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Volumn 37, Issue 10, 2012, Pages 2108-2116

Extracellular superoxide dismutase in cultured astrocytes: Decrease in cell-surface activity and increase in medium activity by lipopolysaccharide- stimulation

Author keywords

Astrocytes; Cell surface activity of SOD; Extracellular superoxide dismutase; Lipopolysaccharide; Neuron and microglia

Indexed keywords

BACTERIUM LIPOPOLYSACCHARIDE; EXTRACELLULAR SUPEROXIDE DISMUTASE; HYPOXANTHINE; MESSENGER RNA; OXYGEN; TETRAZOLIUM; XANTHINE OXIDASE;

EID: 84866738512     PISSN: 03643190     EISSN: 15736903     Source Type: Journal    
DOI: 10.1007/s11064-012-0832-z     Document Type: Article
Times cited : (11)

References (26)
  • 1
    • 0037058827 scopus 로고    scopus 로고
    • Vascular oxidative stress and endothelial dysfunction in patients with chronic heart failure: Role of xanthine-oxidase and extracellular superoxide dismutase
    • Landmesser U, Spiekermann S, Dikalov S, Tatge H, Wilke R, Kohler C, Harrison DG, Hornig B, Drexler H (2002) Vascular oxidative stress and endothelial dysfunction in patients with chronic heart failure: role of xanthine-oxidase and extracellular superoxide dismutase. Circulation 106:3073-3078
    • (2002) Circulation , vol.106 , pp. 3073-3078
    • Landmesser, U.1    Spiekermann, S.2    Dikalov, S.3    Tatge, H.4    Wilke, R.5    Kohler, C.6    Harrison, D.G.7    Hornig, B.8    Drexler, H.9
  • 2
    • 0025260736 scopus 로고
    • Excitatory amino acid release and free radical formation may cooperate in the genesis of ischemia-induced neuronal damage
    • Pellegrini-Giampietro DE, Cherici G, Alesiani M, Carla V, Moroni F (1990) Excitatory amino acid release and free radical formation may cooperate in the genesis of ischemia-induced neuronal damage. J Neurosci 10:1035-1041
    • (1990) J Neurosci , vol.10 , pp. 1035-1041
    • Pellegrini-Giampietro, D.E.1    Cherici, G.2    Alesiani, M.3    Carla, V.4    Moroni, F.5
  • 3
    • 0037378026 scopus 로고    scopus 로고
    • Oxidative stress in Parkinson's disease
    • discussion S36-S38
    • Jenner P (2003) Oxidative stress in Parkinson's disease. Ann Neurol 53(Suppl 3):S26-S36 (discussion S36-S38)
    • (2003) Ann Neurol , vol.53 , Issue.SUPPL. 3
    • Jenner, P.1
  • 4
    • 0014691242 scopus 로고
    • Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein)
    • McCord JM, Fridovich I (1969) Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J Biol Chem 244:6049-6055
    • (1969) J Biol Chem , vol.244 , pp. 6049-6055
    • McCord, J.M.1    Fridovich, I.2
  • 5
    • 0028338554 scopus 로고
    • 10-Fold increase in human plasma extracellular superoxide dismutase content caused by a mutation in heparin-binding domain
    • Sandstrom J, Nilsson P, Karlsson K, Marklund SL (1994) 10-Fold increase in human plasma extracellular superoxide dismutase content caused by a mutation in heparin-binding domain. J Biol Chem 269:19163-19166
    • (1994) J Biol Chem , vol.269 , pp. 19163-19166
    • Sandstrom, J.1    Nilsson, P.2    Karlsson, K.3    Marklund, S.L.4
  • 6
    • 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 (1997) Mouse extracellular superoxide dismutase: primary structure, tissue-specific gene expression, chromosomal localization, and lung in situ hybridization. Am J Respir Cell Mol Biol 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
  • 7
    • 12844261649 scopus 로고    scopus 로고
    • The high concentration of Arg213→Gly extracellular superoxide dismutase (ECSOD) in plasma is caused by a reduction of both heparin and collagen affinities
    • Petersen SV, Olsen DA, Kenney JM, Oury TD, Valnickova Z, Thogersen IB, Crapo JD, Enghild JJ (2005) The high concentration of Arg213→Gly extracellular superoxide dismutase (ECSOD) in plasma is caused by a reduction of both heparin and collagen affinities. Biochem J 385:427-432
    • (2005) Biochem J , vol.385 , pp. 427-432
    • Petersen, S.V.1    Olsen, D.A.2    Kenney, J.M.3    Oury, T.D.4    Valnickova, Z.5    Thogersen, I.B.6    Crapo, J.D.7    Enghild, J.J.8
  • 8
    • 0023791674 scopus 로고
    • Binding of human extracellular superoxide dismutase C to sulphated glycosaminoglycans
    • Karlsson K, Lindahl U, Marklund SL (1988) Binding of human extracellular superoxide dismutase C to sulphated glycosaminoglycans. Biochem J 256:29-33
    • (1988) Biochem J , vol.256 , pp. 29-33
    • Karlsson, K.1    Lindahl, U.2    Marklund, S.L.3
  • 9
    • 0024335080 scopus 로고
    • Interactions between human extracellular superoxide dismutase C and sulfated polysaccharides
    • Adachi T, Marklund SL (1989) Interactions between human extracellular superoxide dismutase C and sulfated polysaccharides. J Biol Chem 264:8537-8541
    • (1989) J Biol Chem , vol.264 , pp. 8537-8541
    • Adachi, T.1    Marklund, S.L.2
  • 10
    • 0033591243 scopus 로고    scopus 로고
    • The heparin-binding domain of extracellular superoxide dismutase is proteolytically processed intracellularly during biosynthesis
    • Enghild JJ, Thøgersen IB, Oury TD, Valnickova Z, Højrup P, Crapo JD (1999) The heparin-binding domain of extracellular superoxide dismutase is proteolytically processed intracellularly during biosynthesis. J Biol Chem 274:14818-14822
    • (1999) J Biol Chem , vol.274 , pp. 14818-14822
    • Enghild, J.J.1    Thøgersen, I.B.2    Oury, T.D.3    Valnickova, Z.4    Højrup, P.5    Crapo, J.D.6
  • 11
    • 0028967256 scopus 로고
    • A site-directed mutant of Cu, Zn-superoxide dismutase modeled after native extracellular superoxide dismutase
    • Gao B, Flores SC, McCord JM (1995) A site-directed mutant of Cu, Zn-superoxide dismutase modeled after native extracellular superoxide dismutase. Biol Trace Elem Res 47:95-100
    • (1995) Biol Trace Elem Res , vol.47 , pp. 95-100
    • Gao, B.1    Flores, S.C.2    McCord, J.M.3
  • 13
    • 84857644147 scopus 로고    scopus 로고
    • Overexpression of extracellular superoxide dismutase has a protective role against hyperoxia-induced brain injury in neonatal mice
    • Zaghloul N, Nasim M, Patel H, Codipilly C, Marambaud P, Dewey S, Schiffer WK, Ahmed M (2012) Overexpression of extracellular superoxide dismutase has a protective role against hyperoxia-induced brain injury in neonatal mice. FEBS J 279:871-881
    • (2012) FEBS J , vol.279 , pp. 871-881
    • Zaghloul, N.1    Nasim, M.2    Patel, H.3    Codipilly, C.4    Marambaud, P.5    Dewey, S.6    Schiffer, W.K.7    Ahmed, M.8
  • 14
    • 0032931698 scopus 로고    scopus 로고
    • Astrocytes enhance radical defense in capillary endothelial cells constituting the blood-brain barrier
    • Schroeter ML, Mertsch K, Giese H, Muller S, Sporbert A, Hickel B, Blasig IE (1999) Astrocytes enhance radical defense in capillary endothelial cells constituting the blood-brain barrier. FEBS Lett 449:241-244
    • (1999) FEBS Lett , vol.449 , pp. 241-244
    • Schroeter, M.L.1    Mertsch, K.2    Giese, H.3    Muller, S.4    Sporbert, A.5    Hickel, B.6    Blasig, I.E.7
  • 15
    • 0031465419 scopus 로고    scopus 로고
    • Antioxidant defense of the brain : A role for astrocyte
    • Wilson JX (1997) Antioxidant defense of the brain : a role for astrocyte. Can J Physiol Pharmacol 75:1149-1163
    • (1997) Can J Physiol Pharmacol , vol.75 , pp. 1149-1163
    • Wilson, J.X.1
  • 16
    • 0036826902 scopus 로고    scopus 로고
    • Preservation of extracellular glutathione by astrocyte derived factor with properties comparable to extracellular superoxide dismutase
    • Stewart VC, Stone R, Gegg ME, Sharpe MA, Hurst RD, Clark JB, Heales SJR (2002) Preservation of extracellular glutathione by astrocyte derived factor with properties comparable to extracellular superoxide dismutase. J Neurochem 83:984-991
    • (2002) J Neurochem , vol.83 , pp. 984-991
    • Stewart, V.C.1    Stone, R.2    Gegg, M.E.3    Sharpe, M.A.4    Hurst, R.D.5    Clark, J.B.6    Heales, S.J.R.7
  • 17
    • 0026654239 scopus 로고
    • Release of excitatory amino acids from cultured hippocampal astrocytes induced by a hypoxic-hypoglycemic stimulation
    • Ogata T, Nakamura Y, Shibata T, Kataoka K (1992) Release of excitatory amino acids from cultured hippocampal astrocytes induced by a hypoxic-hypoglycemic stimulation. J Neurochem 58:1957-1959
    • (1992) J Neurochem , vol.58 , pp. 1957-1959
    • Ogata, T.1    Nakamura, Y.2    Shibata, T.3    Kataoka, K.4
  • 18
    • 0019121308 scopus 로고
    • Effect of striatal cells on in vitro maturation of mesencephalic dopaminergic neurones grown in serum-free conditions
    • di Porzio U, Daguet M-D, Glowinski J, Prochiantz A (1980) Effect of striatal cells on in vitro maturation of mesencephalic dopaminergic neurones grown in serum-free conditions. Nature 288:370-373
    • (1980) Nature , vol.288 , pp. 370-373
    • Di Porzio, U.1    Daguet, M.-D.2    Glowinski, J.3    Prochiantz, A.4
  • 19
    • 0030007344 scopus 로고    scopus 로고
    • Adenosine and propentfylline inhibit the proliferation of culture microglia cells
    • Si QS, Nakamura Y, Schubert P, Rudolphi K, Kataoka K (1996) Adenosine and propentfylline inhibit the proliferation of culture microglia cells. Exp Neurol 137:345-349
    • (1996) Exp Neurol , vol.137 , pp. 345-349
    • Si, Q.S.1    Nakamura, Y.2    Schubert, P.3    Rudolphi, K.4    Kataoka, K.5
  • 20
    • 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 (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Anal Biochem 72:248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 21
    • 0027365777 scopus 로고
    • An immunohistochemical study of copper/zinc superoxide dismutase and manganese superoxide dismutase in rat hippocampus after transient cerebral ischemia
    • Liu XH, Kato H, Nakata N, Kogure K, Kato K (1993) An immunohistochemical study of copper/zinc superoxide dismutase and manganese superoxide dismutase in rat hippocampus after transient cerebral ischemia. Brain Res 625:29-37
    • (1993) Brain Res , vol.625 , pp. 29-37
    • Liu, X.H.1    Kato, H.2    Nakata, N.3    Kogure, K.4    Kato, K.5
  • 22
    • 0031753798 scopus 로고    scopus 로고
    • Amyloid b-peptide (1-40)-mediated oxidative stress in cultured hippocampal neurons. Protein carbonyl formation, CK BB expression, and the level of Cu, Zn, and Mn SOD mRNA
    • Aksenov MY, Aksenova MV, Markesbery WR, Butterfield DA (1998) Amyloid b-peptide (1-40)-mediated oxidative stress in cultured hippocampal neurons. Protein carbonyl formation, CK BB expression, and the level of Cu, Zn, and Mn SOD mRNA. J Mol Neurosci 10:181-192
    • (1998) J Mol Neurosci , vol.10 , pp. 181-192
    • Aksenov, M.Y.1    Aksenova, M.V.2    Markesbery, W.R.3    Butterfield, D.A.4
  • 24
    • 0033548159 scopus 로고    scopus 로고
    • Effect of serum in medium on the expression of inducible nitric oxide synthase and superoxide dismutases in cultured C6 glioma cells
    • Yu W-J, Liau S-S, Chin W-T, Cheng J-T (1999) Effect of serum in medium on the expression of inducible nitric oxide synthase and superoxide dismutases in cultured C6 glioma cells. Neurosci Lett 261:37-40
    • (1999) Neurosci Lett , vol.261 , pp. 37-40
    • Yu, W.-J.1    Liau, S.-S.2    Chin, W.-T.3    Cheng, J.-T.4
  • 26
    • 18044395714 scopus 로고    scopus 로고
    • Extracellular superoxide dismutase: Structural and functional considerations of a protein shaped by two different disulfide bridge patterns
    • Petersen SV, Enghild JJ (2005) Extracellular superoxide dismutase: structural and functional considerations of a protein shaped by two different disulfide bridge patterns. Biomed Pharmacother 59:175-182
    • (2005) Biomed Pharmacother , vol.59 , pp. 175-182
    • Petersen, S.V.1    Enghild, J.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.