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Volumn 42, Issue 5, 2014, Pages 1261-1277

Saikosaponin-D attenuates heat stress-induced oxidative damage in LLC-PK1 cells by increasing the expression of anti-oxidant enzymes and HSP72

Author keywords

Anti Oxidant Enzymes; Heat Stress; HSP72; LLC PK1; Saikosaponin d

Indexed keywords

ANTIOXIDANT; CATALASE; COPPER ZINC SUPEROXIDE DISMUTASE; GLUTATHIONE PEROXIDASE; GLUTATHIONE PEROXIDASE 1; HEAT SHOCK PROTEIN 72; MALONALDEHYDE; REACTIVE OXYGEN METABOLITE; SAIKOSAPONIN D; SUPEROXIDE DISMUTASE; BUPLEURUM ROOT EXTRACT; OLEANOLIC ACID; PLANT EXTRACT; SAIKOSAPONIN; SAPONIN;

EID: 84926123715     PISSN: 0192415X     EISSN: None     Source Type: Journal    
DOI: 10.1142/S0192415X14500797     Document Type: Article
Times cited : (43)

References (71)
  • 1
    • 0022591975 scopus 로고
    • Effects of saikosaponin-d on aminonucleoside nephrosis in rats
    • Abe, H., M. Orita, H. Konishi, S. Arichi and S. Odashima. Effects of saikosaponin-d on aminonucleoside nephrosis in rats. Eur. J. Pharmacol. 120: 171-178, 1986.
    • (1986) Eur. J. Pharmacol. , vol.120 , pp. 171-178
    • Abe, H.1    Orita, M.2    Konishi, H.3    Arichi, S.4    Odashima, S.5
  • 3
    • 0019170333 scopus 로고
    • Pharmacological actions of saikosaponins isolated from Bupleurum falcatum L. Effects of saikosaponins on liver function
    • Abe, H., M. Sakaguchi, M. Yamada, S. Arichi and S. Odashima. Pharmacological actions of saikosaponins isolated from Bupleurum falcatum L. Effects of saikosaponins on liver function. Planta. Med. 40: 366-372, 1980.
    • (1980) Planta. Med. , vol.40 , pp. 366-372
    • Abe, H.1    Sakaguchi, M.2    Yamada, M.3    Arichi, S.4    Odashima, S.5
  • 4
    • 0020468870 scopus 로고
    • Protective effect of saikosaponin-d isolated from Bupleurum falcatum L. on CCl4-induced liver injury in the rat
    • Abe, H., M. Sakaguchi, S. Odashima and S. Arichi. Protective effect of saikosaponin-d isolated from Bupleurum falcatum L. on CCl4-induced liver injury in the rat. Naunyn Schmiedebergs Arch. Pharmacol. 320: 266-271, 1982.
    • (1982) Naunyn Schmiedebergs Arch. Pharmacol. , vol.320 , pp. 266-271
    • Abe, H.1    Sakaguchi, M.2    Odashima, S.3    Arichi, S.4
  • 5
    • 0021318441 scopus 로고
    • Catalase in vitro
    • Aebi, H. Catalase in vitro. Methods Enzymol. 105: 121-126, 1984.
    • (1984) Methods Enzymol. , vol.105 , pp. 121-126
    • Aebi, H.1
  • 6
    • 0025062963 scopus 로고
    • Identification of cytosolic peroxisome proliferator binding protein as a member of the heat shock protein HSP70 family
    • Alvares, K., A. Carrillo, P.M. Yuan, H. Kawano, R.I. Morimoto and J.K. Reddy. Identification of cytosolic peroxisome proliferator binding protein as a member of the heat shock protein HSP70 family. Proc. Natl. Acad. Sci. USA 87: 5293-5297, 1990.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 5293-5297
    • Alvares, K.1    Carrillo, A.2    Yuan, P.M.3    Kawano, H.4    Morimoto, R.I.5    Reddy, J.K.6
  • 8
    • 0026591027 scopus 로고
    • Thermoprotection of a functional epithelium: Heat stress effects on transepithelial transport by flounder renal tubule in primary monolayer culture
    • Brown, M.A., R.P. Upender, L.E. Hightower and J.L. Renfro. Thermoprotection of a functional epithelium: Heat stress effects on transepithelial transport by flounder renal tubule in primary monolayer culture. Proc. Natl. Acad. Sci. USA 89: 3246-3250, 1992.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 3246-3250
    • Brown, M.A.1    Upender, R.P.2    Hightower, L.E.3    Renfro, J.L.4
  • 9
    • 83655183209 scopus 로고    scopus 로고
    • Effects of vitamin e supplementation on renal non-enzymatic antioxidants in young rats submitted to exhaustive exercise stress
    • Bucioli, S.A., L.C. de Abreu, V.E. Valenti, C. Leone and H. Vannucchi. Effects of vitamin E supplementation on renal non-enzymatic antioxidants in young rats submitted to exhaustive exercise stress. BMC Complement. Altern. Med. 11: 133, 2011.
    • (2011) BMC Complement. Altern. Med. , vol.11 , pp. 133
    • Bucioli, S.A.1    De Abreu, L.C.2    Valenti, V.E.3    Leone, C.4    Vannucchi, H.5
  • 11
    • 0027944443 scopus 로고
    • Alterations in mitochondrial membrane fluidity by lipid peroxidation products
    • Chen, J.J. and B.P. Yu. Alterations in mitochondrial membrane fluidity by lipid peroxidation products. Free Radic. Biol. Med. 17: 411-418, 1994.
    • (1994) Free Radic. Biol. Med. , vol.17 , pp. 411-418
    • Chen, J.J.1    Yu, B.P.2
  • 13
    • 64049099495 scopus 로고    scopus 로고
    • Heat-shock response protects peripheral blood mononuclear cells (PBMCs) from hydrogen peroxide-induced mitochondrial disturbance
    • Chiu, H.Y., L.Y. Tsao and R.C. Yang. Heat-shock response protects peripheral blood mononuclear cells (PBMCs) from hydrogen peroxide-induced mitochondrial disturbance. Cell Stress Chaperones 14: 207-217, 2009.
    • (2009) Cell Stress Chaperones , vol.14 , pp. 207-217
    • Chiu, H.Y.1    Tsao, L.Y.2    Yang, R.C.3
  • 16
    • 0020365443 scopus 로고
    • Separation and characterization of the aldehydic products of lipid peroxidation stimulated by ADP-Fe2\+ in rat liver microsomes
    • Esterbauer, H., K.H. Cheeseman, M.U. Dianzani, G. Poli and T.F. Slater. Separation and characterization of the aldehydic products of lipid peroxidation stimulated by ADP-Fe2\+ in rat liver microsomes. Biochem. J. 208: 129-140, 1982.
    • (1982) Biochem. J. , vol.208 , pp. 129-140
    • Esterbauer, H.1    Cheeseman, K.H.2    Dianzani, M.U.3    Poli, G.4    Slater, T.F.5
  • 17
    • 34249673939 scopus 로고    scopus 로고
    • Saikosaponin-d attenuates the development of liver fibrosis by preventing hepatocyte injury
    • Fan, J., X. Li, P. Li, N. Li, T. Wang, H. Shen, Y. Siow, P. Choy and Y. Gong. Saikosaponin-d attenuates the development of liver fibrosis by preventing hepatocyte injury. Biochem. Cell Biol. 85: 189-195, 2007.
    • (2007) Biochem. Cell Biol. , vol.85 , pp. 189-195
    • Fan, J.1    Li, X.2    Li, P.3    Li, N.4    Wang, T.5    Shen, H.6    Siow, Y.7    Choy, P.8    Gong, Y.9
  • 19
    • 0032924105 scopus 로고    scopus 로고
    • Chaperone-mediated protein folding
    • Fink, A.L. Chaperone-mediated protein folding. Physiol. Rev. 79: 425-449, 1999.
    • (1999) Physiol. Rev. , vol.79 , pp. 425-449
    • Fink, A.L.1
  • 20
    • 84860602128 scopus 로고    scopus 로고
    • Association of summer temperatures with hospital admissions for renal diseases in New York state: A case-crossover study
    • Fletcher, B.A., S. Lin, E.F. Fitzgerald and S.A. Hwang. Association of summer temperatures with hospital admissions for renal diseases in New York state: A case-crossover study. Am. J. Epidemio. 175: 907-916, 2012.
    • (2012) Am. J. Epidemio. , vol.175 , pp. 907-916
    • Fletcher, B.A.1    Lin, S.2    Fitzgerald, E.F.3    Hwang, S.A.4
  • 21
    • 0036618903 scopus 로고    scopus 로고
    • Plant's defence and its benefits for animals and medicine: Role of phenolics and terpenoids in avoiding oxygen stress
    • Grassmann, J., S. Hippeli and E.F. Elstner. Plant's defence and its benefits for animals and medicine: Role of phenolics and terpenoids in avoiding oxygen stress. Plant Physiol. Biochem. 40: 471-478, 2002.
    • (2002) Plant Physiol. Biochem. , vol.40 , pp. 471-478
    • Grassmann, J.1    Hippeli, S.2    Elstner, E.F.3
  • 22
    • 35348905486 scopus 로고    scopus 로고
    • Heat shock protein 70 regulates cellular redox status by modulating glutathione-related enzyme activities
    • Guo, S., W. Wharton, P. Moseley and H. Shi. Heat shock protein 70 regulates cellular redox status by modulating glutathione-related enzyme activities. Cell Stress Chaperones 12: 245-254, 2007.
    • (2007) Cell Stress Chaperones , vol.12 , pp. 245-254
    • Guo, S.1    Wharton, W.2    Moseley, P.3    Shi, H.4
  • 23
    • 0028067242 scopus 로고
    • Hyperthermia stimulates nitric oxide formation: Electron paramagnetic resonance detection of.NO-heme in blood
    • Hall, D.M., G.R. Buettner, R.D. Matthes and C.V. Gisolfi. Hyperthermia stimulates nitric oxide formation: Electron paramagnetic resonance detection of.NO-heme in blood. J. Appl. Physiol. 77: 548-553, 1994.
    • (1994) J. Appl. Physiol. , vol.77 , pp. 548-553
    • Hall, D.M.1    Buettner, G.R.2    Matthes, R.D.3    Gisolfi, C.V.4
  • 24
    • 0027300736 scopus 로고
    • Lipid peroxidation: Its mechanism, measurement, and significance
    • Halliwell, B. and S. Chirico. Lipid peroxidation: Its mechanism, measurement, and significance. Am. J. Clin. Nutr. 57: 715S-724S, 1993.
    • (1993) Am. J. Clin. Nutr. , vol.57 , pp. 715S-724S
    • Halliwell, B.1    Chirico, S.2
  • 25
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl, F.U. Molecular chaperones in cellular protein folding. Nature 381: 571-579, 1996.
    • (1996) Nature , vol.381 , pp. 571-579
    • Hartl, F.U.1
  • 26
    • 0026098411 scopus 로고
    • Studies on antinephritic effects of plant components in rats (1) Effects of saikosaponins original-type anti-GBM nephritis in rats and its mechanisms
    • Hattori, T., M. Ito and Y. Suzuki. Studies on antinephritic effects of plant components in rats (1). Effects of saikosaponins original-type anti-GBM nephritis in rats and its mechanisms. Nihon Yakurigaku Zasshi 97: 13-21, 1991.
    • (1991) Nihon Yakurigaku Zasshi , vol.97 , pp. 13-21
    • Hattori, T.1    Ito, M.2    Suzuki, Y.3
  • 27
    • 84861492925 scopus 로고    scopus 로고
    • Protective effects of total flavonoids from Litsea coreana on alcoholic fatty liver in rats associated with down-regulation adipose differentiation-related protein expression
    • Hu, C.M., Q. Cao, X.W. Lv, W.M. Cheng, R. Li and J. Li. Protective effects of total flavonoids from Litsea coreana on alcoholic fatty liver in rats associated with down-regulation adipose differentiation-related protein expression. Am. J. Chin. Med. 40: 599-610, 2012.
    • (2012) Am. J. Chin. Med. , vol.40 , pp. 599-610
    • Hu, C.M.1    Cao, Q.2    Lv, X.W.3    Cheng, W.M.4    Li, R.5    Li, J.6
  • 29
    • 84928332889 scopus 로고    scopus 로고
    • Comparative effects of phosphoenolpyruvate, a glycolytic intermediate, as an organ preservation agent with glucose and N-acetylcysteine against organ damage during cold storage of mouse liver and kidney
    • Ishitsuka, Y., Y. Fukumoto, Y. Kondo, M. Irikura, D. Kadowaki, Y. Narita, S. Hirata, H. Moriuchi, T. Maruyama, N. Hamasaki and T. Irie. Comparative effects of phosphoenolpyruvate, a glycolytic intermediate, as an organ preservation agent with glucose and N-acetylcysteine against organ damage during cold storage of mouse liver and kidney. ISRN Pharmacol. 2013: 1-7, 2013.
    • (2013) ISRN Pharmacol. , vol.2013 , pp. 1-7
    • Ishitsuka, Y.1    Fukumoto, Y.2    Kondo, Y.3    Irikura, M.4    Kadowaki, D.5    Narita, Y.6    Hirata, S.7    Moriuchi, H.8    Maruyama, T.9    Hamasaki, N.10    Irie, T.11
  • 30
    • 0027457953 scopus 로고
    • Thermotolerance in mammalian cells Protein denaturation and aggregation, and stress proteins
    • Kampinga, H.H. Thermotolerance in mammalian cells. Protein denaturation and aggregation, and stress proteins. J. Cell Sci. 104: 11-17, 1993.
    • (1993) J. Cell Sci. , vol.104 , pp. 11-17
    • Kampinga, H.H.1
  • 31
    • 0028903343 scopus 로고
    • Cell type-oriented differential modulatory actions of saikosaponin-d on growth responses and DNA fragmentation of lymphocytes triggered by receptor-mediated and receptor-bypassed pathways
    • Kato, M., M.Y. Pu, K. Isobe, T. Hattori, N. Yanagita and I. Nakashima. Cell type-oriented differential modulatory actions of saikosaponin-d on growth responses and DNA fragmentation of lymphocytes triggered by receptor-mediated and receptor-bypassed pathways. Immunopharmacology 29: 207-213, 1995.
    • (1995) Immunopharmacology , vol.29 , pp. 207-213
    • Kato, M.1    Pu, M.Y.2    Isobe, K.3    Hattori, T.4    Yanagita, N.5    Nakashima, I.6
  • 32
    • 0036461668 scopus 로고    scopus 로고
    • The effect of hyperthermia on the induction of cell death in brain, testis, and thymus of the adult and developing rat
    • Khan, V.R. and I.R. Brown. The effect of hyperthermia on the induction of cell death in brain, testis, and thymus of the adult and developing rat. Cell Stress Chaperones 7: 73-90, 2002.
    • (2002) Cell Stress Chaperones , vol.7 , pp. 73-90
    • Khan, V.R.1    Brown, I.R.2
  • 33
    • 0031793127 scopus 로고    scopus 로고
    • Heat shock protein 70 kDa: Molecular biology, biochemistry, and physiology
    • Kiang, J.G. and G.C. Tsokos. 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
  • 34
    • 77953613805 scopus 로고    scopus 로고
    • Public health impact of global heating due to climate change: Potential effects on chronic non-communicable diseases
    • Kjellstrom, T., A.J. Butler, R.M. Lucas and R. Bonita. Public health impact of global heating due to climate change: Potential effects on chronic non-communicable diseases. Int. J. Public Health 55: 97-103, 2010.
    • (2010) Int. J. Public Health , vol.55 , pp. 97-103
    • Kjellstrom, T.1    Butler, A.J.2    Lucas, R.M.3    Bonita, R.4
  • 36
    • 0032973148 scopus 로고    scopus 로고
    • Overexpression of the human 72 kDa heat shock protein in renal tubular cells confers resistance against oxidative injury and cisplatin toxicity
    • Komatsuda, A., H. Wakui, Y. Oyama, H. Imai, A.B. Miura, H. Itoh and Y. Tashima. Overexpression of the human 72 kDa heat shock protein in renal tubular cells confers resistance against oxidative injury and cisplatin toxicity. Nephrol. Dial. Transplant. 14: 1385-1390, 1999.
    • (1999) Nephrol. Dial. Transplant. , vol.14 , pp. 1385-1390
    • Komatsuda, A.1    Wakui, H.2    Oyama, Y.3    Imai, H.4    Miura, A.B.5    Itoh, H.6    Tashima, Y.7
  • 37
    • 0030597122 scopus 로고    scopus 로고
    • Expression of HSP 70 mRNA is induced in the brain of transgenic mice overexpressing human CuZn-superoxide dismutase following transient global cerebral ischemia
    • Kondo, T., K. Murakami, J. Honkaniemi, F.R. Sharp, C.J. Epstein and P.H. Chan. Expression of HSP 70 mRNA is induced in the brain of transgenic mice overexpressing human CuZn-superoxide dismutase following transient global cerebral ischemia. Brain Res. 737: 321-326, 1996.
    • (1996) Brain Res. , vol.737 , pp. 321-326
    • Kondo, T.1    Murakami, K.2    Honkaniemi, J.3    Sharp, F.R.4    Epstein, C.J.5    Chan, P.H.6
  • 38
    • 0000224564 scopus 로고
    • The constitution of saponins isolated from Bupleurum falcatum L
    • Kubota, T. and H. Hinoh. The constitution of saponins isolated from Bupleurum falcatum L. Tetrahedron Lett. 9: 303-306, 1968.
    • (1968) Tetrahedron Lett. , vol.9 , pp. 303-306
    • Kubota, T.1    Hinoh, H.2
  • 39
    • 0038376295 scopus 로고    scopus 로고
    • Cellular effects of hyperthermia: Relevance to the minimum dose for thermal damage
    • Lepock, J.R. Cellular effects of hyperthermia: Relevance to the minimum dose for thermal damage. Int. J. Hyperthermia 19: 252-266, 2003.
    • (2003) Int. J. Hyperthermia , vol.19 , pp. 252-266
    • Lepock, J.R.1
  • 40
    • 84871258771 scopus 로고    scopus 로고
    • Dendrobium moniliforme attenuates high-fat diet-induced renal damage in mice through the regulation of lipid-induced oxidative stress
    • Lee, W., D.W. Eom, Y. Jung, N. Yamabe, S. Lee, Y. Jeon, Y.R. Hwang, J.H. Lee, Y.K. Kim, K.S. Kang and S.N. Kim. Dendrobium moniliforme attenuates high-fat diet-induced renal damage in mice through the regulation of lipid-induced oxidative stress. Am. J. Chin. Med. 40: 1217-1228, 2012.
    • (2012) Am. J. Chin. Med. , vol.40 , pp. 1217-1228
    • Lee, W.1    Eom, D.W.2    Jung, Y.3    Yamabe, N.4    Lee, S.5    Jeon, Y.6    Hwang, Y.R.7    Lee, J.H.8    Kim, Y.K.9    Kang, K.S.10    Kim, S.N.11
  • 41
    • 19444373031 scopus 로고    scopus 로고
    • Ultrasound-assisted extraction methodology as a tool to improve the antioxidant properties of herbal drug Xiao-chia-hu-tang
    • Liu, C.T., C.Y. Wu, Y.M. Weng and C.Y. Tseng. Ultrasound-assisted extraction methodology as a tool to improve the antioxidant properties of herbal drug Xiao-chia-hu-tang. J. Ethnopharmacol. 99: 293-300, 2005.
    • (2005) J. Ethnopharmacol. , vol.99 , pp. 293-300
    • Liu, C.T.1    Wu, C.Y.2    Weng, Y.M.3    Tseng, C.Y.4
  • 42
    • 84878377687 scopus 로고    scopus 로고
    • PI3K/AKT/mTOR signaling is involved in (-)-epigallocatechin-3-gallate-induced apoptosis of human pancreatic carcinoma cells
    • Liu, S., X.J. Wang, Y. Liu and Y.F. Cui. PI3K/AKT/mTOR signaling is involved in (-)-epigallocatechin-3-gallate-induced apoptosis of human pancreatic carcinoma cells. Am. J. Chin. Med. 41: 629-642, 2013.
    • (2013) Am. J. Chin. Med. , vol.41 , pp. 629-642
    • Liu, S.1    Wang, X.J.2    Liu, Y.3    Cui, Y.F.4
  • 43
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2CT method
    • Livak, K.J. and T.D. Schmittgen. Analysis of relative gene expression data using real-time quantitative PCR and the 2-CT method. Methods 25: 402-408, 2001.
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 44
    • 0037090046 scopus 로고    scopus 로고
    • Heat shock inactivates cellular antioxidant defenses against hydrogen peroxide: Protection by glucose
    • Lord-Fontaine, S. and D.A. Averill-Bates. Heat shock inactivates cellular antioxidant defenses against hydrogen peroxide: Protection by glucose. Free Radic. Biol. Med. 32: 752-765, 2002.
    • (2002) Free Radic. Biol. Med. , vol.32 , pp. 752-765
    • Lord-Fontaine, S.1    Averill-Bates, D.A.2
  • 45
    • 34247892466 scopus 로고    scopus 로고
    • Clofibrate treatment in pigs: Effects on parameters critical with respect to peroxisome proliferator-induced hepatocarcinogenesis in rodents
    • Luci, S., B. Giemsa, G. Hause, H. Kluge and K. Eder. Clofibrate treatment in pigs: Effects on parameters critical with respect to peroxisome proliferator-induced hepatocarcinogenesis in rodents. BMC Pharmacol. 7: 1-11, 2007.
    • (2007) BMC Pharmacol. , vol.7 , pp. 1-11
    • Luci, S.1    Giemsa, B.2    Hause, G.3    Kluge, H.4    Eder, K.5
  • 47
    • 0014691242 scopus 로고
    • Superoxide dismutase an enzymic function for erythrocuprein (hemocuprein)
    • McCord, J.M. and I. Fridovich. Superoxide dismutase an enzymic function for erythrocuprein (hemocuprein). J. Biol. Chem. 244: 6049-6055, 1969.
    • (1969) J. Biol. Chem. , vol.244 , pp. 6049-6055
    • McCord, J.M.1    Fridovich, I.2
  • 48
    • 0028170326 scopus 로고
    • Importance of Se-glutathione peroxidase, catalase, and Cu/Zn-SOD for cell survival against oxidative stress
    • Michiels, C., M. Raes, O. Toussaint and J. Remacle. Importance of Se-glutathione peroxidase, catalase, and Cu/Zn-SOD for cell survival against oxidative stress. Free Radic. Biol. Med. 17: 235-248, 1994.
    • (1994) Free Radic. Biol. Med. , vol.17 , pp. 235-248
    • Michiels, C.1    Raes, M.2    Toussaint, O.3    Remacle, J.4
  • 49
    • 34447315295 scopus 로고    scopus 로고
    • Sequential changes in superoxide production, anion carriers and substrate oxidation in skeletal muscle mitochondria of heat-stressed chickens
    • Mujahid, A., Y. Akiba, C.H. Warden and M. Toyomizu. Sequential changes in superoxide production, anion carriers and substrate oxidation in skeletal muscle mitochondria of heat-stressed chickens. FEBS Lett. 581: 3461-3467, 2007.
    • (2007) FEBS Lett. , vol.581 , pp. 3461-3467
    • Mujahid, A.1    Akiba, Y.2    Warden, C.H.3    Toyomizu, M.4
  • 50
    • 0018384650 scopus 로고
    • Assay for lipid peroxides in animal tissues by thiobarbituric acid reaction
    • Ohkawa, H., N. Ohishi and K. Yagi. Assay for lipid peroxides in animal tissues by thiobarbituric acid reaction. Anal. Biochem. 95: 351-358, 1979.
    • (1979) Anal. Biochem. , vol.95 , pp. 351-358
    • Ohkawa, H.1    Ohishi, N.2    Yagi, K.3
  • 51
    • 0027135501 scopus 로고
    • The function of heat-shock proteins in stress tolerance: Degradation and reactivation of damaged proteins
    • Parsell, D.A. and S. Lindquist. The function of heat-shock proteins in stress tolerance: Degradation and reactivation of damaged proteins. Annu. Rev. Genet. 27: 437-496, 1993.
    • (1993) Annu. Rev. Genet. , vol.27 , pp. 437-496
    • Parsell, D.A.1    Lindquist, S.2
  • 52
    • 84862902475 scopus 로고    scopus 로고
    • Implication of oxidative stress in size-dependent toxicity of silica nanoparticles in kidney cells
    • Passagne, I., M. Morille, M. Rousset, I. Pujalté and B. L'azou. Implication of oxidative stress in size-dependent toxicity of silica nanoparticles in kidney cells. Toxicology 299: 112-124, 2012.
    • (2012) Toxicology , vol.299 , pp. 112-124
    • Passagne, I.1    Morille, M.2    Rousset, M.3    Pujalté, I.4    L'Azou, B.5
  • 53
    • 74049097964 scopus 로고    scopus 로고
    • Cardioprotection by CaMKII-B is mediated by phosphorylation of heat shock factor 1 and subsequent expression of inducible heat shock protein 70
    • Peng, W., Y. Zhang, M. Zheng, H. Cheng, W. Zhu, C.M. Cao and R.P. Xiao. Cardioprotection by CaMKII-B is mediated by phosphorylation of heat shock factor 1 and subsequent expression of inducible heat shock protein 70. Circ. Res. 106: 102-110, 2010.
    • (2010) Circ. Res. , vol.106 , pp. 102-110
    • Peng, W.1    Zhang, Y.2    Zheng, M.3    Cheng, H.4    Zhu, W.5    Cao, C.M.6    Xiao, R.P.7
  • 54
    • 84869390703 scopus 로고    scopus 로고
    • Characterization of the constitutive pig ovary heat shock chaperone machinery and its response to acute thermal stress or to seasonal variations
    • Pennarossa, G., S. Maffei, M.M. Rahman, G. Berruti, T.A. Brevini and F. Gandolfi. Characterization of the constitutive pig ovary heat shock chaperone machinery and its response to acute thermal stress or to seasonal variations. Biol. Reprod. 87: 119, 2012.
    • (2012) Biol. Reprod. , vol.87 , pp. 119
    • Pennarossa, G.1    Maffei, S.2    Rahman, M.M.3    Berruti, G.4    Brevini, T.A.5    Gandolfi, F.6
  • 58
    • 84863347038 scopus 로고    scopus 로고
    • Cytotoxic effect of Eucalyptus citriodora resin on human hepatoma HepG2 cells
    • Shen, K.H., Z.T. Chen and P.D. Duh. Cytotoxic effect of Eucalyptus citriodora resin on human hepatoma HepG2 cells. Am. J. Chin. Med. 40: 399-413, 2012.
    • (2012) Am. J. Chin. Med. , vol.40 , pp. 399-413
    • Shen, K.H.1    Chen, Z.T.2    Duh, P.D.3
  • 60
    • 0028875592 scopus 로고
    • Heat-shock proteins in animal models for acute renal failure
    • Wakui, H., A. Komatsuda and A.B. Miura. Heat-shock proteins in animal models for acute renal failure. Ren. Fail. 17: 641-649, 1995.
    • (1995) Ren. Fail. , vol.17 , pp. 641-649
    • Wakui, H.1    Komatsuda, A.2    Miura, A.B.3
  • 61
    • 12344262051 scopus 로고    scopus 로고
    • Antioxidant activity of Bupleurum kaoi Liu (Chao et Chuang) fractions fractionated by supercritical CO2
    • Wang, B.J., C.T. Liu, C.Y. Tseng and Z.R. Yu. Antioxidant activity of Bupleurum kaoi Liu (Chao et Chuang) fractions fractionated by supercritical CO2. LWT-Food Sci. Technol. 38: 281-287, 2005.
    • (2005) LWT-Food Sci. Technol. , vol.38 , pp. 281-287
    • Wang, B.J.1    Liu, C.T.2    Tseng, C.Y.3    Yu, Z.R.4
  • 62
    • 70649092057 scopus 로고    scopus 로고
    • Estrogen-like activities of saikosaponin-d in vitro: A pilot study
    • Wang, P., J. Ren, J. Tang, D. Zhang, B. Li and Y. Li. Estrogen-like activities of saikosaponin-d in vitro: A pilot study. Eur. J. Pharmacol. 626: 159-165, 2010.
    • (2010) Eur. J. Pharmacol. , vol.626 , pp. 159-165
    • Wang, P.1    Ren, J.2    Tang, J.3    Zhang, D.4    Li, B.5    Li, Y.6
  • 63
    • 0036556790 scopus 로고    scopus 로고
    • Hsp72 expression enhances survival in adenosine triphosphate-depleted renal epithelial cells
    • Wang, Y.H., A.A. Knowlton, F.H. Li and S.C. Borkan. Hsp72 expression enhances survival in adenosine triphosphate-depleted renal epithelial cells. Cell Stress Chaperones 7: 137-145, 2002.
    • (2002) Cell Stress Chaperones , vol.7 , pp. 137-145
    • Wang, Y.H.1    Knowlton, A.A.2    Li, F.H.3    Borkan, S.C.4
  • 64
    • 0032707074 scopus 로고    scopus 로고
    • Antioxidants in the prevention of renal disease
    • Wardle, E.N. Antioxidants in the prevention of renal disease. Ren. Fail. 21: 581-591, 1999.
    • (1999) Ren. Fail. , vol.21 , pp. 581-591
    • Wardle, E.N.1
  • 66
    • 84864213355 scopus 로고    scopus 로고
    • The inhibitory effect of Rheum palmatum against coxsackievirus B3 in vitro and in vivo
    • Xiong, H.R., Y.Y. Shen, L. Lu, W. Hou, F. Luo, H. Xiao and Z.Q. Yang. The inhibitory effect of Rheum palmatum against coxsackievirus B3 in vitro and in vivo. Am. J. Chin. Med. 40: 801-812, 2012.
    • (2012) Am. J. Chin. Med. , vol.40 , pp. 801-812
    • Xiong, H.R.1    Shen, Y.Y.2    Lu, L.3    Hou, W.4    Luo, F.5    Xiao, H.6    Yang, Z.Q.7
  • 67
    • 0025247797 scopus 로고
    • Stress proteins and immunology
    • Young, R.A. Stress proteins and immunology. Annu Rev Immunol. 8: 401-420, 1990.
    • (1990) Annu Rev Immunol. , vol.8 , pp. 401-420
    • Young, R.A.1
  • 68
    • 0037781444 scopus 로고    scopus 로고
    • Production of superoxide dismutase by Deinococcus radiophilus
    • Yun, Y.S. and Y.N. Lee. Production of superoxide dismutase by Deinococcus radiophilus. J. Biochem. Mol. Biol. 36: 282-287, 2003.
    • (2003) J. Biochem. Mol. Biol. , vol.36 , pp. 282-287
    • Yun, Y.S.1    Lee, Y.N.2
  • 69
    • 80051791455 scopus 로고    scopus 로고
    • Selenomethionine: An effective selenium source for sow to improve Se distribution, antioxidant status, and growth performance of pig offspring
    • Zhan, X., Y. Qie, M. Wang, X. Li and R. Zhao. Selenomethionine: An effective selenium source for sow to improve Se distribution, antioxidant status, and growth performance of pig offspring. Biol. Trace Elem. Res. 142: 481-491, 2011.
    • (2011) Biol. Trace Elem. Res. , vol.142 , pp. 481-491
    • Zhan, X.1    Qie, Y.2    Wang, M.3    Li, X.4    Zhao, R.5
  • 70
    • 9444222523 scopus 로고    scopus 로고
    • Redox modulation of the liver with chronic antioxidant enzyme mimetic treatment prevents age-related oxidative damage associated with environmental stress
    • Zhang, H.J., S.R. Doctrow, L. Xu, L.W. Oberley, B. Beecher, J. Morrison, T.D. Oberley and K.C. Kregel. Redox modulation of the liver with chronic antioxidant enzyme mimetic treatment prevents age-related oxidative damage associated with environmental stress. FASEB J. 18: 1547-1549, 2004.
    • (2004) FASEB J. , vol.18 , pp. 1547-1549
    • Zhang, H.J.1    Doctrow, S.R.2    Xu, L.3    Oberley, L.W.4    Beecher, B.5    Morrison, J.6    Oberley, T.D.7    Kregel, K.C.8
  • 71
    • 67349210647 scopus 로고    scopus 로고
    • Saikosaponin accumulation and antioxidative protection in droughtstressed Bupleurum chinense DC plants
    • Zhu, Z., Z. Liang and R. Han. Saikosaponin accumulation and antioxidative protection in droughtstressed Bupleurum chinense DC plants. Environ. Exp. Bot. 66: 326-333, 2009.
    • (2009) Environ. Exp. Bot. , vol.66 , pp. 326-333
    • Zhu, Z.1    Liang, Z.2    Han, R.3


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