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Volumn 25, Issue 4-5, 1998, Pages 554-560

Oxidative damage to sarcoplasmic reticulum Ca2+-ATPase at submicromolar iron concentrations: Evidence for metalcatalyzed oxidation

Author keywords

ATPase; Fenton reaction; Free radical; Iron overload; Oxidative damage; Oxidative stress; Sarcoplasmic reticulum

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM); ADENOSINE TRIPHOSPHATE; ASCORBIC ACID; BUTYLCRESOL; CALCIUM; DIMETHYL SULFOXIDE; DITHIOTHREITOL; HYDROGEN PEROXIDE; IRON; MANNITOL; METAL; REACTIVE OXYGEN METABOLITE; SCAVENGER;

EID: 0032171640     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0891-5849(98)00084-7     Document Type: Article
Times cited : (66)

References (38)
  • 2
    • 0025242698 scopus 로고
    • Review of the current status of calcium and thiols in cell injury
    • Reed D.J. Review of the current status of calcium and thiols in cell injury. Chem. Res. Toxicol. 3:1990;495-502.
    • (1990) Chem. Res. Toxicol. , vol.3 , pp. 495-502
    • Reed, D.J.1
  • 4
    • 0024979877 scopus 로고
    • Role of water in the energy of hydrolysis of phosphate compounds - Energy transduction in biological membranes
    • de Meis L. Role of water in the energy of hydrolysis of phosphate compounds - Energy transduction in biological membranes. Biochim. Biophys. Acta. 973:1989;333-349.
    • (1989) Biochim. Biophys. Acta , vol.973 , pp. 333-349
    • De Meis, L.1
  • 6
  • 8
    • 0025674536 scopus 로고
    • Metal ion-catalyzed oxidation of proteins: Biochemical mechanism and biological consequences
    • Stadtman E.R. Metal ion-catalyzed oxidation of proteins Biochemical mechanism and biological consequences . Free Radic. Biol. Med. 9:1990;315-325.
    • (1990) Free Radic. Biol. Med. , vol.9 , pp. 315-325
    • Stadtman, E.R.1
  • 9
    • 0025911829 scopus 로고
    • Metal-catalyzed oxidation of proteins
    • Stadtman E.R., Oliver C.N. Metal-catalyzed oxidation of proteins. J. Biol. Chem. 266:1991;2005-2008.
    • (1991) J. Biol. Chem. , vol.266 , pp. 2005-2008
    • Stadtman, E.R.1    Oliver, C.N.2
  • 10
    • 0027183423 scopus 로고
    • Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions
    • Stadtman E.R. Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions. Ann. Rev. Biochem. 62:1993;797-821.
    • (1993) Ann. Rev. Biochem. , vol.62 , pp. 797-821
    • Stadtman, E.R.1
  • 11
    • 0015218365 scopus 로고
    • 2+ uptake in skeletal muscle microsomes
    • 2+ uptake in skeletal muscle microsomes. J. Biol. Chem. 246:1971;4759-4763.
    • (1971) J. Biol. Chem. , vol.246 , pp. 4759-4763
    • De Meis, L.1    Hasselbach, W.2
  • 12
    • 0001603503 scopus 로고
    • Regulation of steady state filling in sarcophasmic reticulum
    • Grubmeyer C., Penefsky H.S. Regulation of steady state filling in sarcophasmic reticulum. J. Biol. Chem. 264:1981;5929-5936.
    • (1981) J. Biol. Chem. , vol.264 , pp. 5929-5936
    • Grubmeyer, C.1    Penefsky, H.S.2
  • 13
    • 0018733531 scopus 로고
    • Calculation programs for computing the composition of the solutions containing multiple metals and ligands used for experiments in skinned muscle cells
    • Fabiato A., Fabiato F. Calculation programs for computing the composition of the solutions containing multiple metals and ligands used for experiments in skinned muscle cells. J. Physiol. (Paris). 75:1979;463-505.
    • (1979) J. Physiol. (Paris) , vol.75 , pp. 463-505
    • Fabiato, A.1    Fabiato, F.2
  • 16
    • 0023219256 scopus 로고
    • The deoxyribose method: A simple "test-tube" assay for determination of rate constants for reactions of hydroxyl radicals
    • Halliwell B., Gutteridge J.M.C., Aruoma O.I. The deoxyribose method a simple "test-tube" assay for determination of rate constants for reactions of hydroxyl radicals . Anal. Biochem. 165:1987;215-219.
    • (1987) Anal. Biochem. , vol.165 , pp. 215-219
    • Halliwell, B.1    Gutteridge, J.M.C.2    Aruoma, O.I.3
  • 18
    • 0017872475 scopus 로고
    • Microssomal lipid peroxidation
    • S. Fleischer, Packer L. New York: Academic Press
    • Buege J.A., Aust S.D. Microssomal lipid peroxidation. Fleischer S., Packer L. Methods in enzymology. Vol. 52:1978;302-310 Academic Press, New York.
    • (1978) Methods in Enzymology , vol.52 , pp. 302-310
    • Buege, J.A.1    Aust, S.D.2
  • 20
    • 0017368372 scopus 로고
    • 2+-dependent effect of ATP on spin-labeled sarcoplasmic reticulum
    • 2+-dependent effect of ATP on spin-labeled sarcoplasmic reticulum. J. Biol. Chem. 252:1977;3044-3049.
    • (1977) J. Biol. Chem. , vol.252 , pp. 3044-3049
    • Coan, C.R.1    Inesi, G.2
  • 21
    • 0018117204 scopus 로고
    • 2+-ATPase of the sarcoplasmic reticulum
    • 2+-ATPase of the sarcoplasmic reticulum. J. Biol. Chem. 253:1978;6801-6807.
    • (1978) J. Biol. Chem. , vol.253 , pp. 6801-6807
    • Yamada, S.1    Ikemoto, N.2
  • 27
    • 0000302143 scopus 로고
    • Reaction mechanisms in the radiolysis of peptides, polypeptides, and proteins
    • Garrison W.M. Reaction mechanisms in the radiolysis of peptides, polypeptides, and proteins. Chem. Rev. 87:1987;381-398.
    • (1987) Chem. Rev. , vol.87 , pp. 381-398
    • Garrison, W.M.1
  • 28
    • 0021368004 scopus 로고
    • Oxygen effect in radiolysis of proteins: Part 2. Bovine serum albumin
    • Schuessler H., Schilling K. Oxygen effect in radiolysis of proteins Part 2. Bovine serum albumin . Int. J. Radiat. Biol. 45:1984;267-281.
    • (1984) Int. J. Radiat. Biol. , vol.45 , pp. 267-281
    • Schuessler, H.1    Schilling, K.2
  • 29
    • 0023655369 scopus 로고
    • Protein damage and degradation by oxygen radicals: I. General aspects
    • Davies K.J.A. Protein damage and degradation by oxygen radicals I. General aspects . J. Biol. Chem. 262:1987;9895-9901.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9895-9901
    • Davies, K.J.A.1
  • 30
    • 0023655531 scopus 로고
    • Protein damage and degradation by oxygen radicals: III. Modification of secondary and tertiary structure
    • Davies K.J.A., Delsignore M.E. Protein damage and degradation by oxygen radicals III. Modification of secondary and tertiary structure . J. Biol. Chem. 262:1987;9908-9913.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9908-9913
    • Davies, K.J.A.1    Delsignore, M.E.2
  • 31
    • 0027146667 scopus 로고
    • Oxidative polypeptide cleavage mediated by EDTA-Fe covalently linked to cysteine residues
    • Platis I.E., Ermacora M.R., Fox R.O. Oxidative polypeptide cleavage mediated by EDTA-Fe covalently linked to cysteine residues. Biochemistry. 32:1993;12761-12767.
    • (1993) Biochemistry , vol.32 , pp. 12761-12767
    • Platis, I.E.1    Ermacora, M.R.2    Fox, R.O.3
  • 32
    • 0025316509 scopus 로고
    • A novel mechanism for oxidative cleavage of prolyl peptides induced by the hydroxyl radical
    • Uchida K., Kato Y., Kawakishi S. A novel mechanism for oxidative cleavage of prolyl peptides induced by the hydroxyl radical. Biochem. Biophys. Res. Commun. 169:1990;265-271.
    • (1990) Biochem. Biophys. Res. Commun. , vol.169 , pp. 265-271
    • Uchida, K.1    Kato, Y.2    Kawakishi, S.3
  • 34
    • 0029859988 scopus 로고    scopus 로고
    • 2+-pump dysfunction in rat cardiomyocytes briefly exposed to hydroxyl radicals
    • 2+-pump dysfunction in rat cardiomyocytes briefly exposed to hydroxyl radicals. Free Radic. Biol. Med. 22:1997;37-47.
    • (1997) Free Radic. Biol. Med. , vol.22 , pp. 37-47
    • Morris, T.E.1    Sulakhe, P.V.2
  • 35
    • 0025157647 scopus 로고
    • The pathology of iron overload: A free radical-mediated process?
    • Bacon B.R., Britton R.S. The pathology of iron overload a free radical-mediated process? Hepatology. 11:1990;127-137.
    • (1990) Hepatology , vol.11 , pp. 127-137
    • Bacon, B.R.1    Britton, R.S.2
  • 36
    • 0026472376 scopus 로고
    • Iron metabolism - New perspectives in view
    • Crichton R.R., Ward R.J. Iron metabolism - New perspectives in view. Biochemistry. 31:1992;11256-11264.
    • (1992) Biochemistry , vol.31 , pp. 11256-11264
    • Crichton, R.R.1    Ward, R.J.2
  • 37
    • 0028630777 scopus 로고
    • Tissue iron overload and mechanisms of iron-catalyzed oxidative injury
    • Lesnefsky E.J. Tissue iron overload and mechanisms of iron-catalyzed oxidative injury. Adv. Exp. Med. Biol. 366:1994;129-146.
    • (1994) Adv. Exp. Med. Biol. , vol.366 , pp. 129-146
    • Lesnefsky, E.J.1
  • 38
    • 0025292743 scopus 로고
    • Mechanisms by which mitochondria transport calcium
    • Gunter T.E., Pfeiffer D.R. Mechanisms by which mitochondria transport calcium. Am. J. Physiol. 258:(Cell Physiol. 27):1990;C755-C786.
    • (1990) Am. J. Physiol. , vol.258 , Issue.CELL PHYSIOL. 27
    • Gunter, T.E.1    Pfeiffer, D.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.