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Volumn 228, Issue 5, 2003, Pages 491-498

Adaptive responses to the stress induced by hyperthermia or hydrogen peroxide in human fibroblasts

Author keywords

HSP70 antisense; iNOS antisense; Oxidative DNA damage; Oxidative stress; Stress proteins cross talk

Indexed keywords

ANTISENSE OLIGONUCLEOTIDE; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 32; HEAT SHOCK PROTEIN 70; HYDROGEN PEROXIDE; LACTATE DEHYDROGENASE; NITRIC OXIDE SYNTHASE; REACTIVE OXYGEN METABOLITE; UNCLASSIFIED DRUG; GLUTATHIONE; HEME OXYGENASE 1; INDUCIBLE NITRIC OXIDE SYNTHASE; ANTIOXIDANT; HEME OXYGENASE; HMOX1 PROTEIN, HUMAN; MEMBRANE PROTEIN; NOS2A PROTEIN, HUMAN; OXIDIZING AGENT;

EID: 0141569311     PISSN: 15353702     EISSN: None     Source Type: Journal    
DOI: 10.1177/15353702-0322805-12     Document Type: Conference Paper
Times cited : (47)

References (44)
  • 2
    • 0034533082 scopus 로고    scopus 로고
    • Reactive oxygen species in cell signalling
    • Thannickal J, Fanburg BL. Reactive oxygen species in cell signalling. Am J Physiol 279:L1005-L1028, 2000.
    • (2000) Am J Physiol , vol.279
    • Thannickal, J.1    Fanburg, B.L.2
  • 3
    • 0032874845 scopus 로고    scopus 로고
    • Glutathione and glutathione-dependent enzymes represent a co-ordinately regulated defence against oxidative stress
    • Hayes JD, McLellan LI. Glutathione and glutathione-dependent enzymes represent a co-ordinately regulated defence against oxidative stress. Free Rad Res 31:273-300, 1999.
    • (1999) Free Rad Res , vol.31 , pp. 273-300
    • Hayes, J.D.1    McLellan, L.I.2
  • 4
    • 0037099046 scopus 로고    scopus 로고
    • Chaperoning signalling pathways: Molecular chaperones as stress-sensing "heat shock" proteins
    • Nollen EA, Morimoto RI. Chaperoning signalling pathways: Molecular chaperones as stress-sensing "heat shock" proteins. J Cell Sci 115:2809-2816, 2002.
    • (2002) J Cell Sci , vol.115 , pp. 2809-2816
    • Nollen, E.A.1    Morimoto, R.I.2
  • 5
    • 0034693134 scopus 로고    scopus 로고
    • Nitric oxide-inducible expression of heme oxygenase-1 in human cells. Translation-independent stabilization of the mRNA and evidence for direct action of nitric oxide
    • Bouton C, Demple B. Nitric oxide-inducible expression of heme oxygenase-1 in human cells. Translation-independent stabilization of the mRNA and evidence for direct action of nitric oxide. J Biol Chem 275:32688-32693, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 32688-32693
    • Bouton, C.1    Demple, B.2
  • 6
    • 0034607632 scopus 로고    scopus 로고
    • Endothelial heme oxygenase-1 induction by hypoxia. Modulation by inducible nitric-oxide synthase and S-nitrosothiols
    • Motterlini R, Foresti R, Bassi R, Calabrese V, Clark JE, Green CJ. Endothelial heme oxygenase-1 induction by hypoxia. Modulation by inducible nitric-oxide synthase and S-nitrosothiols. J Biol Chem 275:13613-13620, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 13613-13620
    • Motterlini, R.1    Foresti, R.2    Bassi, R.3    Calabrese, V.4    Clark, J.E.5    Green, C.J.6
  • 7
    • 0032535245 scopus 로고    scopus 로고
    • Regulation of heat shock transcriptional response: Cross talk between a family of heat shock factors, molecular chaperones and negative regulators
    • Morimoto RI. Regulation of heat shock transcriptional response: Cross talk between a family of heat shock factors, molecular chaperones and negative regulators. Genes Dev 12:3788-3796, 1998.
    • (1998) Genes Dev , vol.12 , pp. 3788-3796
    • Morimoto, R.I.1
  • 8
    • 0030923630 scopus 로고    scopus 로고
    • The heme oxygenase system: A regulator of second messenger gases
    • Maines MD. The heme oxygenase system: A regulator of second messenger gases. Annu Rev Pharmacol Toxicol 37:517-554, 1997.
    • (1997) Annu Rev Pharmacol Toxicol , vol.37 , pp. 517-554
    • Maines, M.D.1
  • 10
    • 0032571341 scopus 로고    scopus 로고
    • Induction of inducile nitric oxide synthase and heme oxygenase-1 in rat glial cells
    • Kitamura Y, Matsuoka Y, Nomura Y, Taniguchi T. Induction of inducile nitric oxide synthase and heme oxygenase-1 in rat glial cells. Life Sci 62:1717-1721, 1998.
    • (1998) Life Sci , vol.62 , pp. 1717-1721
    • Kitamura, Y.1    Matsuoka, Y.2    Nomura, Y.3    Taniguchi, T.4
  • 11
    • 0029868298 scopus 로고    scopus 로고
    • Heme-oxygenase-1 induction in glia throughout rat brain following experimental subarachnoid hemorrhage
    • Matz P, Turner C, Weinstein PR, Massa SM, Panter SS, Sharp FR. Heme-oxygenase-1 induction in glia throughout rat brain following experimental subarachnoid hemorrhage. Brain Res 713:211-222, 1996.
    • (1996) Brain Res , vol.713 , pp. 211-222
    • Matz, P.1    Turner, C.2    Weinstein, P.R.3    Massa, S.M.4    Panter, S.S.5    Sharp, F.R.6
  • 12
    • 0023731036 scopus 로고
    • Heme oxygenase: Function, multiplicity, regulatory mechanism and clinical applications
    • Maines MD. Heme oxygenase: Function, multiplicity, regulatory mechanism and clinical applications. FASEB J 2:2557-2568, 1988.
    • (1988) FASEB J , vol.2 , pp. 2557-2568
    • Maines, M.D.1
  • 13
    • 0026629902 scopus 로고
    • Nitric oxide as a secretory product of mammalian cells
    • Nathan C. Nitric oxide as a secretory product of mammalian cells. FASEB J 6:3051-3064, 1992.
    • (1992) FASEB J , vol.6 , pp. 3051-3064
    • Nathan, C.1
  • 15
    • 0026033907 scopus 로고
    • Induction of heme oxygenase: A general response to oxidant stress in cultured mammalian cells
    • Applegate L, Luscher P, Tyrrell R. Induction of heme oxygenase: A general response to oxidant stress in cultured mammalian cells. Cancer Res 51:974-978, 1991.
    • (1991) Cancer Res , vol.51 , pp. 974-978
    • Applegate, L.1    Luscher, P.2    Tyrrell, R.3
  • 16
    • 0024497521 scopus 로고
    • Heme oxygenase is the major 32-kDa stress protein induced in human skin fibroblasts by UVA radiation, hydrogen peroxide, and sodium arsenite
    • Keyse S, Tyrrell R. Heme oxygenase is the major 32-kDa stress protein induced in human skin fibroblasts by UVA radiation, hydrogen peroxide, and sodium arsenite. Proc Natl Acad Sci USA 86:99-103, 1989.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 99-103
    • Keyse, S.1    Tyrrell, R.2
  • 18
    • 0009760791 scopus 로고    scopus 로고
    • Heat shock protein hsp70 over expression confers resistance against nitric oxide
    • Bellmann K, Jaattela D, Wissing D, Burkat V, Bruckhoff J, Kolb H. Heat shock protein hsp70 over expression confers resistance against nitric oxide. FEBS Lett 391:185-188, 1996.
    • (1996) FEBS Lett , vol.391 , pp. 185-188
    • Bellmann, K.1    Jaattela, D.2    Wissing, D.3    Burkat, V.4    Bruckhoff, J.5    Kolb, H.6
  • 21
    • 0035949667 scopus 로고    scopus 로고
    • Neural roles for heme oxygenase: Contrasts to nitric oxide synthase
    • Baranano DE, Snyder SH. Neural roles for heme oxygenase: Contrasts to nitric oxide synthase. Proc Natl Acad Sci USA 98:10996-11002, 2001.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 10996-11002
    • Baranano, D.E.1    Snyder, S.H.2
  • 22
    • 0036183785 scopus 로고    scopus 로고
    • Interactions between inducile nitric oxide synthase and heme oxygenase-1 in glomerulonephritis
    • Datta PK, Gross EJ, Lianos EA. Interactions between inducile nitric oxide synthase and heme oxygenase-1 in glomerulonephritis. Kidney Int 61:847-850, 2002.
    • (2002) Kidney Int , vol.61 , pp. 847-850
    • Datta, P.K.1    Gross, E.J.2    Lianos, E.A.3
  • 23
    • 0037090046 scopus 로고    scopus 로고
    • Heat shock inactivates cellular antioxidant defenses against hydrogen peroxide: Protection by glucose
    • Lord-Fontaine S, Averill-Bates DA. Heat shock inactivates cellular antioxidant defenses against hydrogen peroxide: Protection by glucose. Free Rad Biol Med 32:752-762, 2002.
    • (2002) Free Rad Biol Med , vol.32 , pp. 752-762
    • Lord-Fontaine, S.1    Averill-Bates, D.A.2
  • 24
    • 0028939289 scopus 로고
    • Possible correlation between DNA damage induced by hydrogen peroxide and translocation of heat shock 70 protein into the nucleus
    • Abe T, Konishi T, Hirano T, Kasai H, Shimuzu K, Kashimura M, Hisashi K. Possible correlation between DNA damage induced by hydrogen peroxide and translocation of heat shock 70 protein into the nucleus. Biochem Biophys Res Commun 206:548-555, 1995.
    • (1995) Biochem Biophys Res Commun , vol.206 , pp. 548-555
    • Abe, T.1    Konishi, T.2    Hirano, T.3    Kasai, H.4    Shimuzu, K.5    Kashimura, M.6    Hisashi, K.7
  • 25
    • 85158936396 scopus 로고
    • The effects of hyperthermia on cellular macromolecules
    • Urano M, Douple E, Eds. Utrecht, Netherlands. VSP
    • Roti JI, Laszlo A. The effects of hyperthermia on cellular macromolecules. In: Urano M, Douple E, Eds Hyperthermia and oncology. Utrecht, Netherlands. VSP, Vol 1:pp13-56, 1988.
    • (1988) Hyperthermia and Oncology , vol.1 , pp. 13-56
    • Roti, J.I.1    Laszlo, A.2
  • 26
    • 0033558786 scopus 로고    scopus 로고
    • Enhancement of cytotoxicity of hydrogen peroxide by hyperthermia in Chinese harmesr ovary cells: Role of antioxidant defenses
    • Lord-Fontaine S, Averill D. Enhancement of cytotoxicity of hydrogen peroxide by hyperthermia in Chinese harmesr ovary cells: Role of antioxidant defenses. Arch Biochem Biophys 363:283-295, 1999.
    • (1999) Arch Biochem Biophys , vol.363 , pp. 283-295
    • Lord-Fontaine, S.1    Averill, D.2
  • 27
    • 0141765696 scopus 로고    scopus 로고
    • Hyperthermia enhances the cytotoxic effects of reactive oxygen species to Chinese hamster cells and bovine endothelial cells in vitro
    • Lin P, Quamo S, Ho K, Gladding J. Hyperthermia enhances the cytotoxic effects of reactive oxygen species to Chinese hamster cells and bovine endothelial cells in vitro. Cancer Res 57:1991-1998, 1997.
    • (1997) Cancer Res , vol.57 , pp. 1991-1998
    • Lin, P.1    Quamo, S.2    Ho, K.3    Gladding, J.4
  • 28
    • 0020593607 scopus 로고
    • Thiols, thiol depletion, and thermosensitivity
    • Mitchell JB, Russo A. Thiols, thiol depletion, and thermosensitivity. Radiat Res 95:471-485, 1983.
    • (1983) Radiat Res , vol.95 , pp. 471-485
    • Mitchell, J.B.1    Russo, A.2
  • 29
    • 0029974373 scopus 로고    scopus 로고
    • Regulation of the mouse inducible-type nitric oxide synthase gene promoter by interferon-g, bacterial lipopolysaccharide and N-monomethyl-L-arginine
    • Weisz A, Cicatiello L, Esumi H. Regulation of the mouse inducible-type nitric oxide synthase gene promoter by interferon-g, bacterial lipopolysaccharide and N-monomethyl-L-arginine. Biochem J 316:209-215, 1996.
    • (1996) Biochem J , vol.316 , pp. 209-215
    • Weisz, A.1    Cicatiello, L.2    Esumi, H.3
  • 30
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxicity assays
    • Mosmann T. Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. J Immunol Methods 65:55-63, 1983.
    • (1983) J Immunol Methods , vol.65 , pp. 55-63
    • Mosmann, T.1
  • 31
    • 0025243999 scopus 로고
    • Glutamate toxicity in immature cortical neuron precedes development of glutamate receptor currents
    • Murphy TH, Baraban JM. Glutamate toxicity in immature cortical neuron precedes development of glutamate receptor currents. Dev Brain Res 57:146-150, 1990.
    • (1990) Dev Brain Res , vol.57 , pp. 146-150
    • Murphy, T.H.1    Baraban, J.M.2
  • 32
    • 0026554428 scopus 로고
    • Evaluation of the probe 2′,7′-Dichlorofluorescin as an indicator of Reactive Oxygen Species formation and oxidative stress
    • Lebei CP, Isehiropoulos H, Bondy SC. Evaluation of the probe 2′,7′-Dichlorofluorescin as an indicator of Reactive Oxygen Species formation and oxidative stress. Chem Res Toxicol 5:227-231, 1992.
    • (1992) Chem Res Toxicol , vol.5 , pp. 227-231
    • Lebei, C.P.1    Isehiropoulos, H.2    Bondy, S.C.3
  • 33
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. 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.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 34
    • 0028283301 scopus 로고
    • Measurement of protein thiol groups and glutathione in plasma
    • Packer L, Ed. San Diego: Academic Press
    • Miao Lin H. Measurement of protein thiol groups and glutathione in plasma. In: Packer L, Ed. Methods in Enzymology. San Diego: Academic Press, Vol Part C 233:pp380-385, 1994.
    • (1994) Methods in Enzymology , Issue.PART C 233 , pp. 380-385
    • Miao Lin, H.1
  • 36
    • 0034626735 scopus 로고    scopus 로고
    • Oxidants, oxidative stress and the biology of ageing
    • Finkel T, Holbrook NJ. Oxidants, oxidative stress and the biology of ageing. Nature 408:239-247, 2000.
    • (2000) Nature , vol.408 , pp. 239-247
    • Finkel, T.1    Holbrook, N.J.2
  • 37
    • 0027938689 scopus 로고
    • Oxy- radicals and cancer
    • Cerruti PA. Oxy- radicals and cancer. Lancet 344:862-863, 1994.
    • (1994) Lancet , vol.344 , pp. 862-863
    • Cerruti, P.A.1
  • 38
    • 0034925593 scopus 로고    scopus 로고
    • Tyrosine nitration: LOocalisation, quantification, consequences for protein function and signal transduction
    • Greenace SA, Ischioropoulos H. Tyrosine nitration: LOocalisation, quantification, consequences for protein function and signal transduction. Free Rad Res 34:541-581, 2001.
    • (2001) Free Rad Res , vol.34 , pp. 541-581
    • Greenace, S.A.1    Ischioropoulos, H.2
  • 39
    • 0030878073 scopus 로고    scopus 로고
    • Oxidative DNA damage in the parkinsonian brain. An apparent selective increase in 8-Hydroxyguanine levels in substantia nigra
    • Alan ZI, Jenner A, Daniel SE, Lees AJ, Cairns N, Marsden CD, Jenner P, Halliwell B. Oxidative DNA damage in the parkinsonian brain. An apparent selective increase in 8-Hydroxyguanine levels in substantia nigra. J. Neurochemistry 69:1196-1203, 1997.
    • (1997) J Neurochemistry , vol.69 , pp. 1196-1203
    • Alan, Z.I.1    Jenner, A.2    Daniel, S.E.3    Lees, A.J.4    Cairns, N.5    Marsden, C.D.6    Jenner, P.7    Halliwell, B.8
  • 40
    • 0034946830 scopus 로고    scopus 로고
    • Effect of proteasome inhibition on cellular oxidative damage, antioxidant defences and nitric oxide production
    • Lee M, Hyun DH, Jenner P, Halliwell B. Effect of proteasome inhibition on cellular oxidative damage, antioxidant defences and nitric oxide production. J Neurochem 78:32-41, 2001.
    • (2001) J Neurochem , vol.78 , pp. 32-41
    • Lee, M.1    Hyun, D.H.2    Jenner, P.3    Halliwell, B.4
  • 41
    • 0031831270 scopus 로고    scopus 로고
    • Reactive oxygen-mediated protein oxidation in aging and disease
    • Stadtman ER, Berlet BS. Reactive oxygen-mediated protein oxidation in aging and disease. Drug Metab Rev 30:225-243, 1998.
    • (1998) Drug Metab Rev , vol.30 , pp. 225-243
    • Stadtman, E.R.1    Berlet, B.S.2
  • 42
    • 0036212575 scopus 로고    scopus 로고
    • Regional distribution of heme oxygenase, HSP70, and gluthathione in brain: Relevance for endogenous oxidant/antioxidant balance and stress tolerance
    • Calabrese V, Scapagnini G, Ravagna A, Fariello RG, Giuffrida Stella AM, Abraham NG. Regional distribution of heme oxygenase, HSP70, and gluthathione in brain: Relevance for endogenous oxidant/antioxidant balance and stress tolerance. J Neurosci Res 68:65-75, 2001.
    • (2001) J Neurosci Res , vol.68 , pp. 65-75
    • Calabrese, V.1    Scapagnini, G.2    Ravagna, A.3    Fariello, R.G.4    Giuffrida Stella, A.M.5    Abraham, N.G.6
  • 43
    • 0036236271 scopus 로고    scopus 로고
    • Aging and role of reactive nitrogen species
    • Drew B, Leeuwenburg C. Aging and role of reactive nitrogen species. Ann N Y Acad Sci 959:66-81, 2002.
    • (2002) Ann N Y Acad Sci , vol.959 , pp. 66-81
    • Drew, B.1    Leeuwenburg, C.2
  • 44
    • 17644443401 scopus 로고    scopus 로고
    • Intervention by nitric oxide, NO, and its oxide derivates particularly in mammals
    • Ducrocq C, Servy C, Cudic M, Blanchard EB. Intervention by nitric oxide, NO, and its oxide derivates particularly in mammals. Can J Phisiol Pharmacol 79:95-102, 2001.
    • (2001) Can J Phisiol Pharmacol , vol.79 , pp. 95-102
    • Ducrocq, C.1    Servy, C.2    Cudic, M.3    Blanchard, E.B.4


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