메뉴 건너뛰기




Volumn 2, Issue 4, 2005, Pages 529-536

Modulation of radiation-induced disturbances of antioxidant defense systems by ginsan

Author keywords

Antioxidant enzyme; Cytokine; Ginsan; Radiation

Indexed keywords

ANTIOXIDANT; CATALASE; COPPER ZINC SUPEROXIDE DISMUTASE; CYTOKINE; GAMMA INTERFERON; GINSAN; GINSENG EXTRACT; GLUTATHIONE PEROXIDASE; HEME OXYGENASE 1; INTERLEUKIN 1; MANGANESE SUPEROXIDE DISMUTASE; MESSENGER RNA; POLYSACCHARIDE; RADIOPROTECTIVE AGENT; REACTIVE OXYGEN METABOLITE; THIOL; TRANSFORMING GROWTH FACTOR BETA; TUMOR NECROSIS FACTOR; UNCLASSIFIED DRUG;

EID: 28644448318     PISSN: 1741427X     EISSN: 17414288     Source Type: Journal    
DOI: 10.1093/ecam/neh123     Document Type: Article
Times cited : (47)

References (58)
  • 1
    • 0032030989 scopus 로고    scopus 로고
    • Role of antioxidant enzymes on ionizing radiation resistance
    • Sun J, Chen Y, Li M, Ge Z. Role of antioxidant enzymes on ionizing radiation resistance. Free Radic Biol Med 1998;24:586-93.
    • (1998) Free Radic Biol Med , vol.24 , pp. 586-593
    • Sun, J.1    Chen, Y.2    Li, M.3    Ge, Z.4
  • 2
    • 0029869189 scopus 로고    scopus 로고
    • Mechanisms involved in the generation of free radical
    • Halliwell B. Mechanisms involved in the generation of free radical. Pathol Biol 1996;44:6-13.
    • (1996) Pathol Biol , vol.44 , pp. 6-13
    • Halliwell, B.1
  • 3
    • 17944392524 scopus 로고    scopus 로고
    • Chemopreventive effect of carotenoids and curcumins on mouse colon carcinogenesis after 1,2-dimethylhydrazine initiation
    • Kim JM, Araki S, Kim DJ, Park CB, Takasuka N, Baba-Toriyama H, et al. Chemopreventive effect of carotenoids and curcumins on mouse colon carcinogenesis after 1,2-dimethylhydrazine initiation. Carcinogenesis 1998;19:81-5.
    • (1998) Carcinogenesis , vol.19 , pp. 81-85
    • Kim, J.M.1    Araki, S.2    Kim, D.J.3    Park, C.B.4    Takasuka, N.5    Baba-Toriyama, H.6
  • 4
    • 0025122820 scopus 로고
    • Inhibition of oxygen toxicity by targeting superoxide dismutase to endothelial cell surface
    • Inoue M, Watanabe N, Morino Y, Tanaka Y, Amachi T, Sasaki J. Inhibition of oxygen toxicity by targeting superoxide dismutase to endothelial cell surface. FEBS Lett 1990;269:89-92.
    • (1990) FEBS Lett , vol.269 , pp. 89-92
    • Inoue, M.1    Watanabe, N.2    Morino, Y.3    Tanaka, Y.4    Amachi, T.5    Sasaki, J.6
  • 5
    • 0030967165 scopus 로고    scopus 로고
    • A controlled study trial of selegiline, alpha-tocopherol, or both as treatment of Alzheimer's disease
    • Sano M, Ernersto C, Thomas RG. A controlled study trial of selegiline, alpha-tocopherol, or both as treatment of Alzheimer's disease. N Engl J Med 1997;336:1216-22.
    • (1997) N Engl J Med , vol.336 , pp. 1216-1222
    • Sano, M.1    Ernersto, C.2    Thomas, R.G.3
  • 6
    • 0024385264 scopus 로고
    • Catalase: Its role in xenobiotic detoxification
    • Calabrese FJ, Canada AT. Catalase: its role in xenobiotic detoxification. Pharmacol Ther 1989;44:297-307.
    • (1989) Pharmacol Ther , vol.44 , pp. 297-307
    • Calabrese, F.J.1    Canada, A.T.2
  • 7
    • 0024386312 scopus 로고
    • Superoxide dismutase: Its role in xenobiotic detoxification
    • Canada AT, Calabrese EJ. Superoxide dismutase: its role in xenobiotic detoxification. Pharmacol Ther 1989;44:285-95.
    • (1989) Pharmacol Ther , vol.44 , pp. 285-295
    • Canada, A.T.1    Calabrese, E.J.2
  • 8
    • 0026468245 scopus 로고
    • On the antioxidant effects of ascorbic acid and glutathione
    • Meister A. On the antioxidant effects of ascorbic acid and glutathione. Biochem Pharmacol 1992;44:1905-15.
    • (1992) Biochem Pharmacol , vol.44 , pp. 1905-1915
    • Meister, A.1
  • 9
    • 85008061021 scopus 로고
    • Biosynthesis and functions of glutathione, an essential biofactor
    • Meister A. Biosynthesis and functions of glutathione, an essential biofactor. J Nutr Sci Vitaminol (Tokyo) Spec 1992;1-6.
    • (1992) J Nutr Sci Vitaminol (Tokyo) Spec , pp. 1-6
    • Meister, A.1
  • 10
    • 0027931061 scopus 로고
    • Immunolocalization of antioxidant enzymes in adult hamster kidney
    • Muse KE, Oberley TD, Sempf JM, Oberley LW. Immunolocalization of antioxidant enzymes in adult hamster kidney. Histochem J 1994;26:734-53.
    • (1994) Histochem J , vol.26 , pp. 734-753
    • Muse, K.E.1    Oberley, T.D.2    Sempf, J.M.3    Oberley, L.W.4
  • 11
    • 0023731036 scopus 로고
    • Heme oxygenase: Function, multiplicity, regulatory mechanisms, and clinical applications
    • Maines MD. Heme oxygenase: function, multiplicity, regulatory mechanisms, and clinical applications. FASEB J 1988;2:2557-68.
    • (1988) FASEB J , vol.2 , pp. 2557-2568
    • Maines, M.D.1
  • 13
    • 0024421581 scopus 로고
    • State of the art: Pulmonary strategies of antioxidant defense
    • Heffner JA, Repine JE. State of the art: pulmonary strategies of antioxidant defense. Am Rev Respir Dis 1989;140:531-54.
    • (1989) Am Rev Respir Dis , vol.140 , pp. 531-554
    • Heffner, J.A.1    Repine, J.E.2
  • 14
    • 0029824431 scopus 로고    scopus 로고
    • Antioxidants in human health and disease
    • Halliwell B. Antioxidants in human health and disease. Annu Rev Nutr 1996;16:33-509.
    • (1996) Annu Rev Nutr , vol.16 , pp. 33-509
    • Halliwell, B.1
  • 16
    • 0022657588 scopus 로고
    • Antioxidant properties of the proteins ceruloplasmin, albumin and transferring. A study of their activity in serum and synovial fluid from patients rheumatoid arthritis
    • Gutteridge JM. Antioxidant properties of the proteins ceruloplasmin, albumin and transferring. A study of their activity in serum and synovial fluid from patients rheumatoid arthritis. Biochem Biophys Acta 1986;869:119-27.
    • (1986) Biochem Biophys Acta , vol.869 , pp. 119-127
    • Gutteridge, J.M.1
  • 17
    • 0020257680 scopus 로고
    • Antistress, antifatigue properties of panax ginseng; Comparison with piracetan
    • Banerjce U, Izquierdo JA. Antistress, antifatigue properties of panax ginseng; Comparison with piracetan. Acta Physiol Lat Am 1982;32:277-85.
    • (1982) Acta Physiol Lat Am , vol.32 , pp. 277-285
    • Banerjce, U.1    Izquierdo, J.A.2
  • 18
    • 0025753762 scopus 로고
    • Anti-lipid peroxidative effect of ginsenoside Rbl and Rgl
    • Deng HL, Zhang JT. Anti-lipid peroxidative effect of ginsenoside Rbl and Rgl. Chin Med J (Engl) 1991;104:395-8.
    • (1991) Chin Med J (Engl) , vol.104 , pp. 395-398
    • Deng, H.L.1    Zhang, J.T.2
  • 19
    • 0027434128 scopus 로고
    • Effect of subchronic administration of antioxdants against cigarette smoke exposure in rats
    • Sohn JO, Lim HB, Lee YC, Lee DW, Kim YT. Effect of subchronic administration of antioxdants against cigarette smoke exposure in rats. Arch Toxicol 1993;67:667-73.
    • (1993) Arch Toxicol , vol.67 , pp. 667-673
    • Sohn, J.O.1    Lim, H.B.2    Lee, Y.C.3    Lee, D.W.4    Kim, Y.T.5
  • 20
    • 0030058280 scopus 로고    scopus 로고
    • Ginseng extract scavenges hydroxyl radical, protects unsaturated fatty acid from decomposition caused by iron-mediated lipid peroxidation
    • Zhang D, Yasuda T, Yu Y, Zheng P, Kawabata T, Ma Y, et al. Ginseng extract scavenges hydroxyl radical, protects unsaturated fatty acid from decomposition caused by iron-mediated lipid peroxidation. Free Radic Biol Med 1996;20:145-50.
    • (1996) Free Radic Biol Med , vol.20 , pp. 145-150
    • Zhang, D.1    Yasuda, T.2    Yu, Y.3    Zheng, P.4    Kawabata, T.5    Ma, Y.6
  • 21
    • 0027099857 scopus 로고
    • Ginsenosides protect pulmonary vascular endothelium against free radical-induced injury
    • Kim H, Chen X, Gillis N. Ginsenosides protect pulmonary vascular endothelium against free radical-induced injury. Biochem Biophys Res Commun 1992;189:670-6.
    • (1992) Biochem Biophys Res Commun , vol.189 , pp. 670-676
    • Kim, H.1    Chen, X.2    Gillis, N.3
  • 22
    • 0000626726 scopus 로고    scopus 로고
    • Transcriptional activation of the Cu, Zn-superoxide dismutase gene through the AP2 site by ginsenoside Rb2 extracted from a medical plant, Panax ginseng
    • Kim YH, Park KH, Rho HM. Transcriptional activation of the Cu, Zn-superoxide dismutase gene through the AP2 site by ginsenoside Rb2 extracted from a medical plant, Panax ginseng. J Biol Chem 1996;271:24539-43.
    • (1996) J Biol Chem , vol.271 , pp. 24539-24543
    • Kim, Y.H.1    Park, K.H.2    Rho, H.M.3
  • 24
    • 0029020434 scopus 로고
    • Irradiation increases manganese superoxide dismutase mRNA levels in human fibroblasts
    • Aksahi M, Hachiya M, Paquette RL, Osawa YS, Shimizu SG. Irradiation increases manganese superoxide dismutase mRNA levels in human fibroblasts. J Biol Chem 1995;270:15864-9.
    • (1995) J Biol Chem , vol.270 , pp. 15864-15869
    • Aksahi, M.1    Hachiya, M.2    Paquette, R.L.3    Osawa, Y.S.4    Shimizu, S.G.5
  • 25
    • 0024202127 scopus 로고
    • Induction of manganous superoxide dismutase by tumor necrosis factor: Possible protective mechanism
    • Wong GH, Goeddel DV. Induction of manganous superoxide dismutase by tumor necrosis factor: possible protective mechanism. Science 1988;242:941-4.
    • (1988) Science , vol.242 , pp. 941-944
    • Wong, G.H.1    Goeddel, D.V.2
  • 26
    • 0038012771 scopus 로고    scopus 로고
    • Antioxidant activity of peptides obtained from porcine myofibrillar proteins by protease treatment
    • Saiga A, Tanabe S, Nishimura T. Antioxidant activity of peptides obtained from porcine myofibrillar proteins by protease treatment. J Agric Food Chem 2003;51:3661-7.
    • (2003) J Agric Food Chem , vol.51 , pp. 3661-3667
    • Saiga, A.1    Tanabe, S.2    Nishimura, T.3
  • 27
    • 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 1976;72:248-54.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 28
    • 0014691273 scopus 로고
    • The utility of superoxide dismutase in studying free radical reaction. I. Radicals generated by the interaction of sulfite, dimethyl sulfoxide, and oxygen
    • McCord JM, Fridovich I. The utility of superoxide dismutase in studying free radical reaction. I. Radicals generated by the interaction of sulfite, dimethyl sulfoxide, and oxygen. J Biol Chem 1969;244:6056-63.
    • (1969) J Biol Chem , vol.244 , pp. 6056-6063
    • McCord, J.M.1    Fridovich, I.2
  • 30
    • 0021288821 scopus 로고
    • Assays of glutathione peroxidase
    • Flohe L, Gunzler WA. Assays of glutathione peroxidase. Methods Enzymol 1984;105:114-21.
    • (1984) Methods Enzymol , vol.105 , pp. 114-121
    • Flohe, L.1    Gunzler, W.A.2
  • 31
    • 0033648666 scopus 로고    scopus 로고
    • Heme oxygenase activity: Current methods, applications
    • Ryter SW, Kvam E, Tyrrell RM. Heme oxygenase activity: current methods, applications. Methods Mol Biol 2000;99:369-91.
    • (2000) Methods Mol Biol , vol.99 , pp. 369-391
    • Ryter, S.W.1    Kvam, E.2    Tyrrell, R.M.3
  • 32
    • 0014428865 scopus 로고
    • Estimation of total, protein-bound, nonprotein sulfhydryl groups in tissues with Ellman's reagent
    • Sedlack J, Lindsay RH. Estimation of total, protein-bound, nonprotein sulfhydryl groups in tissues with Ellman's reagent. Anal Biochem 1968;25:192-205.
    • (1968) Anal Biochem , vol.25 , pp. 192-205
    • Sedlack, J.1    Lindsay, R.H.2
  • 33
    • 0027523219 scopus 로고
    • Glutathione depletion induced heme oxygenase-1 (HSP32) mRNA and protein in rat brain
    • Ewing JE, Maines MD. Glutathione depletion induced heme oxygenase-1 (HSP32) mRNA and protein in rat brain. J Neurochem 1993;60:1512-19.
    • (1993) J Neurochem , vol.60 , pp. 1512-1519
    • Ewing, J.E.1    Maines, M.D.2
  • 34
    • 0017641237 scopus 로고
    • Regulation of heme pathway enzymes and cellular glutathione content by metals that do not chelate with tetrapyrroles: Blockade of metals effects by thiol
    • Maines MD, Kappas A. Regulation of heme pathway enzymes and cellular glutathione content by metals that do not chelate with tetrapyrroles: blockade of metals effects by thiol. Proc Natl Acad Sci USA 1977;74:1875-8.
    • (1977) Proc Natl Acad Sci USA , vol.74 , pp. 1875-1878
    • Maines, M.D.1    Kappas, A.2
  • 35
    • 0017360740 scopus 로고
    • Cobalt regulation of heme synthesis and degradation in avian embryo liver cell culture
    • Maines MD, Sinclair P. Cobalt regulation of heme synthesis and degradation in avian embryo liver cell culture. J Biol Chem 1977;252:219-23.
    • (1977) J Biol Chem , vol.252 , pp. 219-223
    • Maines, M.D.1    Sinclair, P.2
  • 37
    • 0034731385 scopus 로고    scopus 로고
    • Smad7-dependent regulation of heme oxygenase-1 by transforming growth factor-in human renal epithelial cells
    • Hill-Kapturczak N, Truong L, Thamilselvan V, Visner GA, Nick HS, Agarwall A. Smad7-dependent regulation of heme oxygenase-1 by transforming growth factor-(in human renal epithelial cells. J Biol Chem 2002;275:40904-9.
    • (2002) J Biol Chem , vol.275 , pp. 40904-40909
    • Hill-Kapturczak, N.1    Truong, L.2    Thamilselvan, V.3    Visner, G.A.4    Nick, H.S.5    Agarwall, A.6
  • 38
    • 0029020434 scopus 로고
    • Irradiation increases manganese superoxide dismutase mRNA levels in human fibroblasts
    • Aksahi M, Hachiya M, Paquette RL, Osawa YS, Shimizu SG. Irradiation increases manganese superoxide dismutase mRNA levels in human fibroblasts. J Biol Chem 1995;270:15864-9.
    • (1995) J Biol Chem , vol.270 , pp. 15864-15869
    • Aksahi, M.1    Hachiya, M.2    Paquette, R.L.3    Osawa, Y.S.4    Shimizu, S.G.5
  • 40
    • 0033981472 scopus 로고    scopus 로고
    • Copper, zinc-superoxide dismutase protects from ultraviolet B-induced apoptosis of SV40-transformed human keratinocytes: The protection is associated with the increased levels of antioxidant enzymes
    • Takahashi H, Hashimoto Y, Aoki N, Kinouchi M, Ishida YA, Iizuka H. Copper, zinc-superoxide dismutase protects from ultraviolet B-induced apoptosis of SV40-transformed human keratinocytes: the protection is associated with the increased levels of antioxidant enzymes. J Dermatol Sci 2000;23:12-21.
    • (2000) J Dermatol Sci , vol.23 , pp. 12-21
    • Takahashi, H.1    Hashimoto, Y.2    Aoki, N.3    Kinouchi, M.4    Ishida, Y.A.5    Iizuka, H.6
  • 43
    • 0025991016 scopus 로고
    • Manganese superoxide dismutase is induced by IFN-γ in multiple cell types: Synergistic induction by IFN-γ and tumor necrosis factor or IL-1
    • Harris CA, Derbin KS, Hunte-McDonough B, Krauss MR, Chen KT, Smith DN, et al. Manganese superoxide dismutase is induced by IFN-γ in multiple cell types: Synergistic induction by IFN-γ and tumor necrosis factor or IL-1. J Immunol 1991;147:149-54.
    • (1991) J Immunol , vol.147 , pp. 149-154
    • Harris, C.A.1    Derbin, K.S.2    Hunte-McDonough, B.3    Krauss, M.R.4    Chen, K.T.5    Smith, D.N.6
  • 44
    • 0025337812 scopus 로고
    • Regulation of manganese superoxide dismutase by lipopolysaccharidem interleukin-1, and tumor necrosis factor
    • Visner GA, Dougall WC, Wilson JM, Burr IA, Nick HS. Regulation of manganese superoxide dismutase by lipopolysaccharidem interleukin-1, and tumor necrosis factor. J Biol Chem 1990;265:2856-64.
    • (1990) J Biol Chem , vol.265 , pp. 2856-2864
    • Visner, G.A.1    Dougall, W.C.2    Wilson, J.M.3    Burr, I.A.4    Nick, H.S.5
  • 45
    • 0024997550 scopus 로고
    • Induction of superoxide dismutase in leukocytes by paraquat: Correlation with age, possible predictor of longevity
    • Niwa Y, Ishimoto K, Kanoh T. Induction of superoxide dismutase in leukocytes by paraquat: correlation with age, possible predictor of longevity. Blood 1990;76:835-41.
    • (1990) Blood , vol.76 , pp. 835-841
    • Niwa, Y.1    Ishimoto, K.2    Kanoh, T.3
  • 46
    • 0020455393 scopus 로고
    • Nucleotide sequence specificity of DNA cleavage by iron-bleomycin: Alteration on ethidium bromide-, actinomycin-, distamycin-intercalated
    • Sugiura Y, Suzuki T. Nucleotide sequence specificity of DNA cleavage by iron-bleomycin: alteration on ethidium bromide-, actinomycin-, distamycin-intercalated. J Biol Chem 1982;257:10544-6.
    • (1982) J Biol Chem , vol.257 , pp. 10544-10546
    • Sugiura, Y.1    Suzuki, T.2
  • 47
    • 0036704534 scopus 로고    scopus 로고
    • Interferon-alpha enhances biological defense activities against oxidative stress in cultured rat hepatocytes and hepatic stellate cells
    • Lu G, Shimizu I, Cui X, Itonaga M, Tamaki K, Fukuno H, et al. Interferon-alpha enhances biological defense activities against oxidative stress in cultured rat hepatocytes and hepatic stellate cells. J Med Invest 2002;49:172-81.
    • (2002) J Med Invest , vol.49 , pp. 172-181
    • Lu, G.1    Shimizu, I.2    Cui, X.3    Itonaga, M.4    Tamaki, K.5    Fukuno, H.6
  • 48
    • 0027407022 scopus 로고
    • Involvement of superoxide dismutase and glutathione peroxidase in attenuation of radiation-induced hyperthermia by interleukin-1 alpha in rats
    • Kandasamy SB, Kumar JS, Harris AH. Involvement of superoxide dismutase and glutathione peroxidase in attenuation of radiation-induced hyperthermia by interleukin-1 alpha in rats. Brain Res 1993;606:106-10.
    • (1993) Brain Res , vol.606 , pp. 106-110
    • Kandasamy, S.B.1    Kumar, J.S.2    Harris, A.H.3
  • 50
    • 0019961923 scopus 로고
    • Changes of glutathione, protein bound SH-groups concentrations in rat adrenals under acute and repeated stress
    • Sedlack J, L'Hanus. Changes of glutathione, protein bound SH-groups concentrations in rat adrenals under acute and repeated stress. Endocrinol Exp 1982;16:103-9.
    • (1982) Endocrinol Exp , vol.16 , pp. 103-109
    • Sedlack, J.1    L'Hanus2
  • 51
    • 0022116963 scopus 로고
    • Long-term effect of hypophysectomy on various fractions of sulfhydryl groups in thyroid, adrenal and some other organs in rats
    • Sedlack J. Long-term effect of hypophysectomy on various fractions of sulfhydryl groups in thyroid, adrenal and some other organs in rats. Endocrinol Exp 1985;19:186-92.
    • (1985) Endocrinol Exp , vol.19 , pp. 186-192
    • Sedlack, J.1
  • 52
    • 0036709597 scopus 로고    scopus 로고
    • Cellular glutathione and thiols metabolism
    • Dickinson DA, Forman HJ. Cellular glutathione and thiols metabolism. Biochem Pharmacol 2002;64:1019-26.
    • (2002) Biochem Pharmacol , vol.64 , pp. 1019-1026
    • Dickinson, D.A.1    Forman, H.J.2
  • 53
    • 0034190372 scopus 로고    scopus 로고
    • Regulation of redox glutathione levels, gene transcription in lung inflammation: Therapeutic approaches
    • Rahman I, MacNee W. Regulation of redox glutathione levels, gene transcription in lung inflammation: therapeutic approaches. Free Radic Biol Med 2000;28:1405-20.
    • (2000) Free Radic Biol Med , vol.28 , pp. 1405-1420
    • Rahman, I.1    MacNee, W.2
  • 54
    • 0026556492 scopus 로고
    • Endogenous glutathione levels modulate both constitutive, UVA radiation/hydrogen peroxide inducible expression of the human heme oxygenase gene
    • Lautier D, Luscher P, Tyrrell RM. Endogenous glutathione levels modulate both constitutive, UVA radiation/hydrogen peroxide inducible expression of the human heme oxygenase gene. Carcinogenesis 1992;13:227-32.
    • (1992) Carcinogenesis , vol.13 , pp. 227-232
    • Lautier, D.1    Luscher, P.2    Tyrrell, R.M.3
  • 55
    • 0029099878 scopus 로고
    • Bone marrow and splenic granulocyte-macrophage colony-stimulating factor and transforming growth factor-β mRNA levels in irradiated mice
    • Chang CM, Limanni A, Bakjer WH, Dobson ME, Kalinich JF, Jackson W, et al. Bone marrow and splenic granulocyte-macrophage colony-stimulating factor and transforming growth factor-β mRNA levels in irradiated mice. Blood 1995;86:2130-6.
    • (1995) Blood , vol.86 , pp. 2130-2136
    • Chang, C.M.1    Limanni, A.2    Bakjer, W.H.3    Dobson, M.E.4    Kalinich, J.F.5    Jackson, W.6
  • 56
    • 0034178260 scopus 로고    scopus 로고
    • TGF-β1 and radiation fibrosis: A master switch, a specific therapeutic target?
    • Martin M, Lefaix JL, Delanian S. TGF-β1 and radiation fibrosis: a master switch, a specific therapeutic target?. Int J Radiat Oncol Biol Phys 2000;47:277-90.
    • (2000) Int J Radiat Oncol Biol Phys , vol.47 , pp. 277-290
    • Martin, M.1    Lefaix, J.L.2    Delanian, S.3
  • 57
    • 0027315238 scopus 로고
    • Reversal of inhibition of reactive oxygen species on respiratory burst of macrophages by polysaccharide from Coriolus versicolor
    • Jun L, Mei Z, Yuan C. Reversal of inhibition of reactive oxygen species on respiratory burst of macrophages by polysaccharide from Coriolus versicolor. Int J Immunopharmacol 1993;15:429-33.
    • (1993) Int J Immunopharmacol , vol.15 , pp. 429-433
    • Jun, L.1    Mei, Z.2    Yuan, C.3
  • 58
    • 20444401603 scopus 로고    scopus 로고
    • The effect of polysaccharide krestin on GPx gene expression in macrophages
    • Pang ZJ, Chen Y, Zhou M. The effect of polysaccharide krestin on GPx gene expression in macrophages. Acta Biochim Biophys Sinica 1999;31:284-8.
    • (1999) Acta Biochim Biophys Sinica , vol.31 , pp. 284-288
    • Pang, Z.J.1    Chen, Y.2    Zhou, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.