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Volumn 593, Issue 1-3, 2008, Pages 30-35

Antioxidant properties of argpyrimidine

Author keywords

Antioxidant; Argpyrimidine; Diabetes mellitus; Free radical; Neurodegenerative disease

Indexed keywords

1,1 DIPHENYL 2 PICRYLHYDRAZYL; ACETOXYPENTANE 2,4 DIONE; ANTIOXIDANT; ARGININE; ARGPYRIMIDINE; HYDROGEN PEROXIDE; KETONE DERIVATIVE; METAL ION; PYRIMIDINE DERIVATIVE; SUPEROXIDE;

EID: 49949107387     PISSN: 00142999     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ejphar.2008.07.030     Document Type: Article
Times cited : (16)

References (29)
  • 1
    • 3242787063 scopus 로고    scopus 로고
    • Analysis of flavonoids and other phenolic compounds using high-performance liquid chromatography with coulometric array detection: relationship to antioxidant activity
    • Aaby K., Hvattum E., and Skrede G. Analysis of flavonoids and other phenolic compounds using high-performance liquid chromatography with coulometric array detection: relationship to antioxidant activity. J. Agric. Food Chem. 52 (2004) 4595-4603
    • (2004) J. Agric. Food Chem. , vol.52 , pp. 4595-4603
    • Aaby, K.1    Hvattum, E.2    Skrede, G.3
  • 2
    • 0030919275 scopus 로고    scopus 로고
    • N-epsilon-(carboxyethyl)lysine, a product of the chemical modification of proteins by methylglyoxal, increases with age in human lens proteins
    • Ahmed M.U., Brinkmann Frye E., Degenhardt T.P., Thorpe S.R., and Baynes J.W. N-epsilon-(carboxyethyl)lysine, a product of the chemical modification of proteins by methylglyoxal, increases with age in human lens proteins. Biochem. J. 324 (1997) 565-570
    • (1997) Biochem. J. , vol.324 , pp. 565-570
    • Ahmed, M.U.1    Brinkmann Frye, E.2    Degenhardt, T.P.3    Thorpe, S.R.4    Baynes, J.W.5
  • 3
    • 14044251043 scopus 로고    scopus 로고
    • Peptide mapping identifies hotspot site of modification in human serum albumin by methylglyoxal involved in ligand binding and esterase activity
    • Ahmed N., Dobler D., Dean M., and Thornalley P.J. Peptide mapping identifies hotspot site of modification in human serum albumin by methylglyoxal involved in ligand binding and esterase activity. J. Biol. Chem. 280 (2005) 5724-5732
    • (2005) J. Biol. Chem. , vol.280 , pp. 5724-5732
    • Ahmed, N.1    Dobler, D.2    Dean, M.3    Thornalley, P.J.4
  • 4
    • 0031054249 scopus 로고    scopus 로고
    • In vitro kinetic studies of formation of antigenic advanced glycation end products (AGEs). Novel inhibition of post-Amadori glycation pathways
    • Booth A.A., Khalifah R.G., Todd P., and Hudson B.G. In vitro kinetic studies of formation of antigenic advanced glycation end products (AGEs). Novel inhibition of post-Amadori glycation pathways. J. Biol. Chem. 272 (1997) 5430-5437
    • (1997) J. Biol. Chem. , vol.272 , pp. 5430-5437
    • Booth, A.A.1    Khalifah, R.G.2    Todd, P.3    Hudson, B.G.4
  • 5
    • 0033972493 scopus 로고    scopus 로고
    • Negative consequences of glycation
    • Brownlee M. Negative consequences of glycation. Metabolism 49 (2000) 9-13
    • (2000) Metabolism , vol.49 , pp. 9-13
    • Brownlee, M.1
  • 6
    • 37049055569 scopus 로고
    • Organic oxidation processes. Part IV. The reaction of lead tetra-acetate with some carbonyl compounds
    • Cavill C.W.K., and Solomon D.H. Organic oxidation processes. Part IV. The reaction of lead tetra-acetate with some carbonyl compounds. J. Chem. Soc. (1955) 4426-4429
    • (1955) J. Chem. Soc. , pp. 4426-4429
    • Cavill, C.W.K.1    Solomon, D.H.2
  • 7
    • 0027174668 scopus 로고
    • A comparison of bathophenanthro-linedisulfonic acid and ferrozine as chelators of iron(II) in reduction reactions
    • Cowart R.E., Singleton F.L., and Hind J.S. A comparison of bathophenanthro-linedisulfonic acid and ferrozine as chelators of iron(II) in reduction reactions. Anal. Biochem. 211 (1993) 151-155
    • (1993) Anal. Biochem. , vol.211 , pp. 151-155
    • Cowart, R.E.1    Singleton, F.L.2    Hind, J.S.3
  • 8
    • 11844293406 scopus 로고    scopus 로고
    • Evaluation of the antioxidant activity of flavonoids by "ferric reducing antioxidant power" assay and cyclic voltammetry
    • Firuzi O., Lacanna A., Petrucci R., Marrosu G., and Saso L. Evaluation of the antioxidant activity of flavonoids by "ferric reducing antioxidant power" assay and cyclic voltammetry. Biochim. Biophys. Acta 1721 (2005) 174-184
    • (2005) Biochim. Biophys. Acta , vol.1721 , pp. 174-184
    • Firuzi, O.1    Lacanna, A.2    Petrucci, R.3    Marrosu, G.4    Saso, L.5
  • 10
    • 0033566287 scopus 로고    scopus 로고
    • Neurotoxicity of methylglyoxal and 3-deoxyglucosone on cultured cortical neurons: synergism between glycation and oxidative stress, possibly involved in neurodegenerative diseases
    • Kikuchi S., Shinpo K., Moriwaka F., Makita Z., Miyata T., and Tashiro K. Neurotoxicity of methylglyoxal and 3-deoxyglucosone on cultured cortical neurons: synergism between glycation and oxidative stress, possibly involved in neurodegenerative diseases. J. Neurosci. Res. 57 (1999) 280-289
    • (1999) J. Neurosci. Res. , vol.57 , pp. 280-289
    • Kikuchi, S.1    Shinpo, K.2    Moriwaka, F.3    Makita, Z.4    Miyata, T.5    Tashiro, K.6
  • 11
    • 0037414534 scopus 로고    scopus 로고
    • Abnormal solvent effects on hydrogen atom abstractions. 1. The reactions of phenols with 2,2-diphenyl-1-picrylhydrazyl (dpph*) in alcohols
    • Litwinienko G., and Ingold K.U. Abnormal solvent effects on hydrogen atom abstractions. 1. The reactions of phenols with 2,2-diphenyl-1-picrylhydrazyl (dpph*) in alcohols. J. Org. Chem. 68 (2003) 3433-3438
    • (2003) J. Org. Chem. , vol.68 , pp. 3433-3438
    • Litwinienko, G.1    Ingold, K.U.2
  • 12
    • 0000775778 scopus 로고    scopus 로고
    • Bond dissociation energies of O-H bonds in substituted phenols from equilibration studies
    • Lucarini M., Pedrielli P., and Pedulli G.F. Bond dissociation energies of O-H bonds in substituted phenols from equilibration studies. J. Org. Chem. 61 (1996) 9259-9263
    • (1996) J. Org. Chem. , vol.61 , pp. 9259-9263
    • Lucarini, M.1    Pedrielli, P.2    Pedulli, G.F.3
  • 13
  • 14
    • 0033603599 scopus 로고    scopus 로고
    • Methylglyoxal modification of protein. Chemical and immunochemical characterization of methylglyoxal-arginine adducts
    • Oya T., Hattori N., Mizuno Y., Miyata S., Maeda S., Osawa T., and Uchida K. Methylglyoxal modification of protein. Chemical and immunochemical characterization of methylglyoxal-arginine adducts. J. Biol. Chem. 274 (1999) 18492-18502
    • (1999) J. Biol. Chem. , vol.274 , pp. 18492-18502
    • Oya, T.1    Hattori, N.2    Mizuno, Y.3    Miyata, S.4    Maeda, S.5    Osawa, T.6    Uchida, K.7
  • 15
    • 0142102552 scopus 로고    scopus 로고
    • Methylglyoxal modifies heat shock protein 27 in glomerular mesangial cells
    • Padival A.K., Crabb J.W., and Nagaraj R.H. Methylglyoxal modifies heat shock protein 27 in glomerular mesangial cells. FEBS Lett. 551 (2003) 113-118
    • (2003) FEBS Lett. , vol.551 , pp. 113-118
    • Padival, A.K.1    Crabb, J.W.2    Nagaraj, R.H.3
  • 16
    • 0034810395 scopus 로고    scopus 로고
    • 5-Pyrimidinols: novel chain-breaking antioxidants more effective than phenols
    • Pratt D.A., DiLabio G.A., Brigati G., Pedulli G.F., and Valgimigli L. 5-Pyrimidinols: novel chain-breaking antioxidants more effective than phenols. J Am. Chem. Soc. 123 (2001) 4625-4626
    • (2001) J Am. Chem. Soc. , vol.123 , pp. 4625-4626
    • Pratt, D.A.1    DiLabio, G.A.2    Brigati, G.3    Pedulli, G.F.4    Valgimigli, L.5
  • 17
    • 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
  • 18
    • 0035955478 scopus 로고    scopus 로고
    • Morphological evidence for lipid peroxidation and protein glycoxidation in spinal cords from sporadic amyotrophic lateral sclerosis patients
    • Shibata N., Nagai R., Uchida K., Horiuchi S., Yamada S., Hirano A., Kawaguchi M., Yamamoto T., Sasaki S., and Kobayashi M. Morphological evidence for lipid peroxidation and protein glycoxidation in spinal cords from sporadic amyotrophic lateral sclerosis patients. Brain Res. 917 (2001) 97-104
    • (2001) Brain Res. , vol.917 , pp. 97-104
    • Shibata, N.1    Nagai, R.2    Uchida, K.3    Horiuchi, S.4    Yamada, S.5    Hirano, A.6    Kawaguchi, M.7    Yamamoto, T.8    Sasaki, S.9    Kobayashi, M.10
  • 19
    • 0031214523 scopus 로고    scopus 로고
    • Protein modification by methylglyoxal: chemical nature and synthetic mechanism of a major fluorescent adduct
    • Shipanova I.N., Glomb M.A., and Nagaraj R.H. Protein modification by methylglyoxal: chemical nature and synthetic mechanism of a major fluorescent adduct. Arch. Biochem. Biophys. 344 (1997) 29-36
    • (1997) Arch. Biochem. Biophys. , vol.344 , pp. 29-36
    • Shipanova, I.N.1    Glomb, M.A.2    Nagaraj, R.H.3
  • 20
    • 0345254972 scopus 로고    scopus 로고
    • Oxidative DNA damage and glioma cell death induced by tetrahydropapaveroline
    • Soh Y., Shin M.H., Lee J.S., Jang J.H., Kim O.H., Kang H., and Surh Y.J. Oxidative DNA damage and glioma cell death induced by tetrahydropapaveroline. Mutat. Res. 544 (2003) 129-142
    • (2003) Mutat. Res. , vol.544 , pp. 129-142
    • Soh, Y.1    Shin, M.H.2    Lee, J.S.3    Jang, J.H.4    Kim, O.H.5    Kang, H.6    Surh, Y.J.7
  • 21
    • 0029935490 scopus 로고    scopus 로고
    • Free radical scavenging activity of curcuminoids
    • Sreejayan N., and Rao M.N. Free radical scavenging activity of curcuminoids. Arzneimittelforschung 46 (1996) 169-171
    • (1996) Arzneimittelforschung , vol.46 , pp. 169-171
    • Sreejayan, N.1    Rao, M.N.2
  • 22
    • 0032124868 scopus 로고    scopus 로고
    • Effect of bile acids on lipid peroxidation: the role of iron
    • Sreejayan N., and von Ritter C. Effect of bile acids on lipid peroxidation: the role of iron. Free Radic. Biol. Med. 25 (1998) 50-56
    • (1998) Free Radic. Biol. Med. , vol.25 , pp. 50-56
    • Sreejayan, N.1    von Ritter, C.2
  • 23
    • 0032980115 scopus 로고    scopus 로고
    • Clinical significance of glycation
    • Thornalley P.J. Clinical significance of glycation. Clin. Lab. 45 (1999) 263-273
    • (1999) Clin. Lab. , vol.45 , pp. 263-273
    • Thornalley, P.J.1
  • 24
    • 0033617305 scopus 로고    scopus 로고
    • Solvent effects on the antioxidant activity of vitamin E(1)
    • Valgimigli L., Banks J.T., Lusztyk J., and Ingold K.U. Solvent effects on the antioxidant activity of vitamin E(1). J. Org. Chem. 64 (1999) 3381-3383
    • (1999) J. Org. Chem. , vol.64 , pp. 3381-3383
    • Valgimigli, L.1    Banks, J.T.2    Lusztyk, J.3    Ingold, K.U.4
  • 25
    • 23744454602 scopus 로고    scopus 로고
    • Advanced glycation end products in human cancer tissues: detection of Nepsilon-(carboxymethyl)lysine and argpyrimidine
    • van Heijst J.W., Niessen H.W., Hoekman K., and Schalkwijk C.G. Advanced glycation end products in human cancer tissues: detection of Nepsilon-(carboxymethyl)lysine and argpyrimidine. Ann. N.Y. Acad. Sci. 1043 (2005) 725-733
    • (2005) Ann. N.Y. Acad. Sci. , vol.1043 , pp. 725-733
    • van Heijst, J.W.1    Niessen, H.W.2    Hoekman, K.3    Schalkwijk, C.G.4
  • 26
    • 0032820452 scopus 로고    scopus 로고
    • Quantifying cellular oxidative stress by dichlorofluorescein assay using microplate reader
    • Wang H., and Joseph J.A. Quantifying cellular oxidative stress by dichlorofluorescein assay using microplate reader. Free Radic. Biol. Med. 27 (1999) 612-616
    • (1999) Free Radic. Biol. Med. , vol.27 , pp. 612-616
    • Wang, H.1    Joseph, J.A.2
  • 27
    • 0030893744 scopus 로고    scopus 로고
    • Methylglyoxal-modified arginine residues-a signal for receptor-mediated endocytosis and degradation of proteins by monocytic THP-1 cells
    • Westwood M.E., Argirov O.K., Abordo E.A., and Thornalley P.J. Methylglyoxal-modified arginine residues-a signal for receptor-mediated endocytosis and degradation of proteins by monocytic THP-1 cells. Biochim. Biophys. Acta 1356 (1997) 84-94
    • (1997) Biochim. Biophys. Acta , vol.1356 , pp. 84-94
    • Westwood, M.E.1    Argirov, O.K.2    Abordo, E.A.3    Thornalley, P.J.4
  • 28
    • 0035869429 scopus 로고    scopus 로고
    • Chromatographic quantification of argpyrimidine, a methylglyoxal-derived product in tissue proteins: comparison with pentosidine
    • Wilker S.C., Chellan P., Arnold B.M., and Nagaraj R.H. Chromatographic quantification of argpyrimidine, a methylglyoxal-derived product in tissue proteins: comparison with pentosidine. Anal. Biochem. 290 (2001) 353-358
    • (2001) Anal. Biochem. , vol.290 , pp. 353-358
    • Wilker, S.C.1    Chellan, P.2    Arnold, B.M.3    Nagaraj, R.H.4
  • 29
    • 14244256331 scopus 로고    scopus 로고
    • A newly synthetic chromium complex-chromium(phenylalanine)3 improves insulin responsiveness and reduces whole body glucose tolerance
    • Yang X., Palanichamy K., Ontko A.C., Rao M.N., Fang C.X., Ren J., and Sreejayan N. A newly synthetic chromium complex-chromium(phenylalanine)3 improves insulin responsiveness and reduces whole body glucose tolerance. FEBS Lett. 579 (2005) 1458-1464
    • (2005) FEBS Lett. , vol.579 , pp. 1458-1464
    • Yang, X.1    Palanichamy, K.2    Ontko, A.C.3    Rao, M.N.4    Fang, C.X.5    Ren, J.6    Sreejayan, N.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.