adams, D.J.2    Bjercke, R.J.3    Edwards, D.P.4    McGuire, W.L.5
  • 23
    • 0004913317 scopus 로고
    • Coinduction of glucose-regulated proteins and doxorubicin resistance in Chinese hamster cells
    • Shen, J., Hughes, C., Chao, C., Cai, J., Bartels, C., Gessner, T., and Subject, J. (1987) Coinduction of glucose-regulated proteins and doxorubicin resistance in Chinese hamster cells. Proc. Natl. Acad. Sci. USA 84, 3278-3282
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 3278-3282
    • Shen, J.1    Hughes, C.2    Chao, C.3    Cai, J.4    Bartels, C.5    Gessner, T.6    Subject, J.7
  • 27
    • 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., and Behrman, H. R. (1995) Physiological and pharmacological inhibitors of luteinizing hormone-dependent steroidogenesis induce heat shock protein-70 in rat luteal cells. Endocrinology 136, 1775-1781
    • (1995) Endocrinology , vol.136 , pp. 1775-1781
    • Khanna, A.1    Aten, R.F.2    Behrman, H.R.3
  • 29
    • 0019847456 scopus 로고
    • Whole-cell uptake and nuclear localization of 1,25-dihydroxycholecalciferol by breast cancer cells (T47D) in culture
    • Sher, E., Eisman, J. A., Moseley, J. M., and Martin, T. J. (1981) Whole-cell uptake and nuclear localization of 1,25-dihydroxycholecalciferol by breast cancer cells (T47D) in culture. Biochem. J. 200, 315-320
    • (1981) Biochem. J. , vol.200 , pp. 315-320
    • Sher, E.1    Eisman, J.A.2    Moseley, J.M.3    Martin, T.J.4
  • 31
    • 0025793407 scopus 로고
    • Heat treatment induces an increase in intracellular cyclic AMP content in human epidermoid A-431 cells
    • Kiang, J. G., Wu, Y, Y., and Lin, M. C. (1991) Heat treatment induces an increase in intracellular cyclic AMP content in human epidermoid A-431 cells. Biochem. J. 276, 683-689
    • (1991) Biochem. J. , vol.276 , pp. 683-689
    • Kiang, J.G.1    Wu, Y.Y.2    Lin, M.C.3
  • 32
    • 0017250284 scopus 로고
    • Stimulatory effect of 3′,5′-adenosine monophosphate on protein synthesis in heatshocked murine leukemia lymphoblasts
    • Fuhr, J. E., Overton, M., andYang, T. J. (1976) Stimulatory effect of 3′,5′-adenosine monophosphate on protein synthesis in heatshocked murine leukemia lymphoblasts. J. Natl. Cancer Inst. 56, 89-191
    • (1976) J. Natl. Cancer Inst. , vol.56 , pp. 89-191
    • Fuhr, J.E.1    Overton, M.2    Yang, T.J.3
  • 34
    • 0019852661 scopus 로고
    • Estradiol stimulates synthesis of a major intracellular protein in a human breast cancer cell line (MCF-7)
    • Edwards D. P., Adams, D. J., and McGuire, W. L. (1981) Estradiol stimulates synthesis of a major intracellular protein in a human breast cancer cell line (MCF-7). Breast Cancer Res. Treat. 1, 209-223
    • (1981) Breast Cancer Res. Treat. , vol.1 , pp. 209-223
    • Edwards, D.P.1    Adams, D.J.2    McGuire, W.L.3
  • 35
    • 0020503779 scopus 로고
    • Purification of an estrogen-regulated breast cancer protein by monoclonal antibody affinity chromatography
    • Adams, D. F., Hajj, H., Bitar, K. G., Edwards, D. P., and McGuire, W. L. (1983) Purification of an estrogen-regulated breast cancer protein by monoclonal antibody affinity chromatography. Endocrinology 113, 415-417
    • (1983) Endocrinology , vol.113 , pp. 415-417
    • Adams, D.F.1    Hajj, H.2    Bitar, K.G.3    Edwards, D.P.4    McGuire, W.L.5
  • 36
    • 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, D. R., and Luque, E. H. (1991) 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. 20, 33-42
    • (1991) Breast Cancer Res. Treat. , vol.20 , pp. 33-42
    • Ciocca, D.R.1    Luque, E.H.2
  • 37
    • 0027292089 scopus 로고
    • The 28-kDa protein whose phosphorylation is induced by protein kinase C activators in MCF-7 cells belongs to the family of low molecular mass heat shock proteins and is the estrogcn-regulatcd 24-kDa protein
    • Fucher, C., Capdevielle, J., Canal, I., Ferrara, P., Mazarguil. H., McGuire, W. L. and Darbon, J. M. (1993) The 28-kDa protein whose phosphorylation is induced by protein kinase C activators in MCF-7 cells belongs to the family of low molecular mass heat shock proteins and is the estrogcn-regulatcd 24-kDa protein. J. Biol. Chem. 268, 15168-15173
    • (1993) J. Biol. Chem. , vol.268 , pp. 15168-15173
    • Fucher, C.1    Capdevielle, J.2    Canal, I.3    Ferrara, P.4    Mazarguil, H.5    McGuire, W.L.6    Darbon, J.M.7
  • 38
    • 0031034622 scopus 로고    scopus 로고
    • Heat shock factor-1 protein in heat shock factor-1 gene-transfected human epidermoid A431 cells requires phosphorylation before inducing heat shock protein-70 production
    • Ding, X. Z., Tsokos, G. C., and Kiang, J. G. (1997) Heat shock factor-1 protein in heat shock factor-1 gene-transfected human epidermoid A431 cells requires phosphorylation before inducing heat shock protein-70 production. J. Clin. Invest. 99, 136-143
    • (1997) J. Clin. Invest. , vol.99 , pp. 136-143
    • Ding, X.Z.1    Tsokos, G.C.2    Kiang, J.G.3
  • 39
    • 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., and Morimoto, R. I. (1990) In vitro activation of heat shock transcription factor DNA-binding by calcium and biochemical conditions that affect, protein conformation. Proc. Natl. Acad. Sci. USA 87, 3748-3752
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 3748-3752
    • Mosser, D.D.1    Kotzbauer, P.T.2    Sarge, K.D.3    Morimoto, R.I.4
  • 40
    • 0025922155 scopus 로고
    • 2+ is essential for multistep activation of the heat shock factor in permeabilized cells
    • 2+ is essential for multistep activation of the heat shock factor in permeabilized cells. Mol. Cell. Biol. 11, 3365-3368
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 3365-3368
    • Price, B.D.1    Calderwood, S.K.2
  • 41
    • 0025755922 scopus 로고
    • Heat shock factor and the heat shock response
    • Sorger, P. K. (1991) Heat shock factor and the heat shock response. Cell 65, 363-366
    • (1991) Cell , vol.65 , pp. 363-366
    • Sorger, P.K.1
  • 42
    • 0025014982 scopus 로고
    • Complex modes of heat shock factor activation
    • Zimarino, V., Tsai, C., Wu, C. (1990) Complex modes of heat shock factor activation. Mol. Cell. Biol. 10, 752-759
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 752-759
    • Zimarino, V.1    Tsai, C.2    Wu, C.3
  • 43
    • 0023515282 scopus 로고
    • Mechanisms of heatshock gent activation in higher eukaryotes
    • Bienz, M., and Pelham, H. R. B. (1987) Mechanisms of heatshock gent activation in higher eukaryotes. Adv. Genet. 24, 31-72
    • (1987) Adv. Genet. , vol.24 , pp. 31-72
    • Bienz, M.1    Pelham, H.R.B.2
  • 44
    • 0031570448 scopus 로고    scopus 로고
    • Overexpression of the heat shock protein 70 enhances the TCR/CD3- And Fas/Apo-l/CD95-mediated apoptotic cell death in Jurkat cells
    • Liossis, S.-N. C., Ding, X. Z., Kiang, J. G., and Tsokos, G. C. (1997) Overexpression of the heat shock protein 70 enhances the TCR/CD3- and Fas/Apo-l/CD95-mediated apoptotic cell death in Jurkat cells. J. Immunol. 158, 5668-5675
    • (1997) J. Immunol. , vol.158 , pp. 5668-5675
    • Liossis, S.-N.C.1    Ding, X.Z.2    Kiang, J.G.3    Tsokos, G.C.4


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