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Volumn 1622, Issue 2, 2003, Pages 128-132

Triosephosphates are toxic to superoxide dismutase-deficient Escherichia coli

Author keywords

Aminoguanidine; D Glyceraldehyde 3 phospate; Dihydroxyacetone phosphate; Methylglyoxal; Superoxide dismutase; Triosephosphates autoxidation

Indexed keywords

GLYCERALDEHYDE 3 PHOSPHATE; SUPEROXIDE DISMUTASE;

EID: 0038444475     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0304-4165(03)00134-X     Document Type: Article
Times cited : (9)

References (24)
  • 1
    • 0035053034 scopus 로고    scopus 로고
    • Suppression of the accumulation of triosephosphates and increased formation of methylglyoxal in human red blood cells during hyperglycaemia by thiamine in vitro
    • Thornalley P.J., Jahan I., Ng R. Suppression of the accumulation of triosephosphates and increased formation of methylglyoxal in human red blood cells during hyperglycaemia by thiamine in vitro. J. Biochem. 129:2001;543-549.
    • (2001) J. Biochem. , vol.129 , pp. 543-549
    • Thornalley, P.J.1    Jahan, I.2    Ng, R.3
  • 2
    • 0033803537 scopus 로고    scopus 로고
    • Epalrestat, an aldose reductase ihibitor, reduces the levels of Nepsilon-(carboxymethyl)lysine protein adducts and their precursors in erythrocytes from diabetic patients
    • Hamada Y., Nakamura J., Naruse K., Komori T., Kato K., Kasuya Y., Nagai R., Horiuchi S., Hotta N. Epalrestat, an aldose reductase ihibitor, reduces the levels of Nepsilon-(carboxymethyl)lysine protein adducts and their precursors in erythrocytes from diabetic patients. Diabetes Care. 23:2000;1539-1544.
    • (2000) Diabetes Care , vol.23 , pp. 1539-1544
    • Hamada, Y.1    Nakamura, J.2    Naruse, K.3    Komori, T.4    Kato, K.5    Kasuya, Y.6    Nagai, R.7    Horiuchi, S.8    Hotta, N.9
  • 3
    • 0027396022 scopus 로고
    • The formation of methylglyoxal from triose phosphates. Investigation using a specific assay for methylglyoxal
    • Phillips S.A., Thornalley P.J. The formation of methylglyoxal from triose phosphates. Investigation using a specific assay for methylglyoxal. Eur. J. Biochem. 212:1993;101-105.
    • (1993) Eur. J. Biochem. , vol.212 , pp. 101-105
    • Phillips, S.A.1    Thornalley, P.J.2
  • 4
    • 0027286747 scopus 로고
    • Mechanism for the formation of methylglyoxal from triosephosphates
    • Richard J.P. Mechanism for the formation of methylglyoxal from triosephosphates. Biochem. Soc. Trans. 21:1993;549-553.
    • (1993) Biochem. Soc. Trans. , vol.21 , pp. 549-553
    • Richard, J.P.1
  • 5
    • 0030176306 scopus 로고    scopus 로고
    • Pharmacology of methylglyoxal: Formation, modification of proteins and nucleic acids, and enzymatic detoxification - A role in pathogenesis and antiproliferative chemotherapy
    • Thornalley P.J. Pharmacology of methylglyoxal: formation, modification of proteins and nucleic acids, and enzymatic detoxification - a role in pathogenesis and antiproliferative chemotherapy. Gen. Pharmacol. 27:1996;565-573.
    • (1996) Gen. Pharmacol. , vol.27 , pp. 565-573
    • Thornalley, P.J.1
  • 6
    • 0021361665 scopus 로고
    • The autoxidation of glyceraldehyde and other simple monosaccharides under physiological conditions catalysed by buffer ions
    • Thornalley P., Wolff S., Crabbe J., Stern A. The autoxidation of glyceraldehyde and other simple monosaccharides under physiological conditions catalysed by buffer ions. Biochim. Biophys. Acta. 797:1984;276-287.
    • (1984) Biochim. Biophys. Acta , vol.797 , pp. 276-287
    • Thornalley, P.1    Wolff, S.2    Crabbe, J.3    Stern, A.4
  • 7
    • 0023333090 scopus 로고
    • Superoxide radical initiates the autoxidation of dihydroxyacetone
    • Mashino T., Fridovich I. Superoxide radical initiates the autoxidation of dihydroxyacetone. Arch. Biochem. Biophys. 254:1987;547-551.
    • (1987) Arch. Biochem. Biophys. , vol.254 , pp. 547-551
    • Mashino, T.1    Fridovich, I.2
  • 9
    • 0029041226 scopus 로고
    • Lethal oxidative damage and mutagenesis are generated by iron in delta for mutants of Escherichia coli: Protective role of superoxide dismutase
    • Touati D., Jacques M., Tardat B., Bouchard L., Despied S. Lethal oxidative damage and mutagenesis are generated by iron in delta for mutants of Escherichia coli: protective role of superoxide dismutase. J. Bacteriol. 177:1995;2305-2314.
    • (1995) J. Bacteriol. , vol.177 , pp. 2305-2314
    • Touati, D.1    Jacques, M.2    Tardat, B.3    Bouchard, L.4    Despied, S.5
  • 11
    • 0016419299 scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase from rabbit muscle-1
    • Amelunxen R.E., Carr D.O. Glyceraldehyde-3-phosphate dehydrogenase from rabbit muscle-1. Methods Enzymol. 41:1975;264-267.
    • (1975) Methods Enzymol. , vol.41 , pp. 264-267
    • Amelunxen, R.E.1    Carr, D.O.2
  • 12
    • 0030039967 scopus 로고    scopus 로고
    • Methylglyoxal assay in cells as 2-methylquinoxaline using 1,2-diaminobenzene as derivatizing reagent
    • Cordeiro C., Ponces Freire A. Methylglyoxal assay in cells as 2-methylquinoxaline using 1,2-diaminobenzene as derivatizing reagent. Anal. Biochem. 234:1996;221-224.
    • (1996) Anal. Biochem. , vol.234 , pp. 221-224
    • Cordeiro, C.1    Ponces Freire, A.2
  • 14
    • 0001298780 scopus 로고
    • Oxygen-dependent mutagenesis in Escherichia coli lacking superoxide dismutase
    • Farr S.B., D'Ari R., Touati D. Oxygen-dependent mutagenesis in Escherichia coli lacking superoxide dismutase. Proc. Natl. Acad. Sci. U. S. A. 83:1986;8268-8272.
    • (1986) Proc. Natl. Acad. Sci. U. S. A. , vol.83 , pp. 8268-8272
    • Farr, S.B.1    D'Ari, R.2    Touati, D.3
  • 15
    • 0024469795 scopus 로고
    • Cytogenetic response to 1,2-dicarbonyls and hydrogen peroxide in Chinese hamster ovary AUXB1 cells and human peripheral lymphocytes
    • Tucker J.D., Taylor R.T., Christensen M.L., Strout C.L., Hanna M.L., Carrano A.V. Cytogenetic response to 1,2-dicarbonyls and hydrogen peroxide in Chinese hamster ovary AUXB1 cells and human peripheral lymphocytes. Mutat. Res. 224:1989;269-279.
    • (1989) Mutat. Res. , vol.224 , pp. 269-279
    • Tucker, J.D.1    Taylor, R.T.2    Christensen, M.L.3    Strout, C.L.4    Hanna, M.L.5    Carrano, A.V.6
  • 16
    • 0030914358 scopus 로고    scopus 로고
    • Types of mutations induced by glyoxal, a major oxidative DNA-damage product, in Salmonella typhimurium
    • Murata-Kamiya N., Kaji H., Kasai H. Types of mutations induced by glyoxal, a major oxidative DNA-damage product, in Salmonella typhimurium. Mutat. Res. 377:1997;13-16.
    • (1997) Mutat. Res. , vol.377 , pp. 13-16
    • Murata-Kamiya, N.1    Kaji, H.2    Kasai, H.3
  • 17
    • 0034632250 scopus 로고    scopus 로고
    • Methylglyoxal induces G:C to C:G and G:C to T:A transversions in the supF gene on a shuttle vector plasmid replicated in mammalian cells
    • Murata-Kamiya N., Kamiya H., Kaji H., Kasai H. Methylglyoxal induces G:C to C:G and G:C to T:A transversions in the supF gene on a shuttle vector plasmid replicated in mammalian cells. Mutat. Res. 468:2000;173-182.
    • (2000) Mutat. Res. , vol.468 , pp. 173-182
    • Murata-Kamiya, N.1    Kamiya, H.2    Kaji, H.3    Kasai, H.4
  • 20
    • 0032032578 scopus 로고    scopus 로고
    • Overexpression of glyoxalase-I in bovine endothelial cells inhibits intracellular advanced glycation endproduct formation and prevents hyperglycemia-induced increases in macromolecular endocytosis
    • Shinohara M., Thornalley P.J., Giardino I., Beisswenger P., Thorpe S.R., Onorato J., Brownlee M. Overexpression of glyoxalase-I in bovine endothelial cells inhibits intracellular advanced glycation endproduct formation and prevents hyperglycemia-induced increases in macromolecular endocytosis. J. Clin. Invest. 101:1998;1142-1147.
    • (1998) J. Clin. Invest. , vol.101 , pp. 1142-1147
    • Shinohara, M.1    Thornalley, P.J.2    Giardino, I.3    Beisswenger, P.4    Thorpe, S.R.5    Onorato, J.6    Brownlee, M.7
  • 21
    • 18144453930 scopus 로고    scopus 로고
    • Inhibition of glyceraldehyde-3-phosphate dehydrogenase in post-ischaemic myocardium
    • Knight R.J., Kofoed K.F., Schelbert H.R., Buxton D.B. Inhibition of glyceraldehyde-3-phosphate dehydrogenase in post-ischaemic myocardium. Cardiovasc. Res. 32:1996;1016-1023.
    • (1996) Cardiovasc. Res. , vol.32 , pp. 1016-1023
    • Knight, R.J.1    Kofoed, K.F.2    Schelbert, H.R.3    Buxton, D.B.4
  • 22
    • 0034710891 scopus 로고    scopus 로고
    • Hyperglycemia-induced mitochondrial superoxide overproduction activates the hexosamine pathway and induces plasminogen activator inhibitor-1 expression by increasing Sp1 glycosylation
    • Du X.L., Edelstein D., Rossetti L., Fantus I.G., Goldberg H., Ziyadeh F., Wu J., Brownlee M. Hyperglycemia-induced mitochondrial superoxide overproduction activates the hexosamine pathway and induces plasminogen activator inhibitor-1 expression by increasing Sp1 glycosylation. Proc. Natl. Acad. Sci. U. S. A. 97:2000;12222-12226.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 12222-12226
    • Du, X.L.1    Edelstein, D.2    Rossetti, L.3    Fantus, I.G.4    Goldberg, H.5    Ziyadeh, F.6    Wu, J.7    Brownlee, M.8
  • 23
    • 0028934990 scopus 로고
    • Mechanism of protein modification by glyoxal and glycolaldehyde, reactive intermediates of the Maillard reaction
    • Glomb M.A., Monnier V.M. Mechanism of protein modification by glyoxal and glycolaldehyde, reactive intermediates of the Maillard reaction. J. Biol. Chem. 270:1995;10017-10026.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10017-10026
    • Glomb, M.A.1    Monnier, V.M.2
  • 24
    • 0019322413 scopus 로고
    • The effect of methylglyoxal on the glycolytic enzymes
    • Leoncini G., Maresca M., Bonsignore A. The effect of methylglyoxal on the glycolytic enzymes. FEBS Lett. 117:1980;17-18.
    • (1980) FEBS Lett. , vol.117 , pp. 17-18
    • Leoncini, G.1    Maresca, M.2    Bonsignore, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.