메뉴 건너뛰기




Volumn 46, Issue 6, 2012, Pages 750-757

Alterations in renal iron metabolism caused by a copper/zinc-superoxide dismutase deficiency

Author keywords

Iron; Iron regulatory proteins; Kidney; Reactive oxygen species; SOD

Indexed keywords

COPPER ZINC SUPEROXIDE DISMUTASE; IRON REGULATORY FACTOR;

EID: 84860725094     PISSN: 10715762     EISSN: 10292470     Source Type: Journal    
DOI: 10.3109/10715762.2012.673223     Document Type: Article
Times cited : (8)

References (37)
  • 1
    • 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
  • 2
    • 58149305448 scopus 로고    scopus 로고
    • Role of iron in carcinogenesis: Cancer as a ferrotoxic disease
    • Toyokuni S. Role of iron in carcinogenesis: cancer as a ferrotoxic disease. Cancer Sci 2009;100:9-16
    • (2009) Cancer Sci , vol.100 , pp. 9-16
    • Toyokuni, S.1
  • 3
    • 79952162002 scopus 로고    scopus 로고
    • Regulation of cellular iron metabolism
    • Wang J, Pantopoulos K. Regulation of cellular iron metabolism. Biochem J 2011;434:365-381.
    • (2011) Biochem J , vol.434 , pp. 365-381
    • Wang, J.1    Pantopoulos, K.2
  • 4
    • 0029758487 scopus 로고    scopus 로고
    • Molecular control of vertebrate iron metabolism: MRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress
    • DOI 10.1073/pnas.93.16.8175
    • Hentze MW, Köhn LC. Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress. Proc Natl Acad Sci USA 1996;93:8175-8182. (Pubitemid 26269529)
    • (1996) Proceedings of the National Academy of Sciences of the United States of America , vol.93 , Issue.16 , pp. 8175-8182
    • Hentze, M.W.1    Kuhn, L.C.2
  • 5
    • 0035933846 scopus 로고    scopus 로고
    • IRP1 activation by extracellular oxidative stress in the perfused rat liver
    • Mueller S, Pantopoulos K, Hübner CA, Stremmel W, Hentze MW. IRP1 activation by extracellular oxidative stress in the perfused rat liver. J Biol Chem 2001;276:23192-231926.
    • (2001) J Biol Chem , vol.276 , pp. 23192-231926
    • Mueller, S.1    Pantopoulos, K.2    Hübner, C.A.3    Stremmel, W.4    Hentze, M.W.5
  • 6
    • 79959539376 scopus 로고    scopus 로고
    • Iron regulatory protein 1 outcompetes iron regulatory protein 2 in regulating cellular iron homeostasis in response to nitric oxide
    • Styś A, Galy B, Starzyń ski RR, Smuda E, Drapier JC, Lipiń ski P, et al. Iron regulatory protein 1 outcompetes iron regulatory protein 2 in regulating cellular iron homeostasis in response to nitric oxide. J Biol Chem 2011;286:22846-22854.
    • (2011) J Biol Chem , vol.286 , pp. 22846-22854
    • Styś, A.1    Galy, B.2    Starzyń Ski, R.R.3    Smuda, E.4    Drapier, J.C.5    Lipiń Ski, P.6
  • 7
    • 0032571304 scopus 로고    scopus 로고
    • Regulation of iron regulatory protein 1 during hypoxia and hypoxiafreoxygenation
    • DOI 10.1074/jbc.273.13.7588
    • Hanson ES, Leibold EA. Regulation of iron regulatory protein 1 during hypoxia and hypoxia/reoxygenation. J Biol Chem 1998;273:7588-7593. (Pubitemid 28152786)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.13 , pp. 7588-7593
    • Hanson, E.S.1    Leibold, E.A.2
  • 9
    • 0029055581 scopus 로고
    • Rapid responses to oxidative stress mediated by iron regulatory protein
    • Pantopoulos K, Hentze MW. Rapid responses to oxidative stress mediated by iron regulatory protein. EMBO J 1995; 14:2917-2924.
    • (1995) EMBO J , vol.14 , pp. 2917-2924
    • Pantopoulos, K.1    Hentze, M.W.2
  • 10
    • 0031760436 scopus 로고    scopus 로고
    • Ovarian function in superoxide dismutase 1 and 2 knockout mice
    • DOI 10.1210/en.139.9.4008
    • Matzuk MM, Dionne L, Guo Q, Kumar TR, Lebovitz RM. Ovarian function in superoxide dismutase 1 and 2 knockout mice. Endocrinol 1998;139:4008-4011. (Pubitemid 28512286)
    • (1998) Endocrinology , vol.139 , Issue.9 , pp. 4008-4011
    • Matzuk, M.M.1    Dionne, L.2    Guo, Q.3    Kumar, T.R.4    Lebovitz, R.M.5
  • 12
    • 74549208029 scopus 로고    scopus 로고
    • Chronic ethanol consumption results in atypical liver injury in copper/zinc superoxide dismutase deficient mice
    • Curry-McCoy TV, Osna NA, Nanji AA, Donohue TM Jr. Chronic ethanol consumption results in atypical liver injury in copper/zinc superoxide dismutase deficient mice. Alcohol Clin Exp Res 2010;34:251-261.
    • (2010) Alcohol Clin Exp Res , vol.34 , pp. 251-261
    • Curry-Mccoy, T.V.1    Osna, N.A.2    Nanji, A.A.3    Donohue Jr., T.M.4
  • 13
    • 13244277942 scopus 로고    scopus 로고
    • CuZnSOD deficiency leads to persistent and widespread oxidative damage and hepatocarcinogenesis later in life
    • DOI 10.1038/sj.onc.1208207
    • Elchuri S, Oberley TD, Qi W, Eisenstein RS, Jackson Roberts L, Van Remmen H, et al. CuZnSOD deficiency leads to persistent and widespread oxidative damage and hepatocarcinogenesis later in life. Oncogene 2005;24:367-380. (Pubitemid 40188585)
    • (2005) Oncogene , vol.24 , Issue.3 , pp. 367-380
    • Elchuri, S.1    Oberley, T.D.2    Qi, W.3    Eisenstein, R.S.4    Roberts, L.J.5    Van Remmen, H.6    Epstein, C.J.7    Huang, T.-T.8
  • 15
    • 33845969893 scopus 로고    scopus 로고
    • CuZn-SOD deficiency causes ApoB degradation and induces hepatic lipid accumulation by impaired lipoprotein secretion in mice
    • DOI 10.1074/jbc.M603422200
    • Uchiyama S, Shimizu T, Shirasawa T. CuZn-SOD deficiency causes ApoB degradation and induces hepatic lipid accumulation by impaired lipoprotein secretion in mice. J Biol Chem 2006;281:31713-31719. (Pubitemid 46041436)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.42 , pp. 31713-31719
    • Uchiyama, S.1    Shimizu, T.2    Shirasawa, T.3
  • 16
    • 34250825268 scopus 로고    scopus 로고
    • Deterioration of ischemia/reperfusion-induced acute renal failure in SOD1-deficient mice
    • DOI 10.1080/10715760601038791, PII 770494159
    • Yamanobe T, Okada F, Iuchi Y, Onuma K, Tomita Y, Fujii J, et al. Deterioration of ischemia/reperfusion-induced acute renal failure in SOD1-deficient mice. Free Radic Res 2007; 41:200-207. (Pubitemid 46992870)
    • (2007) Free Radical Research , vol.41 , Issue.2 , pp. 200-207
    • Yamanobe, T.1    Okada, F.2    Iuchi, Y.3    Onuma, K.4    Tomita, Y.5    Fujii, J.6
  • 17
    • 33847757480 scopus 로고    scopus 로고
    • Elevated oxidative stress in erythrocytes due to a SOD1 deficiency causes anaemia and triggers autoantibody production
    • DOI 10.1042/BJ20061386
    • Iuchi Y, Okada F, Onuma K, Onoda T, Asao H, Kobayashi M, et al. Elevated oxidative stress in erythrocytes due to a SOD1 deficiency causes anaemia and triggers autoantibody production. Biochem J 2007;402:219-227. (Pubitemid 46383419)
    • (2007) Biochemical Journal , vol.402 , Issue.2 , pp. 219-227
    • Iuchi, Y.1    Okada, F.2    Onuma, K.3    Onoda, T.4    Asao, H.5    Kobayashi, M.6    Fujii, J.7
  • 18
    • 33646344248 scopus 로고    scopus 로고
    • Phenotypes of mice lacking extracellular superoxide dismutase and copper- and zinc-containing superoxide dismutase
    • DOI 10.1074/jbc.M510764200
    • Sentman ML, Granström M, Jakobson H, Reaume A, Basu S, Marklund SL, et al. Phenotypes of mice lacking extracellular superoxide dismutase and copper-and zinccontaining superoxide dismutase. J Biol Chem 2006;281: 6904-6909. (Pubitemid 43847452)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.11 , pp. 6904-6909
    • Sentman, M.-L.1    Granstrom, M.2    Jakobson, H.3    Reaume, A.4    Basu, S.5    Marklund, S.L.6
  • 19
    • 14244254585 scopus 로고    scopus 로고
    • Down-regulation of iron regulatory protein 1 activities and expression in superoxide dismutase 1 knock-out mice is not associated with alterations in iron metabolism
    • DOI 10.1074/jbc.M411055200
    • Starzynski RR, Lipinski P, Drapier JC, Diet A, Smuda E, Bartlomiejczyk T, et al. Down-regulation of iron regulatory protein 1 activities and expression in superoxide dismutase 1 knock-out mice is not associated with alterations in iron metabolism. J Biol Chem 2005;280:4207-4212. (Pubitemid 40288586)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.6 , pp. 4207-4212
    • Starzynski, R.R.1    Lipinski, P.2    Drapier, J.-C.3    Diet, A.4    Smuda, E.5    Bartlomiejczyk, T.6    Gralak, M.A.7    Kruszewski, M.8
  • 20
    • 66949174343 scopus 로고    scopus 로고
    • Haemolytic anaemia and alterations in hepatic iron metabolism in aged mice lacking Cu,Znsuperoxide dismutase
    • Starzyś s ki RR, Canonne-Hergaux F, Willemetz A, Gralak MA, Woliń ski J, Styś A, et al. Haemolytic anaemia and alterations in hepatic iron metabolism in aged mice lacking Cu,Znsuperoxide dismutase. Biochem J 2009;420:383-390.
    • (2009) Biochem J , vol.420 , pp. 383-390
    • Starzyś Kis, R.R.1    Canonne-Hergaux, F.2    Willemetz, A.3    Gralak, M.A.4    Woliński, J.5    Styś, A.6
  • 21
    • 67650720048 scopus 로고    scopus 로고
    • Protective role of glutathione S-transferase A4 induced in copper/zinc-superoxide dismutase knockout mice
    • Yoshihara D, Fujiwara N, Ookawara T, Kato S, Sakiyama H, Yokoe S, et al. Protective role of glutathione S-transferase A4 induced in copper/zinc- superoxide dismutase knockout mice. Free Radic Biol Med 2009;47:559-567.
    • (2009) Free Radic Biol Med , vol.47 , pp. 559-567
    • Yoshihara, D.1    Fujiwara, N.2    Ookawara, T.3    Kato, S.4    Sakiyama, H.5    Yokoe, S.6
  • 23
    • 0029914953 scopus 로고    scopus 로고
    • Phosphorylation and activation of both iron regulatory proteins 1 and 2 in HL-60 cells
    • DOI 10.1074/jbc.271.12.7168
    • Schalinske KL, Eisenstein RS. Phosphorylation and activation of both iron regulatory proteins 1 and 2 in HL-60 cells. J Biol Chem 1996;271:7168-7176. (Pubitemid 26104157)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.12 , pp. 7168-7176
    • Schalinske, K.L.1    Eisenstein, R.S.2
  • 24
    • 33846706460 scopus 로고    scopus 로고
    • Renal iron metabolism: Transferrin iron delivery and the role of iron regulatory proteins
    • DOI 10.1681/ASN.2006080908
    • Zhang D, Meyron-Holtz E, Rouault TA. Renal iron metabolism: transferrin iron delivery and the role of iron regulatory proteins. J Am Soc Nephrol 2007;18:401-406. (Pubitemid 46193305)
    • (2007) Journal of the American Society of Nephrology , vol.18 , Issue.2 , pp. 401-406
    • Zhang, D.1    Meyron-Holtz, E.2    Rouault, T.A.3
  • 25
    • 57049185266 scopus 로고    scopus 로고
    • Role of the kidney in iron homeostasis: Renal expression of Prohepcidin, Ferroportin, and DMT1 in anemic mice
    • Veuthey T, D'Anna MC, Roque ME. Role of the kidney in iron homeostasis: renal expression of Prohepcidin, Ferroportin, and DMT1 in anemic mice. Am J Physiol Renal Physiol 2008;295:F1213-F1221.
    • (2008) Am J Physiol Renal Physiol , vol.295
    • Veuthey, T.1    D'Anna, M.C.2    Roque, M.E.3
  • 26
    • 79952162002 scopus 로고    scopus 로고
    • Regulation of cellular iron metabolism
    • Wang J, Pantopoulos K. Regulation of cellular iron metabolism. Biochem J 2011;434:365-381.
    • (2011) Biochem J , vol.434 , pp. 365-381
    • Wang, J.1    Pantopoulos, K.2
  • 27
    • 79952451733 scopus 로고    scopus 로고
    • Nrf2 regulates ferroportin 1-mediated iron efflux and counteracts lipopolysaccharide-induced ferroportin 1 mRNA suppression in macrophages
    • Harada N, Kanayama M, Maruyama A, Yoshida A, Tazumi K, Hosoya T, et al. Nrf2 regulates ferroportin 1-mediated iron efflux and counteracts lipopolysaccharide-induced ferroportin 1 mRNA suppression in macrophages. Arch Biochem Biophys 2011;508:101-109.
    • (2011) Arch Biochem Biophys , vol.508 , pp. 101-109
    • Harada, N.1    Kanayama, M.2    Maruyama, A.3    Yoshida, A.4    Tazumi, K.5    Hosoya, T.6
  • 29
    • 79958146087 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-2a mediates the adaptive increase of intestinal ferroportin during iron defi-ciency in mice
    • Taylor M, Qu A, Anderson ER, Matsubara T, Martin A, Gonzalez FJ, et al. Hypoxia-inducible factor-2a mediates the adaptive increase of intestinal ferroportin during iron defi-ciency in mice. Gastroenterol 2011;140:2044-2055.
    • (2011) Gastroenterol , vol.140 , pp. 2044-2055
    • Taylor, M.1    Qu, A.2    Anderson, E.R.3    Matsubara, T.4    Martin, A.5    Gonzalez, F.J.6
  • 31
    • 77953854244 scopus 로고    scopus 로고
    • Hypoxic regulation of erythropoiesis and iron metabolism
    • Haase VH. Hypoxic regulation of erythropoiesis and iron metabolism. Am J Physiol Renal Physiol 2010;299: F1-F13.
    • (2010) Am J Physiol Renal Physiol , vol.299
    • Haase, V.H.1
  • 32
    • 0030886381 scopus 로고    scopus 로고
    • Heme oxygenase 1 is required for mammalian iron reutilization
    • Poss KD, Tonegawa S. Heme oxygenase 1 is required for mammalian iron reutilization. Proc Natl Acad Sci USA. 1997;94:10919-1024.
    • (1997) Proc Natl Acad Sci USA. , vol.94 , pp. 10919-1024
    • Poss, K.D.1    Tonegawa, S.2
  • 34
    • 0141781072 scopus 로고    scopus 로고
    • A phosphomimetic mutation at Ser-138 renders iron regulatory protein 1 sensitive to iron-dependent degradation
    • DOI 10.1128/MCB.23.19.6973-6981.2003
    • Fillebeen C, Chahine D, Caltagirone A, Segal P, Pantopoulos K. A phosphomimetic mutation at Ser-138 renders iron regulatory protein 1 sensitive to iron-dependent degradation. Mol Cell Biol 2003;23:6973-6981. (Pubitemid 37214664)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.19 , pp. 6973-6981
    • Fillebeen, C.1    Chahine, D.2    Caltagirone, A.3    Segal, P.4    Pantopoulos, K.5
  • 35
    • 19544363018 scopus 로고    scopus 로고
    • IRP1 Ser-711 is a phosphorylation site, critical for regulation of RNA-binding and aconitase activities
    • DOI 10.1042/BJ20041623
    • Fillebeen C, Caltagirone A, Martelli A, Moulis JM, Pantopoulos K. IRP1 Ser-711 is a phosphorylation site, critical for regulation of RNA-binding and aconitase activities. Biochem J 2005;388:143-150. (Pubitemid 40732941)
    • (2005) Biochemical Journal , vol.388 , Issue.1 , pp. 143-150
    • Fillebeen, C.1    Caltagirone, A.2    Martelli, A.3    Moulis, J.-M.4    Pantopoulos, K.5
  • 37
    • 0031002851 scopus 로고    scopus 로고
    • The iron-sulfur cluster of iron regulatory protein 1 modulates the accessibility of RNA binding and phosphorylation sites
    • DOI 10.1021/bi9624447
    • Schalinske KL, Anderson SA, Tuazon PT, Chen OS, Kennedy MC, Eisenstein RS, et al. The iron-sulfur cluster of iron regulatory protein 1 modulates the accessibility of RNA binding and phosphorylation sites. Biochemistry 1997;36: 3950-3958. (Pubitemid 27154716)
    • (1997) Biochemistry , vol.36 , Issue.13 , pp. 3950-3958
    • Schalinske, K.L.1    Anderson, S.A.2    Tuazon, P.T.3    Chen, O.S.4    Kennedy, M.C.5    Eisenstein, R.S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.