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Volumn 66, Issue 5, 2006, Pages 522-535

Superoxide dismutase in the prostate lobes of aging Brown Norway rats

Author keywords

Benign prostatic hyperplasia; Morphology; Reactive oxygen; Testosterone

Indexed keywords

COPPER ZINC SUPEROXIDE DISMUTASE; MANGANESE SUPEROXIDE DISMUTASE; REACTIVE OXYGEN METABOLITE; SUPEROXIDE DISMUTASE; SUPEROXIDE DISMUTASE 3; TESTOSTERONE; UNCLASSIFIED DRUG; ZINC;

EID: 33645361965     PISSN: 02704137     EISSN: 10970045     Source Type: Journal    
DOI: 10.1002/pros.20364     Document Type: Article
Times cited : (6)

References (54)
  • 1
    • 0033015743 scopus 로고    scopus 로고
    • The aging paradox: Free radical theory of aging
    • Ashok BT, Ali R. The aging paradox: Free radical theory of aging. Exp Gerontol 1999;34:293-303.
    • (1999) Exp Gerontol , vol.34 , pp. 293-303
    • Ashok, B.T.1    Ali, R.2
  • 2
    • 0028085968 scopus 로고
    • Alterations in free radical activity in aging drosophila
    • Shi L, Sawada M, Sester U, Carlson JC. Alterations in free radical activity in aging drosophila. Exp Gerontol 1994;29:575-584.
    • (1994) Exp Gerontol , vol.29 , pp. 575-584
    • Shi, L.1    Sawada, M.2    Sester, U.3    Carlson, J.C.4
  • 3
    • 0030585316 scopus 로고    scopus 로고
    • Age-related changes in the activities of antioxidant enzymes and lipid peroxidation status in ventral and dorsolateral prostate lobes of noble rats
    • Ghatak S, Ho SM. Age-related changes in the activities of antioxidant enzymes and lipid peroxidation status in ventral and dorsolateral prostate lobes of noble rats. Biochem Biophys Res Commun 1996;222:362-367.
    • (1996) Biochem Biophys Res Commun , vol.222 , pp. 362-367
    • Ghatak, S.1    Ho, S.M.2
  • 4
    • 0035032925 scopus 로고    scopus 로고
    • Impairment of learning and memory in rats caused by oxidative stress and aging, and changes in antioxidative defense systems
    • Fukui K, Onodera K, Shinkai T, Suzuki S, Urano S. Impairment of learning and memory in rats caused by oxidative stress and aging, and changes in antioxidative defense systems. Ann NY Acad Sci 2001;928:168-175.
    • (2001) Ann NY Acad Sci , vol.928 , pp. 168-175
    • Fukui, K.1    Onodera, K.2    Shinkai, T.3    Suzuki, S.4    Urano, S.5
  • 5
    • 0037382969 scopus 로고    scopus 로고
    • Sex hormone-induced alterations in the activities of antioxidant enzymes and lipid peroxidation status in the prostate of noble rats
    • Tam NN, Ghatak S, Ho SM. Sex hormone-induced alterations in the activities of antioxidant enzymes and lipid peroxidation status in the prostate of noble rats. Prostate 2003;55:1-8.
    • (2003) Prostate , vol.55 , pp. 1-8
    • Tam, N.N.1    Ghatak, S.2    Ho, S.M.3
  • 6
    • 0345596416 scopus 로고    scopus 로고
    • Alterations of antioxidant enzymes and oxidative damage to macromolecules in different organs of rats during aging
    • Tian L, Cai Q, Wei H. Alterations of antioxidant enzymes and oxidative damage to macromolecules in different organs of rats during aging. Free Radic Biol Med 1998;24:1477-1484.
    • (1998) Free Radic Biol Med , vol.24 , pp. 1477-1484
    • Tian, L.1    Cai, Q.2    Wei, H.3
  • 8
    • 0035039021 scopus 로고    scopus 로고
    • Protein oxidation in aging and age-related diseases
    • Stadtman ER. Protein oxidation in aging and age-related diseases. Ann NY Acad Sci 2001;928:22-38.
    • (2001) Ann NY Acad Sci , vol.928 , pp. 22-38
    • Stadtman, E.R.1
  • 9
    • 0037249066 scopus 로고    scopus 로고
    • Relation of aging with oxidative protein damage parameters in the rat skeletal muscle
    • Cakatay U, Telci A, Kayali R, Tekeli F, Akcay T, Sivas A. Relation of aging with oxidative protein damage parameters in the rat skeletal muscle. Clin Biochem 2003;36:51-55.
    • (2003) Clin Biochem , vol.36 , pp. 51-55
    • Cakatay, U.1    Telci, A.2    Kayali, R.3    Tekeli, F.4    Akcay, T.5    Sivas, A.6
  • 10
    • 0029007378 scopus 로고
    • Oxidative stress and aging in the mongolian gerbil (meriones unguiculatus)
    • Sohal RS, Agarwal S, Sohal BH. Oxidative stress and aging in the mongolian gerbil (meriones unguiculatus). Mech Ageing Dev 1995;81:15-25.
    • (1995) Mech Ageing Dev , vol.81 , pp. 15-25
    • Sohal, R.S.1    Agarwal, S.2    Sohal, B.H.3
  • 12
    • 0035872001 scopus 로고    scopus 로고
    • Age-related changes in oxidative damage to lipids and DNA in rat skin
    • Tahara S, Matsuo M, Kaneko T. Age-related changes in oxidative damage to lipids and DNA in rat skin. Mech Ageing Dev 2001;122:415-426.
    • (2001) Mech Ageing Dev , vol.122 , pp. 415-426
    • Tahara, S.1    Matsuo, M.2    Kaneko, T.3
  • 13
    • 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 2000;408:239-247.
    • (2000) Nature , vol.408 , pp. 239-247
    • Finkel, T.1    Holbrook, N.J.2
  • 14
    • 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. 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 2001;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
  • 15
    • 0036323863 scopus 로고    scopus 로고
    • Role of superoxide dismutases in oxidative damage and neurodegenerative disorders
    • Maier CM, Chan PH. Role of superoxide dismutases in oxidative damage and neurodegenerative disorders. Neuroscientist 2002;8:323-334.
    • (2002) Neuroscientist , vol.8 , pp. 323-334
    • Maier, C.M.1    Chan, P.H.2
  • 16
    • 0032571387 scopus 로고    scopus 로고
    • Reduced fertility in female mice lacking copper-zinc superoxide dismutase
    • Ho YS, Gargano M, Cao J, Bronson RT, Heimler I, Hutz RJ. Reduced fertility in female mice lacking copper-zinc superoxide dismutase. J Biol Chem 1998;273:7765-7769.
    • (1998) J Biol Chem , vol.273 , pp. 7765-7769
    • Ho, Y.S.1    Gargano, M.2    Cao, J.3    Bronson, R.T.4    Heimler, I.5    Hutz, R.J.6
  • 17
    • 0036667555 scopus 로고    scopus 로고
    • Superoxide dismutase multigene family: A comparison of the CuZn-SOD (SOD1), Mn-SOD (SOD2), and EC-SOD (SOD3) gene structures, evolution, and expression
    • Zelko IN, Mariani TJ, Folz RJ. Superoxide dismutase multigene family: A comparison of the CuZn-SOD (SOD1), Mn-SOD (SOD2), and EC-SOD (SOD3) gene structures, evolution, and expression. Free Radic Biol Med 2002;33:337-349.
    • (2002) Free Radic Biol Med , vol.33 , pp. 337-349
    • Zelko, I.N.1    Mariani, T.J.2    Folz, R.J.3
  • 19
    • 0032561328 scopus 로고    scopus 로고
    • Increased oxidative damage is correlated to altered mitochondrial function in heterozygous manganese superoxide dismutase knockout mice
    • Williams MD, Van Remmen H, Conrad CC, Huang TT, Epstein CJ, Richardson A. Increased oxidative damage is correlated to altered mitochondrial function in heterozygous manganese superoxide dismutase knockout mice. J Biol Chem 1998;273:28510-28515.
    • (1998) J Biol Chem , vol.273 , pp. 28510-28515
    • Williams, M.D.1    Van Remmen, H.2    Conrad, C.C.3    Huang, T.T.4    Epstein, C.J.5    Richardson, A.6
  • 21
    • 1842709537 scopus 로고
    • Isolation and sequence of complementary DNA encoding human extracellular superoxide dismutase
    • Hjalmarsson K, Marklund SL, Engstrom A, Edlund T. Isolation and sequence of complementary DNA encoding human extracellular superoxide dismutase. Proc Natl Acad Sci USA 1987;84:6340-6344.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 6340-6344
    • Hjalmarsson, K.1    Marklund, S.L.2    Engstrom, A.3    Edlund, T.4
  • 22
    • 0031253163 scopus 로고    scopus 로고
    • Mouse extracellular superoxide dismutase: Primary structure, tissue-specific gene expression, chromosomal localization, and lung in situ hybridization
    • Folz RJ, Guan J, Seldin MF, Oury TD, Enghild JJ, Crapo JD. Mouse extracellular superoxide dismutase: Primary structure, tissue-specific gene expression, chromosomal localization, and lung in situ hybridization. Am J Respir Cell Mol Biol 1997;17:393-403.
    • (1997) Am J Respir Cell Mol Biol , vol.17 , pp. 393-403
    • Folz, R.J.1    Guan, J.2    Seldin, M.F.3    Oury, T.D.4    Enghild, J.J.5    Crapo, J.D.6
  • 24
    • 0029992837 scopus 로고    scopus 로고
    • The rat extracellular superoxide dismutase dimer is converted to a tetramer by the exchange of a single amino acid
    • Carlsson LM, Marklund SL, Edlund T. The rat extracellular superoxide dismutase dimer is converted to a tetramer by the exchange of a single amino acid. Proc Natl Acad Sci USA 1996;93:5219-5222.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 5219-5222
    • Carlsson, L.M.1    Marklund, S.L.2    Edlund, T.3
  • 25
    • 0029064709 scopus 로고
    • Mice lacking extracellular superoxide dismutase are more sensitive to hyperoxia
    • Carlsson LM, Jonsson J, Edlund T, Marklund SL. Mice lacking extracellular superoxide dismutase are more sensitive to hyperoxia. Proc Natl Acad Sci USA 1995;92:6264-6268.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 6264-6268
    • Carlsson, L.M.1    Jonsson, J.2    Edlund, T.3    Marklund, S.L.4
  • 27
    • 0028966530 scopus 로고
    • DNA base modifications and antioxidant enzyme activities in human benign prostatic hyperplasia
    • Olinski R, Zastawny TH, Foksinski M, Barecki A, Dizdaroglu M. DNA base modifications and antioxidant enzyme activities in human benign prostatic hyperplasia. Free Radic Biol Med 1995;18:807-813.
    • (1995) Free Radic Biol Med , vol.18 , pp. 807-813
    • Olinski, R.1    Zastawny, T.H.2    Foksinski, M.3    Barecki, A.4    Dizdaroglu, M.5
  • 28
    • 0029984062 scopus 로고    scopus 로고
    • Antioxidant and redox regulation of gene transcription
    • Sen CK, Packer L. Antioxidant and redox regulation of gene transcription. FASEB J 1996;10:709-720.
    • (1996) FASEB J , vol.10 , pp. 709-720
    • Sen, C.K.1    Packer, L.2
  • 31
    • 0033796721 scopus 로고    scopus 로고
    • Regulation of leydig cell steroidogenic function during aging
    • Zirkin BR, Chen H. Regulation of leydig cell steroidogenic function during aging. Biol Reprod 2000;63:977-981.
    • (2000) Biol Reprod , vol.63 , pp. 977-981
    • Zirkin, B.R.1    Chen, H.2
  • 32
    • 0024402834 scopus 로고
    • An assay for superoxide dismutase activity in mammalian tissue homogenates
    • Spitz DR, Oberley LW. An assay for superoxide dismutase activity in mammalian tissue homogenates. Anal Biochem 1989;179:8-18.
    • (1989) Anal Biochem , vol.179 , pp. 8-18
    • Spitz, D.R.1    Oberley, L.W.2
  • 33
    • 9144261759 scopus 로고    scopus 로고
    • The unusually stable quaternary structure of human cu,zn-superoxide dismutase 1 is controlled by both metal occupancy and disulfide status
    • Arnesano F, Banci L, Bertini I, Martinelli M, Furukawa Y, O'Halloran TV. The unusually stable quaternary structure of human cu,zn-superoxide dismutase 1 is controlled by both metal occupancy and disulfide status. J Biol Chem 2004;279:47998-48003.
    • (2004) J Biol Chem , vol.279 , pp. 47998-48003
    • Arnesano, F.1    Banci, L.2    Bertini, I.3    Martinelli, M.4    Furukawa, Y.5    O'Halloran, T.V.6
  • 34
    • 20744444389 scopus 로고    scopus 로고
    • Manganese activation of superoxide dismutase 2 in the mitochondria of saccharomyces cerevisiae
    • Luk E, Yang M, Jensen LT, Bourbonnais Y, Culotta VC. Manganese activation of superoxide dismutase 2 in the mitochondria of saccharomyces cerevisiae. J Biol Chem 2005;280:22715-22720.
    • (2005) J Biol Chem , vol.280 , pp. 22715-22720
    • Luk, E.1    Yang, M.2    Jensen, L.T.3    Bourbonnais, Y.4    Culotta, V.C.5
  • 35
    • 0021297080 scopus 로고
    • Anatomy of the prostate and morphogenesis of BPH
    • McNeal JE. Anatomy of the prostate and morphogenesis of BPH. Prog Clin Biol Res 1984;145:27-53.
    • (1984) Prog Clin Biol Res , vol.145 , pp. 27-53
    • McNeal, J.E.1
  • 37
    • 0034878783 scopus 로고    scopus 로고
    • Increased androgen receptor expression correlates with development of age-dependent, lobe-specific spontaneous hyperplasia of the brown norway rat prostate
    • Banerjee PP, Banerjee S, Brown TR. Increased androgen receptor expression correlates with development of age-dependent, lobe-specific spontaneous hyperplasia of the brown norway rat prostate. Endocrinology 2001;142:4066-4075.
    • (2001) Endocrinology , vol.142 , pp. 4066-4075
    • Banerjee, P.P.1    Banerjee, S.2    Brown, T.R.3
  • 38
    • 0020697979 scopus 로고
    • Subcellular distribution of androgen receptors in human normal, benign hyperplastic, and malignant prostatic tissues: Characterization of nuclear salt-resistant receptors
    • Barrack ER, Bujnovszky P, Walsh PC. Subcellular distribution of androgen receptors in human normal, benign hyperplastic, and malignant prostatic tissues: Characterization of nuclear salt-resistant receptors. Cancer Res 1983;43:1107-1116.
    • (1983) Cancer Res , vol.43 , pp. 1107-1116
    • Barrack, E.R.1    Bujnovszky, P.2    Walsh, P.C.3
  • 39
    • 0021149603 scopus 로고
    • The development of human benign prostatic hyperplasia with age
    • Berry SJ, Coffey DS, Walsh PC, Ewing LL. The development of human benign prostatic hyperplasia with age. J Urol 1984;132:474-479.
    • (1984) J Urol , vol.132 , pp. 474-479
    • Berry, S.J.1    Coffey, D.S.2    Walsh, P.C.3    Ewing, L.L.4
  • 40
    • 0014691242 scopus 로고
    • Superoxide dismutase, an enzymic function for erythrocuprein (hemocuprein)
    • McCord JM, Fridovich I. Superoxide dismutase, an enzymic function for erythrocuprein (hemocuprein). J Biol Chem 1969;244:6049-6055.
    • (1969) J Biol Chem , vol.244 , pp. 6049-6055
    • McCord, J.M.1    Fridovich, I.2
  • 41
    • 0031554917 scopus 로고    scopus 로고
    • Spectrophotometric assay for superoxide dismutase based on tetrazolium salt 3′-1-(phenylamino)-carbonyl-3, 4-tetrazolium-bis(4-methoxy-6-nitro) benzenesulfonic acid hydrate reduction by xanthine-xanthine oxidase
    • Ukeda H, Maeda S, Ishii T, Sawamura M. Spectrophotometric assay for superoxide dismutase based on tetrazolium salt 3′-1-(phenylamino)- carbonyl-3, 4-tetrazolium]-bis(4-methoxy-6-nitro)benzenesulfonic acid hydrate reduction by xanthine-xanthine oxidase. Anal Biochem 1997;251:206-209.
    • (1997) Anal Biochem , vol.251 , pp. 206-209
    • Ukeda, H.1    Maeda, S.2    Ishii, T.3    Sawamura, M.4
  • 42
    • 0035874180 scopus 로고    scopus 로고
    • Effects of age and strain on small intestinal and hepatic antioxidant defense enzymes in wistar and fisher 344 rats
    • Jang I, Chae K, Cho J. Effects of age and strain on small intestinal and hepatic antioxidant defense enzymes in wistar and fisher 344 rats. Mech Ageing Dev 2001;122(6):561-570.
    • (2001) Mech Ageing Dev , vol.122 , Issue.6 , pp. 561-570
    • Jang, I.1    Chae, K.2    Cho, J.3
  • 43
    • 0025210008 scopus 로고
    • Alteration of antioxidant enzymes with aging in rat skeletal muscle and liver
    • Ji LL, Dillon D, Wu E. Alteration of antioxidant enzymes with aging in rat skeletal muscle and liver. Am J Physiol 1990;258:R918-R923.
    • (1990) Am J Physiol , vol.258
    • Ji, L.L.1    Dillon, D.2    Wu, E.3
  • 44
    • 4344644670 scopus 로고    scopus 로고
    • Effect of glutathione depletion on antioxidant enzymes in the epididymis, seminal vesicles, and liver and on spermatozoa motility in the aging brown norway rat
    • Zubkova EV, Robaire B. Effect of glutathione depletion on antioxidant enzymes in the epididymis, seminal vesicles, and liver and on spermatozoa motility in the aging brown norway rat. Biol Reprod 2004;71:1002-1008.
    • (2004) Biol Reprod , vol.71 , pp. 1002-1008
    • Zubkova, E.V.1    Robaire, B.2
  • 46
    • 0142012094 scopus 로고    scopus 로고
    • Extracellular superoxide dismutase in biology and medicine
    • Fattman CL, Schaefer LM, Oury TD. Extracellular superoxide dismutase in biology and medicine. Free Radic Biol Med 2003;35:236-256.
    • (2003) Free Radic Biol Med , vol.35 , pp. 236-256
    • Fattman, C.L.1    Schaefer, L.M.2    Oury, T.D.3
  • 47
    • 0034721928 scopus 로고    scopus 로고
    • Copper activation of superoxide dismutase 1 (SOD1) in vivo. Role for protein-protein interactions with the copper chaperone for SOD1
    • Schmidt PJ, Kunst C, Culotta VC. Copper activation of superoxide dismutase 1 (SOD1) in vivo. Role for protein-protein interactions with the copper chaperone for SOD1. J Biol Chem 2000;275:33771-33776.
    • (2000) J Biol Chem , vol.275 , pp. 33771-33776
    • Schmidt, P.J.1    Kunst, C.2    Culotta, V.C.3
  • 50
    • 0036931270 scopus 로고    scopus 로고
    • Zinc fingers-folds for many occasions
    • Matthews JM, Sunde M. Zinc fingers-folds for many occasions. IUBMB Life 2002;54:351-355.
    • (2002) IUBMB Life , vol.54 , pp. 351-355
    • Matthews, J.M.1    Sunde, M.2
  • 51
    • 0035696301 scopus 로고    scopus 로고
    • Functions of zinc in signaling, proliferation and differentiation of mammalian cells
    • Beyersmann D, Haase H. Functions of zinc in signaling, proliferation and differentiation of mammalian cells. Biometals 2001;14:331-341.
    • (2001) Biometals , vol.14 , pp. 331-341
    • Beyersmann, D.1    Haase, H.2
  • 52
    • 0035693751 scopus 로고    scopus 로고
    • The role of zinc in caspase activation and apoptotic cell death
    • Truong-Tran AQ, Carter J, Ruffin RE, Zalewski PD. The role of zinc in caspase activation and apoptotic cell death. Biometals 2001;14:315-330.
    • (2001) Biometals , vol.14 , pp. 315-330
    • Truong-Tran, A.Q.1    Carter, J.2    Ruffin, R.E.3    Zalewski, P.D.4
  • 53
    • 2342437480 scopus 로고    scopus 로고
    • Zinc for prostate disease and other conditions: A little evidence, a lot of hype, and a significant potential problem
    • Moyad MA. Zinc for prostate disease and other conditions: A little evidence, a lot of hype, and a significant potential problem. Urol Nurs 2004;24:49-52.
    • (2004) Urol Nurs , vol.24 , pp. 49-52
    • Moyad, M.A.1
  • 54
    • 0036720332 scopus 로고    scopus 로고
    • Direct effect of zinc on mitochondrial apoptogenesis in prostate cells
    • Feng P, Li TL, Guan ZX, Franklin RB, Costello LC. Direct effect of zinc on mitochondrial apoptogenesis in prostate cells. Prostate 2002;52:311-318.
    • (2002) Prostate , vol.52 , pp. 311-318
    • Feng, P.1    Li, T.L.2    Guan, Z.X.3    Franklin, R.B.4    Costello, L.C.5


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