메뉴 건너뛰기




Volumn 30, Issue 2, 1999, Pages 125-132

Analysis of the oxidative stress response of Penicillium chrysogenum to menadione

Author keywords

Glucose 6 phosphate dehydrogenase; Glutathione; Menadione; Oxidative stress; Penicillium chrysogenum; Superoxide dismutase

Indexed keywords

COPPER ZINC SUPEROXIDE DISMUTASE; GLUCOSE 6 PHOSPHATE DEHYDROGENASE; GLUTATHIONE DISULFIDE; GLUTATHIONE REDUCTASE; GLUTATHIONE TRANSFERASE; MANGANESE SUPEROXIDE DISMUTASE; MENADIONE; SUPEROXIDE;

EID: 0345561613     PISSN: 10715762     EISSN: None     Source Type: Journal    
DOI: 10.1080/10715769900300131     Document Type: Article
Times cited : (78)

References (47)
  • 1
    • 0031032498 scopus 로고    scopus 로고
    • A mechanism for production of hydroxyl radicals by the brown-rot fungus Coniophora puteana: Fe(III) reduction by cellobiose dehydrogenase and Fe(II) oxidation at a distance from the hyphae
    • S.M. Hyde and P.M. Wood (1997) A mechanism for production of hydroxyl radicals by the brown-rot fungus Coniophora puteana: Fe(III) reduction by cellobiose dehydrogenase and Fe(II) oxidation at a distance from the hyphae. Microbiology, 143, 259-266.
    • (1997) Microbiology , vol.143 , pp. 259-266
    • Hyde, S.M.1    Wood, P.M.2
  • 2
    • 0031985659 scopus 로고    scopus 로고
    • Manganese peroxidase-dependent oxidation of glyoxylic and oxalic acids synthesized by Ceriporiopsis subvermispora
    • U. Urzúa, P.J. Kersten and R. Vicuña (1998) Manganese peroxidase-dependent oxidation of glyoxylic and oxalic acids synthesized by Ceriporiopsis subvermispora. Applied and Environmental Microbiology, 64, 68-73.
    • (1998) Applied and Environmental Microbiology , vol.64 , pp. 68-73
    • Urzúa, U.1    Kersten, P.J.2    Vicuña, R.3
  • 3
    • 0025995442 scopus 로고
    • Mechanisms of natural resistance to human pathogenic fungi
    • J.W. Murphy (1991) Mechanisms of natural resistance to human pathogenic fungi. Annual Review of Microbiology, 45, 509-538.
    • (1991) Annual Review of Microbiology , vol.45 , pp. 509-538
    • Murphy, J.W.1
  • 4
    • 0028171293 scopus 로고
    • 2 from the oxidative burst orchestrates the plant hypersensitive disease resistance response
    • 2 from the oxidative burst orchestrates the plant hypersensitive disease resistance response. Cell, 79, 583-593.
    • (1994) Cell , vol.79 , pp. 583-593
    • Levine, A.1    Tenhaken, R.2    Dixonand, R.3    Lamb, C.J.4
  • 5
    • 0002941117 scopus 로고
    • Glucose transforming enzymes
    • eds. W. M. Fogarty and C. T. Kelly, Elsevier Applied Science, London
    • A. Crueger and W. Crueger (1990) Glucose transforming enzymes. In Micrabial Enzymes and Biotechnology (eds. W. M. Fogarty and C. T. Kelly), Elsevier Applied Science, London, pp.177-226.
    • (1990) Micrabial Enzymes and Biotechnology , pp. 177-226
    • Crueger, A.1    Crueger, W.2
  • 6
    • 0031279445 scopus 로고    scopus 로고
    • Influence of the dissolved oxygen concentration on the penicillin biosynthetic pathway in steady-state cultures of Penicillium chrysogenum
    • C.M. Henriksen, J. Nielsen and J. Villadsen (1997) Influence of the dissolved oxygen concentration on the penicillin biosynthetic pathway in steady-state cultures of Penicillium chrysogenum. Biotechnology Progress, 13, 776-782.
    • (1997) Biotechnology Progress , vol.13 , pp. 776-782
    • Henriksen, C.M.1    Nielsen, J.2    Villadsen, J.3
  • 7
    • 0030750021 scopus 로고    scopus 로고
    • Phenoxyacetic acid induces glutathione-dependent detoxification and depletes the glutathione pool in Penicillium chrysogenum
    • T. Emri, I. Pócsi and A. Szentirmai (1997) Phenoxyacetic acid induces glutathione-dependent detoxification and depletes the glutathione pool in Penicillium chrysogenum. Journal of Basic Microbiology, 37, 181-186.
    • (1997) Journal of Basic Microbiology , vol.37 , pp. 181-186
    • Emri, T.1    Pócsi, I.2    Szentirmai, A.3
  • 8
    • 0002588423 scopus 로고
    • The effect of oxidative stress on Saccharomyces cerevisiae
    • D.J. Jamieson (1995) The effect of oxidative stress on Saccharomyces cerevisiae. Redox Report, 1, 89-95.
    • (1995) Redox Report , vol.1 , pp. 89-95
    • Jamieson, D.J.1
  • 9
    • 0029619396 scopus 로고
    • Adaptive response of Schizosaccharomyces pombe to hydrogen peroxide and menadione
    • J. Lee, I.W. Dawes and J.-H. Roe (1995) Adaptive response of Schizosaccharomyces pombe to hydrogen peroxide and menadione. Microbiology, 141, 3127-3132.
    • (1995) Microbiology , vol.141 , pp. 3127-3132
    • Lee, J.1    Dawes, I.W.2    Roe, J.-H.3
  • 10
    • 0029885872 scopus 로고    scopus 로고
    • Analysis of the adaptive oxidative stress response of Candida albicans
    • D.J. Jamieson, D.W.S. Stephen and E.C. Terrière (1996) Analysis of the adaptive oxidative stress response of Candida albicans. FEMS Microbiology Letters, 138, 83-88.
    • (1996) FEMS Microbiology Letters , vol.138 , pp. 83-88
    • Jamieson, D.J.1    Stephen, D.W.S.2    Terrière, E.C.3
  • 12
    • 0030878151 scopus 로고    scopus 로고
    • Glutathione metabolism and protection against oxidative stress caused by peroxides in Penicillium chrysogenum
    • T. Emri, I. Pócsi and A. Szentirmai (1997) Glutathione metabolism and protection against oxidative stress caused by peroxides in Penicillium chrysogenum. Free Radical Biology and Medicine, 23, 809-814.
    • (1997) Free Radical Biology and Medicine , vol.23 , pp. 809-814
    • Emri, T.1    Pócsi, I.2    Szentirmai, A.3
  • 13
    • 0028223899 scopus 로고
    • Regulation of specific activity of glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase in Penicillium chrysogenum
    • T. Emri, G. Bartók, and A. Szentirmai (1994) Regulation of specific activity of glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase in Penicillium chrysogenum. FEMS Microbiology Letters, 117, 67-70.
    • (1994) FEMS Microbiology Letters , vol.117 , pp. 67-70
    • Emri, T.1    Bartók, G.2    Szentirmai, A.3
  • 14
    • 2642595054 scopus 로고    scopus 로고
    • Changes in the glutathione (GSH) metabolism of Penicillium chrysogenum grown on different nitrogen sulphur and carbon sources
    • T. Emri, I. Pócsi and A. Szentirmai (1998) Changes in the glutathione (GSH) metabolism of Penicillium chrysogenum grown on different nitrogen sulphur and carbon sources. Journal of Basic Microbiology, 38, 3-8.
    • (1998) Journal of Basic Microbiology , vol.38 , pp. 3-8
    • Emri, T.1    Pócsi, I.2    Szentirmai, A.3
  • 15
    • 0021316160 scopus 로고
    • Glutathione metabolism in yeast Saccharomyces cerevisiae. Evidence that γ-glutamyltranspeptidase is a vacuolar enzyme
    • C.J. Jaspers and M.J. Penninckx (1984) Glutathione metabolism in yeast Saccharomyces cerevisiae. Evidence that γ-glutamyltranspeptidase is a vacuolar enzyme. Biochimie, 66, 71-74.
    • (1984) Biochimie , vol.66 , pp. 71-74
    • Jaspers, C.J.1    Penninckx, M.J.2
  • 16
    • 0030859939 scopus 로고    scopus 로고
    • An important role for glutathione and γ-glutamyltranspeptidase in the supply of growth requirements during nitrogen starvation of the yeast Saccharomyces cerevisiae
    • K. Mehdi and M.J. Penninckx (1997) An important role for glutathione and γ-glutamyltranspeptidase in the supply of growth requirements during nitrogen starvation of the yeast Saccharomyces cerevisiae. Microbiology, 143, 1885-1889.
    • (1997) Microbiology , vol.143 , pp. 1885-1889
    • Mehdi, K.1    Penninckx, M.J.2
  • 17
    • 0031052694 scopus 로고    scopus 로고
    • Aging of Penicillium chrysogenum cultures under carbon starvation: I: Morphological changes and secondary metabolite production
    • T. Pusztahelyi, I. Pócsi, J. Kozma and A. Szentirmai (1997) Aging of Penicillium chrysogenum cultures under carbon starvation: I: morphological changes and secondary metabolite production. Biotechnology and Applied Biochemistry, 25, 81-86.
    • (1997) Biotechnology and Applied Biochemistry , vol.25 , pp. 81-86
    • Pusztahelyi, T.1    Pócsi, I.2    Kozma, J.3    Szentirmai, A.4
  • 18
    • 0031044452 scopus 로고    scopus 로고
    • Aging of Penicillium chrysogenum cultures under carbon starvation: II: Protease and N-acetyl-β-D-hexosaminidase production
    • T. Pusztahelyi, I. Pócsi and A. Szentirmai (1997) Aging of Penicillium chrysogenum cultures under carbon starvation: II: protease and N-acetyl-β-D-hexosaminidase production. Biotechnology and Applied Biochemistry, 25, 87-93.
    • (1997) Biotechnology and Applied Biochemistry , vol.25 , pp. 87-93
    • Pusztahelyi, T.1    Pócsi, I.2    Szentirmai, A.3
  • 19
    • 0017151033 scopus 로고
    • Purification and properties of rat lung soluble glutathione peroxidase
    • D.T.Y. Chiu, F.H. Stults and A.L. Tappel (1976) Purification and properties of rat lung soluble glutathione peroxidase. Biochimica et Biophysica Acta, 445, 558-566.
    • (1976) Biochimica et Biophysica Acta , vol.445 , pp. 558-566
    • Chiu, D.T.Y.1    Stults, F.H.2    Tappel, A.L.3
  • 20
    • 0021307110 scopus 로고
    • Reversible inactivation of Saccharomyces cerevisiae glutathione reductase under reducing conditions
    • M.C. Pinto, A.M. Mata and J. López-Barea (1984) Reversible inactivation of Saccharomyces cerevisiae glutathione reductase under reducing conditions. Archives of Biochemistry and Biophysics, 228, 1-12.
    • (1984) Archives of Biochemistry and Biophysics , vol.228 , pp. 1-12
    • Pinto, M.C.1    Mata, A.M.2    López-Barea, J.3
  • 22
    • 0016170267 scopus 로고
    • Microbial assimilation of methanol. Induction and function of catalase in Candida boidinii
    • R. Roggenkamp, H. Sahm and F. Wagner (1974) Microbial assimilation of methanol. Induction and function of catalase in Candida boidinii. FEBS Letters, 41, 283-286.
    • (1974) FEBS Letters , vol.41 , pp. 283-286
    • Roggenkamp, R.1    Sahm, H.2    Wagner, F.3
  • 24
    • 0021288861 scopus 로고
    • Assay of superoxide dismutase activity in tumour tissue
    • L.W. Oberley and D.R. Spitz (1984) Assay of superoxide dismutase activity in tumour tissue. Methods in Enzymology, 105, 457-464.
    • (1984) Methods in Enzymology , vol.105 , pp. 457-464
    • Oberley, L.W.1    Spitz, D.R.2
  • 25
    • 0022272493 scopus 로고
    • Determination of glutathione and glutathione disulphide in biological samples
    • M.E. Anderson (1985) Determination of glutathione and glutathione disulphide in biological samples. Methods in Enzymology, 113, 548-555.
    • (1985) Methods in Enzymology , vol.113 , pp. 548-555
    • Anderson, M.E.1
  • 27
    • 0028369668 scopus 로고
    • Intracellular hydrogen peroxide and superoxide anion detection in endothelial cells
    • W.O. Carter, P.K. Narayanan and J.P. Robinson (1994) Intracellular hydrogen peroxide and superoxide anion detection in endothelial cells. Journal of Leukocyte Biology, 55, 253-258.
    • (1994) Journal of Leukocyte Biology , vol.55 , pp. 253-258
    • Carter, W.O.1    Narayanan, P.K.2    Robinson, J.P.3
  • 28
    • 0020669405 scopus 로고
    • Determination of total protein
    • G.L. Peterson (1983) Determination of total protein. Methods in Enzymology, 91, 86-105.
    • (1983) Methods in Enzymology , vol.91 , pp. 86-105
    • Peterson, G.L.1
  • 30
    • 0027483385 scopus 로고
    • Saccharomyces cerevisiae has an inducible response to menadione which differs from that to hydrogen peroxide
    • J. Flattery-O'Brien, L.P. Collinson and I.W. Dawes (1993) Saccharomyces cerevisiae has an inducible response to menadione which differs from that to hydrogen peroxide. Journal of General Microbiology, 139, 501-507.
    • (1993) Journal of General Microbiology , vol.139 , pp. 501-507
    • Flattery-O'brien, J.1    Collinson, L.P.2    Dawes, I.W.3
  • 31
    • 0022336892 scopus 로고
    • Biosynthesis of superoxide dismutase in Saccharomyces cerevisiae: Effect of paraquat and copper
    • F.J. Lee and H.M. Hassan (1985) Biosynthesis of superoxide dismutase in Saccharomyces cerevisiae: effect of paraquat and copper. Journal of Free Radicals in Biology and Medicine, 1, 319-325.
    • (1985) Journal of Free Radicals in Biology and Medicine , vol.1 , pp. 319-325
    • Lee, F.J.1    Hassan, H.M.2
  • 32
    • 0003791735 scopus 로고
    • Evolution and biological roles of fungal superoxide dismutases
    • eds. G. Winkelmann and D.R. Winge, Marcel Dekker, New York
    • D.O. Natvig, W.H. Dvorachek, Jr. and K. Sylvester (1994) Evolution and biological roles of fungal superoxide dismutases. In Metal Ions in Fungi (eds. G. Winkelmann and D.R. Winge), Marcel Dekker, New York, pp. 391-412.
    • (1994) Metal Ions in Fungi , pp. 391-412
    • Natvig, D.O.1    Dvorachek W.H., Jr.2    Sylvester, K.3
  • 33
    • 0028597439 scopus 로고
    • Analysis of Saccharomyces cerevisiae proteins induced by peroxide and superoxide stress
    • D.J. Jamieson, S.L. Rivers and D.W.S. Stephen (1994) Analysis of Saccharomyces cerevisiae proteins induced by peroxide and superoxide stress. Microbiology, 140, 3277-3283.
    • (1994) Microbiology , vol.140 , pp. 3277-3283
    • Jamieson, D.J.1    Rivers, S.L.2    Stephen, D.W.S.3
  • 34
    • 0038631349 scopus 로고
    • Superoxide dismutases in Saccharomyces cerevisiae
    • eds. G. Winkelmann and D. R. Winge, Marcel Dekker, New York
    • F. Galiazzo, M.T. Carrì, M.R. Ciriolo and G. Rotilio (1994) Superoxide dismutases in Saccharomyces cerevisiae. In Metal Ions in Fungi (eds. G. Winkelmann and D. R. Winge), Marcel Dekker, New York, pp. 361-390.
    • (1994) Metal Ions in Fungi , pp. 361-390
    • Galiazzo, F.1    Carrì, M.T.2    Ciriolo, M.R.3    Rotilio, G.4
  • 36
    • 0030004354 scopus 로고    scopus 로고
    • Glutathione is an essential metabolite required for resistance to oxidative stress in the yeast Saccharomyces cerevisiae
    • C.M. Grant, F.H. MacIver and I.W. Dawes (1996) Glutathione is an essential metabolite required for resistance to oxidative stress in the yeast Saccharomyces cerevisiae. Current Genetics, 29, 511-515.
    • (1996) Current Genetics , vol.29 , pp. 511-515
    • Grant, C.M.1    MacIver, F.H.2    Dawes, I.W.3
  • 37
    • 0030222083 scopus 로고    scopus 로고
    • Glutathioneis an important antioxidant molecule in the yeast Saccharomyces cerevisiae
    • D.W.S. Stephen and D.J. Jamieson (1996) Glutathioneis an important antioxidant molecule in the yeast Saccharomyces cerevisiae. FEMS Microbiology Letters, 141, 207-212.
    • (1996) FEMS Microbiology Letters , vol.141 , pp. 207-212
    • Stephen, D.W.S.1    Jamieson, D.J.2
  • 38
    • 0030220855 scopus 로고    scopus 로고
    • Menadione causes increases in the level of glutathione and in the activity of γ-glutamylcysteine synthetase in cultured Chinese hamster V79 cells
    • T. Ochi (1996) Menadione causes increases in the level of glutathione and in the activity of γ-glutamylcysteine synthetase in cultured Chinese hamster V79 cells. Toxicology, 112, 45-55.
    • (1996) Toxicology , vol.112 , pp. 45-55
    • Ochi, T.1
  • 39
    • 0344516544 scopus 로고    scopus 로고
    • Transport of glutathione S-conjugates in the yeasts Saccharomyces cerevisiae
    • R. Ża̧dziński, J. Maszewski and G. Bartosz (1996) Transport of glutathione S-conjugates in the yeasts Saccharomyces cerevisiae. Cell Biology International, 20, 325-330.
    • (1996) Cell Biology International , vol.20 , pp. 325-330
    • Za̧dziński, R.1    Maszewski, J.2    Bartosz, G.3
  • 40
    • 0031034766 scopus 로고    scopus 로고
    • Amino acid-dependent regulation of the Saccharomyces cerevisiae GSH1 gene by hydrogen peroxide
    • D.W.S. Stephen and D.J. Jamieson (1997) Amino acid-dependent regulation of the Saccharomyces cerevisiae GSH1 gene by hydrogen peroxide. Molecular Microbiology, 23, 203-210.
    • (1997) Molecular Microbiology , vol.23 , pp. 203-210
    • Stephen, D.W.S.1    Jamieson, D.J.2
  • 42
    • 0028331325 scopus 로고
    • Utilization of side-chain precursors for penicillin biosynthesis in a high-producing strain of Penicillium chrysogenum
    • S.H. Eriksen, B. Jensen, I. Schneider, S. Kaasgaard and J. Olsen (1994) Utilization of side-chain precursors for penicillin biosynthesis in a high-producing strain of Penicillium chrysogenum. Applied Microbiology and Biotechnology, 40, 883-887.
    • (1994) Applied Microbiology and Biotechnology , vol.40 , pp. 883-887
    • Eriksen, S.H.1    Jensen, B.2    Schneider, I.3    Kaasgaard, S.4    Olsen, J.5
  • 44
    • 0021918078 scopus 로고
    • Isopenicillin N synthetase of Penicillium chrysogenum, an enzyme that converts δ-(L-α-aminoadipyl)-L-cysteinyl-D -valine to isopenicillin N
    • F.R. Ramos, M.J. López-Nieto and J.F. Martin (1985) Isopenicillin N synthetase of Penicillium chrysogenum, an enzyme that converts δ-(L-α-aminoadipyl)-L-cysteinyl-D -valine to isopenicillin N. Antimicrobial Agents and Chemotherapy, 27, 380-387.
    • (1985) Antimicrobial Agents and Chemotherapy , vol.27 , pp. 380-387
    • Ramos, F.R.1    López-Nieto, M.J.2    Martin, J.F.3
  • 45
    • 0002012473 scopus 로고
    • Nitrogen regulation of penicillin and cephalosporin fermentations
    • ed. S. Sanchez-Esquivel, CRC Press, Boca Raton
    • S. Sanchez, M.E. Flores and A.L. Demain (1988) Nitrogen regulation of penicillin and cephalosporin fermentations. In Nitrogen Source Control of Microbial Processes (ed. S. Sanchez-Esquivel), CRC Press, Boca Raton, pp. 121-136.
    • (1988) Nitrogen Source Control of Microbial Processes , pp. 121-136
    • Sanchez, S.1    Flores, M.E.2    Demain, A.L.3
  • 46
    • 0028009523 scopus 로고
    • The thioredoxin system of Penicillium chrysogenum and its possible role in penicillin biosynthesis
    • G. Cohen, A. Argaman, R. Schreiber, M. Mislovati and Y. Aharonowitz (1994) The thioredoxin system of Penicillium chrysogenum and its possible role in penicillin biosynthesis. Journal of Bacteriology, 176, 973-984.
    • (1994) Journal of Bacteriology , vol.176 , pp. 973-984
    • Cohen, G.1    Argaman, A.2    Schreiber, R.3    Mislovati, M.4    Aharonowitz, Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.