메뉴 건너뛰기




Volumn 189, Issue 2, 2008, Pages 121-130

Unusual location and characterization of Cu/Zn-containing superoxide dismutase from filamentous fungus Humicola lutea

Author keywords

Cu Zn superoxide dismutase; Enzyme glycosylation; Intracellular location; Mitochondrial intermembrane space; Protein sequencing

Indexed keywords

BIOLOGICAL MARKER; CARBOHYDRATE; COPPER ZINC SUPEROXIDE DISMUTASE; HYDROGEN PEROXIDE; POTASSIUM CYANIDE;

EID: 38049100479     PISSN: 03028933     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00203-007-0300-3     Document Type: Article
Times cited : (15)

References (54)
  • 2
    • 0344927978 scopus 로고    scopus 로고
    • Alteration of antioxidant enzyme gene expression during cold acclimation of near isogenic wheat lines
    • Baek K, Skinner DZ (2003) Alteration of antioxidant enzyme gene expression during cold acclimation of near isogenic wheat lines. Plant Sci 165:1221-1227
    • (2003) Plant Sci , vol.165 , pp. 1221-1227
    • Baek, K.1    Skinner, D.Z.2
  • 3
    • 0015153416 scopus 로고
    • Superoxide dismutase: Improved assay and an assay applicable to polyacrylamide gels
    • Beauchamp C, Fridovich I (1971) Superoxide dismutase: Improved assay and an assay applicable to polyacrylamide gels. Anal Biochem 44:276-287
    • (1971) Anal Biochem , vol.44 , pp. 276-287
    • Beauchamp, C.1    Fridovich, I.2
  • 4
    • 0001422064 scopus 로고
    • Glucose-6-phosphate dehydrogenase
    • 3rd edn vol III Verlag Chemie Weinheim
    • Bergmeyer HU, Moellering H (1983) Glucose-6-phosphate dehydrogenase. In: Moss DW (ed) Methods of enzymatic analysis, 3rd edn, vol III. Verlag Chemie, Weinheim, pp 191-197
    • (1983) Methods of Enzymatic Analysis , pp. 191-197
    • Bergmeyer, H.U.1    Moellering, H.2    Moss, D.W.3
  • 6
    • 0017348934 scopus 로고
    • Mitochondrial production of superoxide radical and hydrogen peroxide
    • Boveris A (1977) Mitochondrial production of superoxide radical and hydrogen peroxide. Adv Exp Med Biol 78:67-82
    • (1977) Adv Exp Med Biol , vol.78 , pp. 67-82
    • Boveris, A.1
  • 7
    • 0041825657 scopus 로고    scopus 로고
    • Replacement of a cytosolic copper/zinc superoxide dismutase by a novel cytosolic manganese superoxide dismutase in crustaceans that use copper (haemocyanin) for oxygen transport
    • Brouwer M, Hoexum-Brouwer T, Grater W, Brown-Peterson N (2003) Replacement of a cytosolic copper/zinc superoxide dismutase by a novel cytosolic manganese superoxide dismutase in crustaceans that use copper (haemocyanin) for oxygen transport. Biochem J 374:219-228
    • (2003) Biochem J , vol.374 , pp. 219-228
    • Brouwer, M.1    Hoexum-Brouwer, T.2    Grater, W.3    Brown-Peterson, N.4
  • 8
    • 0025195232 scopus 로고
    • 2-dependent methionine auxotrophy in Cu,Zn superoxide dismutase-deficient mutants of Saccharomyces cerevisiae
    • 2-dependent methionine auxotrophy in Cu,Zn superoxide dismutase-deficient mutants of Saccharomyces cerevisiae. J Bacteriol 172:1840-1845
    • (1990) J Bacteriol , vol.172 , pp. 1840-1845
    • Chang, E.1    Kosman, D.2
  • 9
    • 0024227428 scopus 로고
    • Molecular immunochemistry of the Cu,Zn superoxide dismutase in rat hepatocytes
    • Chang L-Y, Slot JW, Geuze HJ, Crapo JD (1988) Molecular immunochemistry of the Cu,Zn superoxide dismutase in rat hepatocytes. J Cell Biol 107:2169-2179
    • (1988) J Cell Biol , vol.107 , pp. 2169-2179
    • Chang, L.-Y.1    Slot, J.W.2    Geuze, H.J.3    Crapo, J.D.4
  • 10
    • 0025165393 scopus 로고
    • Structure, exon pattern, and chromosome mapping of the gene for cytosolic copper-zinc superoxide dismutase (sod-1) from Neurospora crassa
    • Chary P, Hallewell RA, Natvig DO (1990) Structure, exon pattern, and chromosome mapping of the gene for cytosolic copper-zinc superoxide dismutase (sod-1) from Neurospora crassa. J Biol Chem 265:18961-18967
    • (1990) J Biol Chem , vol.265 , pp. 18961-18967
    • Chary, P.1    Hallewell, R.A.2    Natvig, D.O.3
  • 11
    • 33644798462 scopus 로고    scopus 로고
    • A copper chaperone for superoxide dismutase that confers three types of copper/zinc superoxide dismutase activity in Arabidopsis
    • Chu CC, Lee WC, Guo WY, Pan SM, Chen LJ, Li HM, Jinn TL (2005) A copper chaperone for superoxide dismutase that confers three types of copper/zinc superoxide dismutase activity in Arabidopsis. Plant Physiol 139:425-436
    • (2005) Plant Physiol , vol.139 , pp. 425-436
    • Chu, C.C.1    Lee, W.C.2    Guo, W.Y.3    Pan, S.M.4    Chen, L.J.5    Li, H.M.6    Jinn, T.L.7
  • 12
    • 0015239046 scopus 로고
    • Hepatic sulfite oxidase. Purification and properties
    • Cohen HJ, Fridovich I (1971) Hepatic sulfite oxidase. Purification and properties. J Biol Chem 246:359-366
    • (1971) J Biol Chem , vol.246 , pp. 359-366
    • Cohen, H.J.1    Fridovich, I.2
  • 13
    • 0026476480 scopus 로고
    • Copper, zinc superoxide dismutase is primarily a cytosolic protein in human cells
    • Crapo JD, Oury TD, Rabouille C, Slot JW, Chang L (1992) Copper, zinc superoxide dismutase is primarily a cytosolic protein in human cells. Proc Natl Acad Sci USA 89:10405-10409
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10405-10409
    • Crapo, J.D.1    Oury, T.D.2    Rabouille, C.3    Slot, J.W.4    Chang, L.5
  • 17
    • 0041344579 scopus 로고    scopus 로고
    • Factors controlling the uptake of yeast copper/zinc superoxide dismutase into mitochondria
    • Field LS, Furukawa Y, O'Halloran TV, Culotta VC (2003) Factors controlling the uptake of yeast copper/zinc superoxide dismutase into mitochondria. J Biol Chem 278:28052-28059
    • (2003) J Biol Chem , vol.278 , pp. 28052-28059
    • Field, L.S.1    Furukawa, Y.2    O'Halloran, T.V.3    Culotta, V.C.4
  • 20
    • 0012908373 scopus 로고
    • Measuring the activity of superoxide dismutases: An embarrassment of riches
    • CRC Boca Baton
    • Fridovich I (1982) Measuring the activity of superoxide dismutases: an embarrassment of riches. In: Oberly LW (ed) Superoxide dismutase, vol 1. CRC, Boca Baton, pp 69-77
    • (1982) Superoxide Dismutase Vol 1 , pp. 69-77
    • Fridovich, I.1    Oberly, L.W.2
  • 21
    • 0020644952 scopus 로고
    • Superoxide radical: An endogenous toxicant
    • Fridovich I (1983) Superoxide radical: an endogenous toxicant. Ann Rev Pharmacol Toxicol 23:239-257
    • (1983) Ann Rev Pharmacol Toxicol , vol.23 , pp. 239-257
    • Fridovich, I.1
  • 22
    • 0029053451 scopus 로고
    • Superoxide radical and superoxide dismutases
    • Fridovich I (1995) Superoxide radical and superoxide dismutases. Annu Rev Biochem 64:97-112
    • (1995) Annu Rev Biochem , vol.64 , pp. 97-112
    • Fridovich, I.1
  • 23
    • 0019907606 scopus 로고
    • Rat liver Cu,Zn-superoxide dismutase. Subcellular location in lysosomes
    • Geller BL, Winge DR (1982) Rat liver Cu,Zn-superoxide dismutase. Subcellular location in lysosomes. J Biol Chem 257:8945-8952
    • (1982) J Biol Chem , vol.257 , pp. 8945-8952
    • Geller, B.L.1    Winge, D.R.2
  • 24
    • 0028068186 scopus 로고
    • Free radicals, anti-oxidants, and human disease: Curiosity, cause, or consequence?
    • Halliwell B (1994) Free radicals, anti-oxidants, and human disease: curiosity, cause, or consequence? Lancet 344:721-724
    • (1994) Lancet , vol.344 , pp. 721-724
    • Halliwell, B.1
  • 25
    • 0019017560 scopus 로고
    • Intracellular localization, isolation and characterization of two distinct varieties of superoxide dismutase from Neurospora crassa
    • Henry LEA, Cammack R, Schwitzguebel JP, Palmert JM, Hall D (1980) Intracellular localization, isolation and characterization of two distinct varieties of superoxide dismutase from Neurospora crassa. Biochem J 187:321-328
    • (1980) Biochem J , vol.187 , pp. 321-328
    • Henry, L.E.A.1    Cammack, R.2    Schwitzguebel, J.P.3    Palmert, J.M.4    Hall, D.5
  • 26
    • 0028121255 scopus 로고
    • Salt stress-induced changes in superoxide dismutase isozymes in leaves and mesophyll protoplasts from Vigna unguiculata (L.) Walp
    • Hernandez JA, del Rio LA, Sevillap F (1994) Salt stress-induced changes in superoxide dismutase isozymes in leaves and mesophyll protoplasts from Vigna unguiculata (L.) Walp. New Phytol 126:37-44
    • (1994) New Phytol , vol.126 , pp. 37-44
    • Hernandez, J.A.1    Del Rio, L.A.2    Sevillap, F.3
  • 27
    • 12744277871 scopus 로고    scopus 로고
    • Evolutionary and mechanistic theories of aging
    • Hughes KA, Reynolds RM (2005) Evolutionary and mechanistic theories of aging. Annu Rev Entomol 50:421-445
    • (2005) Annu Rev Entomol , vol.50 , pp. 421-445
    • Hughes, K.A.1    Reynolds, R.M.2
  • 29
    • 19344364055 scopus 로고    scopus 로고
    • MnSOD in mouse heart: Acute responses to ischemic preconditioning and ischemia-reperfusion injury
    • Jin ZQ, Zhou HZ, Cecchini G, Gray MO, Karliner JS (2005) MnSOD in mouse heart: acute responses to ischemic preconditioning and ischemia-reperfusion injury. Am J Physiol Heart Circ Physiol 288:2986-2994
    • (2005) Am J Physiol Heart Circ Physiol , vol.288 , pp. 2986-2994
    • Jin, Z.Q.1    Zhou, H.Z.2    Cecchini, G.3    Gray, M.O.4    Karliner, J.S.5
  • 30
    • 0025915727 scopus 로고
    • Cu,Zn superoxide dismutase is a peroxisomal enzyme in human fibroblast and hepatoma cells
    • Keller GA, Warner TG, Steimer KS, Hallewel RA (1991) Cu,Zn superoxide dismutase is a peroxisomal enzyme in human fibroblast and hepatoma cells. Proc Natl Acad Sci USA 88:7381-7385
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 7381-7385
    • Keller, G.A.1    Warner, T.G.2    Steimer, K.S.3    Hallewel, R.A.4
  • 31
    • 77957002874 scopus 로고
    • Isocitric dehydrogenase
    • Kornberg A (1955) Isocitric dehydrogenase. Meth Enzymol 1:707-708
    • (1955) Meth Enzymol , vol.1 , pp. 707-708
    • Kornberg, A.1
  • 34
    • 0035941352 scopus 로고    scopus 로고
    • Candida albicans express an usual cytoplasmic manganese-containing superoxide dismutase (SOD3 gene product) upon the entry and during the stationary phase
    • Lamarre C, LeMay J-D, Deslauriers N, Bourbonnais Y (2001) Candida albicans express an usual cytoplasmic manganese-containing superoxide dismutase (SOD3 gene product) upon the entry and during the stationary phase. J Biol Chem 276:43784-43791
    • (2001) J Biol Chem , vol.276 , pp. 43784-43791
    • Lamarre, C.1    Lemay, J.-D.2    Deslauriers, N.3    Bourbonnais, Y.4
  • 35
    • 0018400899 scopus 로고
    • Preparation and analysis of mitochondrial ribosomes
    • Lambowitz AM (1979) Preparation and analysis of mitochondrial ribosomes. Meth Enzymol 59:421-433
    • (1979) Meth Enzymol , vol.59 , pp. 421-433
    • Lambowitz, A.M.1
  • 37
    • 0014691242 scopus 로고
    • Superoxide dismutase. An enzymic function for erythrocuprein (haemocuprein)
    • McCord JM, Fridovich I (1969) Superoxide dismutase. An enzymic function for erythrocuprein (haemocuprein). J Biol Chem 244:6049-6055
    • (1969) J Biol Chem , vol.244 , pp. 6049-6055
    • McCord, J.M.1    Fridovich, I.2
  • 38
    • 0017643072 scopus 로고
    • Purification and properties of superoxide dismutase from red alga, Porphyridium cruentum
    • Misra HP, Fridovich I (1977) Purification and properties of superoxide dismutase from red alga, Porphyridium cruentum. J Biol Chem 252:6421-6423
    • (1977) J Biol Chem , vol.252 , pp. 6421-6423
    • Misra, H.P.1    Fridovich, I.2
  • 40
    • 0035914342 scopus 로고    scopus 로고
    • Subcellular distribution of superoxide dismutases in rat liver: Cu/Zn-SOD in mitochondria
    • Okado-Matsumoto A, Fridovich I (2001) Subcellular distribution of superoxide dismutases in rat liver: Cu/Zn-SOD in mitochondria. J Biol Chem 276:38388-38393
    • (2001) J Biol Chem , vol.276 , pp. 38388-38393
    • Okado-Matsumoto, A.1    Fridovich, I.2
  • 41
    • 0000563992 scopus 로고
    • Localization of superoxide dismutase in glyoxysomes from Citrullus vulgaris. Functional implications in cellular metabolism
    • Sandalio LM, Del Rio LA (1987) Localization of superoxide dismutase in glyoxysomes from Citrullus vulgaris. Functional implications in cellular metabolism. J Plant Physiol 127:395-409
    • (1987) J Plant Physiol , vol.127 , pp. 395-409
    • Sandalio, L.M.1    Del Rio, L.A.2
  • 42
    • 0024994885 scopus 로고
    • Response of plant antioxidant defence genes to environmental stress
    • Scandalios JG (1990) Response of plant antioxidant defence genes to environmental stress. Adv Genet 27:1-41
    • (1990) Adv Genet , vol.27 , pp. 1-41
    • Scandalios, J.G.1
  • 43
    • 0004785633 scopus 로고
    • The effect of aeration on the activity of alcohol oxidase and enzymes utilising hydrogen peroxide in the course of Candida maltosa growth on paraffin
    • Shilova NK, Matyashova RN, Ilchenko AP (1989) The effect of aeration on the activity of alcohol oxidase and enzymes utilising hydrogen peroxide in the course of Candida maltosa growth on paraffin. Microbiologiya (Moskow) 58:430-435
    • (1989) Microbiologiya (Moskow) , vol.58 , pp. 430-435
    • Shilova, N.K.1    Matyashova, R.N.2    Ilchenko, A.P.3
  • 44
    • 0029828902 scopus 로고    scopus 로고
    • The yeast copper/zinc superoxide dismutase and the pentose phosphate pathway play overlapping roles in oxidative stress protection
    • Slekar KH, Kosman D, Culotta VC (1996) The yeast copper/zinc superoxide dismutase and the pentose phosphate pathway play overlapping roles in oxidative stress protection. J Biol Chem 271:28831-28836
    • (1996) J Biol Chem , vol.271 , pp. 28831-28836
    • Slekar, K.H.1    Kosman, D.2    Culotta, V.C.3
  • 47
    • 0035851122 scopus 로고    scopus 로고
    • A fraction of yeast Cu,Zn-superoxide dismutase and its metallochaperone, CCS, localize to the intermembrane space of mitochondria. a physiological role for SOD1 in guarding against mitochondrial oxidative damage
    • Sturtz LA, Diekert K, Jensen LT, Lill R, Culotta VC (2001) A fraction of yeast Cu,Zn-superoxide dismutase and its metallochaperone, CCS, localize to the intermembrane space of mitochondria. A physiological role for SOD1 in guarding against mitochondrial oxidative damage. J Biol Chem 276:38084-38089
    • (2001) J Biol Chem , vol.276 , pp. 38084-38089
    • Sturtz, L.A.1    Diekert, K.2    Jensen, L.T.3    Lill, R.4    Culotta, V.C.5
  • 48
    • 0023607878 scopus 로고
    • Expresion of human extracellular supeoxide dismutase in Chinese hamster ovary cells and characterization of the product
    • Tibell L, Hjalmarsson K, Edlund T, Skogman G, Engström E (1987) Expresion of human extracellular supeoxide dismutase in Chinese hamster ovary cells and characterization of the product. Biochemistry 84:6634-6638
    • (1987) Biochemistry , vol.84 , pp. 6634-6638
    • Tibell, L.1    Hjalmarsson, K.2    Edlund, T.3    Skogman, G.4    Engström, E.5
  • 49
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H, Staehelin T, Gordon G (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci USA 76:4350-4354
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, G.3
  • 51
    • 31344476584 scopus 로고    scopus 로고
    • Effect of nutrition factors on the synthesis of superoxide dismutase, catalase, and membrane lipid peroxide levels in Cordyceps militaris mycelium
    • Wang ZS, Gu YX, Yuan QS (2006) Effect of nutrition factors on the synthesis of superoxide dismutase, catalase, and membrane lipid peroxide levels in Cordyceps militaris mycelium. Curr Microbiol 52:74-79
    • (2006) Curr Microbiol , vol.52 , pp. 74-79
    • Wang, Z.S.1    Gu, Y.X.2    Yuan, Q.S.3
  • 52
    • 0037423865 scopus 로고    scopus 로고
    • Gene transfer of extracellular superoxide dismutase reduces arterial press in spontaneously hypertensive rats: Role of heparin-binding domain
    • Watanabe Y, Faraci FM, Heistad DD, Chu Y, Iida Sh, Lund DD, Weiss RM, DiBona GF (2003) Gene transfer of extracellular superoxide dismutase reduces arterial press in spontaneously hypertensive rats: role of heparin-binding domain. Circ Res 92:461-468
    • (2003) Circ Res , vol.92 , pp. 461-468
    • Watanabe, Y.1    Faraci, F.M.2    Heistad, D.D.3    Chu, Y.4    Sh, I.5    Lund, D.D.6    Weiss, R.M.7    Dibona, G.F.8
  • 53
    • 0015848173 scopus 로고
    • Superoxide dismutase: Organelle specificity
    • Weisinger RA, Fridovich I (1973) Superoxide dismutase: organelle specificity. J Biol Chem 248:3582-3592
    • (1973) J Biol Chem , vol.248 , pp. 3582-3592
    • Weisinger, R.A.1    Fridovich, I.2
  • 54
    • 0033584947 scopus 로고    scopus 로고
    • Isolation of a germin-like protein with manganese superoxide dismutase activity from cells of a moss, Barbula unguiculata.
    • Yamahara T, Shiono T, Sizuki T, Tanaka K, Takiot S, Yamazaki S, Satoh T (1999) Isolation of a germin-like protein with manganese superoxide dismutase activity from cells of a moss, Barbula unguiculata. J Biol Chem 274:33274-33278
    • (1999) J Biol Chem , vol.274 , pp. 33274-33278
    • Yamahara, T.1    Shiono, T.2    Sizuki, T.3    Tanaka, K.4    Takiot, S.5    Yamazaki, S.6    Satoh, T.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.