메뉴 건너뛰기




Volumn 66, Issue 1, 2002, Pages 36-43

Effect of carnosine and related compounds on the inactivation of human Cu, Zn-superoxide dismutase by modification of fructose and glycolaldehyde

Author keywords

Carnosine; Fructose; Glycation; Glycolaldehyde; SOD

Indexed keywords

ACETALDEHYDE; ALANYLHISTIDINE; ANSERINE; CARNOSINE; DIPEPTIDE; DRUG DERIVATIVE; FRUCTOSE; GLYCOLALDEHYDE; GLYCYLHISTIDINE; HISTIDINE; HOMOCARNOSINE; HYDROXYL RADICAL; SCAVENGER; SUPEROXIDE DISMUTASE;

EID: 0036366273     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.66.36     Document Type: Article
Times cited : (51)

References (36)
  • 1
    • 0021782568 scopus 로고
    • Nonenzymatic covalent posttransla-tional modification of proteins
    • Harding, J. J., Nonenzymatic covalent posttransla-tional modification of proteins in vivo. Adv. Protein Chem., 37, 248-334 (1985).
    • (1985) In Vivo. Adv. Protein Chem. , vol.37 , pp. 248-334
    • Harding, J.J.1
  • 2
    • 0025732948 scopus 로고
    • Role of oxidative stress in development of complications in diabetes
    • Baynes, J. W., Role of oxidative stress in development of complications in diabetes. Diabetes, 40, 405-412 (1991).
    • (1991) Diabetes , vol.40 , pp. 405-412
    • Baynes, J.W.1
  • 3
    • 0019363254 scopus 로고
    • The biochemistry of the complications of diabetes mellitus
    • Brownlee, M. and Cerami, A., The biochemistry of the complications of diabetes mellitus. Annu. Rev. Biochem., 50, 385-431 (1981).
    • (1981) Annu. Rev. Biochem. , vol.50 , pp. 385-431
    • Brownlee, M.1    Cerami, A.2
  • 4
    • 0027253061 scopus 로고
    • Long-term complications of diabetes mellitus
    • Nathan, D. M., Long-term complications of diabetes mellitus. N. Engl. J. Med., 328, 1676-1685 (1993).
    • (1993) N. Engl. J. Med. , vol.328 , pp. 1676-1685
    • Nathan, D.M.1
  • 7
    • 0019475899 scopus 로고
    • Nonenzymatic browning in vivo: Possible process for aging of long-lived proteins
    • Monnier, V. M. and Cerami, A., Nonenzymatic browning in vivo: possible process for aging of long-lived proteins. Science, 211, 491-493 (1981).
    • (1981) Science , vol.211 , pp. 491-493
    • Monnier, V.M.1    Cerami, A.2
  • 9
    • 0028453652 scopus 로고
    • Glycation and diabetic complications
    • Brownlee, M., Glycation and diabetic complications. Diabetes, 43, 836-841 (1994).
    • (1994) Diabetes , vol.43 , pp. 836-841
    • Brownlee, M.1
  • 10
    • 0001302366 scopus 로고
    • EPR spin-trapping studies of the hydroxyl radical scavenging activity of carnosine and related dipeptides
    • Chan, W. K. M., Decker, E. A., Lee, J. B., and Butterfield, D. A., EPR spin-trapping studies of the hydroxyl radical scavenging activity of carnosine and related dipeptides. J. Agric. Food Chem., 42, 1407-1410 (1994).
    • (1994) J. Agric. Food Chem. , vol.42 , pp. 1407-1410
    • Chan, W.K.M.1    Decker, E.A.2    Lee, J.B.3    Butterfield, D.A.4
  • 11
    • 0023221558 scopus 로고
    • Increase in the glucosylated form of erythrocyte Cu, Zn-superoxide dismutase in diabetes and close association of the nonenzymatic glucosyla-tion with the enzyme activity
    • Arai, K., Iizuka, S., Toda, Y., Oikawa, K., and Taniguchi, N., Increase in the glucosylated form of erythrocyte Cu, Zn-superoxide dismutase in diabetes and close association of the nonenzymatic glucosyla-tion with the enzyme activity. Biochim. Biophys. Acta, 924, 292-296 (1987).
    • (1987) Biochim. Biophys. Acta , vol.924 , pp. 292-296
    • Arai, K.1    Iizuka, S.2    Toda, Y.3    Oikawa, K.4    Taniguchi, N.5
  • 12
    • 0026044928 scopus 로고
    • Sites of glycation of human and horse liver alcohol dehydrogenase in vivo
    • Shilton, B. H. and Walton, D. J., Sites of glycation of human and horse liver alcohol dehydrogenase in vivo. J. Biol. Chem., 266, 5587-5592 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 5587-5592
    • Shilton, B.H.1    Walton, D.J.2
  • 13
    • 0033032135 scopus 로고    scopus 로고
    • Relative quantification of glycated Cu, Zn-superoxide dismutase in erythrocytes by electrospray ionization mass spectrometry
    • Sarawathi, M., Nakanishi, T., and Shimizu, A., Relative quantification of glycated Cu, Zn-superoxide dismutase in erythrocytes by electrospray ionization mass spectrometry. Biochim. Biophys. Acta, 1426, 483-490 (1999).
    • (1999) Biochim. Biophys. Acta , vol.1426 , pp. 483-490
    • Sarawathi, M.1    Nakanishi, T.2    Shimizu, A.3
  • 14
    • 0030694740 scopus 로고    scopus 로고
    • Glycation-induced inactivation and loss of antigenicity of catalase and superoxide dismutase
    • Yan, H. and Harding, J., Glycation-induced inactivation and loss of antigenicity of catalase and superoxide dismutase. Biochem. J., 328, 599-605 (1997).
    • (1997) Biochem. J. , vol.328 , pp. 599-605
    • Yan, H.1    Harding, J.2
  • 15
    • 0023582040 scopus 로고
    • Glycation and inactivation of human Cu, Zn-superoxide dismutase. Identification of the in vitro glycated sites
    • Arai, K., Maguchi, S., Fujii, S., Ishibashi, H., Oikawa, K., and Taniguchi, N., Glycation and inactivation of human Cu, Zn-superoxide dismutase. Identification of the in vitro glycated sites. J. Biol. Chem., 262, 16969-16972 (1987).
    • (1987) J. Biol. Chem. , vol.262 , pp. 16969-16972
    • Arai, K.1    Maguchi, S.2    Fujii, S.3    Ishibashi, H.4    Oikawa, K.5    Taniguchi, N.6
  • 16
    • 0026732669 scopus 로고
    • Site-specific and random fragmentation of Cu, Zn-superoxide dismutase by glycation reaction
    • Ookawara, T., Kawamura, N., Kitagawa, Y., and Taniguchi, N., Site-specific and random fragmentation of Cu, Zn-superoxide dismutase by glycation reaction. J. Biol. Chem., 267, 18505-18510 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 18505-18510
    • Ookawara, T.1    Kawamura, N.2    Kitagawa, Y.3    Taniguchi, N.4
  • 17
    • 0031305769 scopus 로고    scopus 로고
    • Inactivation of Cu, Zn-superoxide dismutase by intermediates of Maillard reaction and glycolytic pathways and some sugars
    • Ukeda, H., Hasegawa, Y., Ishii, T., and Sawamura, M., Inactivation of Cu, Zn-superoxide dismutase by intermediates of Maillard reaction and glycolytic pathways and some sugars. Biosci. Biotechnol. Biochem., 61, 2039-2042 (1997).
    • (1997) Biosci. Biotechnol. Biochem. , vol.61 , pp. 2039-2042
    • Ukeda, H.1    Hasegawa, Y.2    Ishii, T.3    Sawamura, M.4
  • 18
    • 0344158770 scopus 로고
    • Antioxidant activity of carnosine, homocarno-sine, and anserine present in muscle and brain
    • Kohen, R., Yamamoto, Y., Cundy, K.C., and Ames, B. N., Antioxidant activity of carnosine, homocarno-sine, and anserine present in muscle and brain. Proc. Natl. Acad. Sci. U.S.A., 85, 3175-3179 (1988).
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 3175-3179
    • Kohen, R.1    Yamamoto, Y.2    Cundy, K.C.3    Ames, B.N.4
  • 19
    • 0019364820 scopus 로고
    • Interactions among carnosine, anserine, ophidine and copper in biochemical adaptation
    • Brown, C. E., Interactions among carnosine, anserine, ophidine and copper in biochemical adaptation. J. Theor. Biol., 88, 245-256 (1981).
    • (1981) J. Theor. Biol. , vol.88 , pp. 245-256
    • Brown, C.E.1
  • 20
    • 0019165526 scopus 로고
    • Myocardial protection by a carnosine-buffered cardioplegic solution
    • Gercken, G., Bischoff, H., and Trotz, M., Myocardial protection by a carnosine-buffered cardioplegic solution. Arzneimittelforschung, 30, 2140-2143 (1980).
    • (1980) Arzneimittelforschung , vol.30 , pp. 2140-2143
    • Gercken, G.1    Bischoff, H.2    Trotz, M.3
  • 21
    • 0032699972 scopus 로고    scopus 로고
    • Hydrogen peroxide-mediated Cu, Zn-superoxide dismutase fragmentation: Protection by carnosine, homocarnosine and anserine
    • Choi, S. Y., Kwon, H. Y., Kwon, O. B., and Kang, J. H., Hydrogen peroxide-mediated Cu, Zn-superoxide dismutase fragmentation: protection by carnosine, homocarnosine and anserine. Biochim. Biophys. Acta, 1472, 651-657 (1999).
    • (1999) Biochim. Biophys. Acta , vol.1472 , pp. 651-657
    • Choi, S.Y.1    Kwon, H.Y.2    Kwon, O.B.3    Kang, J.H.4
  • 22
    • 0031554917 scopus 로고    scopus 로고
    • Spectrophotometric assay for superoxide dismutase based on tetrazolium salt 3'-{1-[(Phenylamino)-carbonyl]-3,4-tetrazolium}-bis(4-methoxy-6-nitro) benzenesulfonic acid hydrate reduction by xanthine-xanthine oxidase
    • Ukeda, H., Maeda, S., Ishii, T., and Sawamura, M., Spectrophotometric assay for superoxide dismutase based on tetrazolium salt 3'-{1-[(phenylamino)-carbonyl]-3,4-tetrazolium}-bis(4-methoxy-6-nitro) benzenesulfonic acid hydrate reduction by xanthine-xanthine oxidase. Anal. Biochem., 251, 206-209 (1997).
    • (1997) Anal. Biochem. , vol.251 , pp. 206-209
    • Ukeda, H.1    Maeda, S.2    Ishii, T.3    Sawamura, M.4
  • 23
    • 85007943457 scopus 로고
    • Enzymatic production of glyoxal from ethylene glycol using alcohol oxidase from methanol yeast
    • Isobe, K. and Nishise, H., Enzymatic production of glyoxal from ethylene glycol using alcohol oxidase from methanol yeast. Biosci. Biotechnol. Biochem., 58, 170-173 (1994).
    • (1994) Biosci. Biotechnol. Biochem. , vol.58 , pp. 170-173
    • Isobe, K.1    Nishise, H.2
  • 24
    • 0001462340 scopus 로고    scopus 로고
    • Immobilized enzyme-based microtiter plate assay for glucose in foods
    • Ukeda, H., Fujita, Y., Ohira, M., and Sawamura, M., Immobilized enzyme-based microtiter plate assay for glucose in foods. J. Agric. Food Chem., 44, 3858-3863 (1996).
    • (1996) J. Agric. Food Chem. , vol.44 , pp. 3858-3863
    • Ukeda, H.1    Fujita, Y.2    Ohira, M.3    Sawamura, M.4
  • 25
    • 0025293777 scopus 로고
    • Hydrogen peroxide production during experimental protein glycation
    • Jiang, Z.-Y., Woollard, A. C. S., and Wolff, S. P., Hydrogen peroxide production during experimental protein glycation. FEBS Lett., 268, 69-71 (1990).
    • (1990) FEBS Lett. , vol.268 , pp. 69-71
    • Jiang, Z.-Y.1    Woollard, A.C.S.2    Wolff, S.P.3
  • 26
    • 0023219256 scopus 로고
    • The deoxyribose method: A simple “test-tube” assay for determination of rate constants for reaction of hydroxyl radical
    • Halliwell, B., Gutteridge, J. M. C., and Auroma, O. I., The deoxyribose method: a simple “test-tube” assay for determination of rate constants for reaction of hydroxyl radical. Anal. Biochem., 165, 215-219 (1987).
    • (1987) Anal. Biochem. , vol.165 , pp. 215-219
    • Halliwell, B.1    Gutteridge, J.M.C.2    Auroma, O.I.3
  • 27
    • 0030854261 scopus 로고    scopus 로고
    • Human neutrophils employ the my-eloperoxidase-hydrogen peroxide-chloride system to convert hydroxy-amino acids into glycolaldehyde, 2-hydroxypropanol, and acrolein
    • Anderson, M. M., Hazen, S. L., Hsu, F. F., and Heinecke, J. W., Human neutrophils employ the my-eloperoxidase-hydrogen peroxide-chloride system to convert hydroxy-amino acids into glycolaldehyde, 2-hydroxypropanol, and acrolein. J. Clin. Invest., 99, 424-432 (1997).
    • (1997) J. Clin. Invest. , vol.99 , pp. 424-432
    • Erson, M.M.1    Hazen, S.L.2    Hsu, F.F.3    Heinecke, J.W.4
  • 28
    • 0029781438 scopus 로고    scopus 로고
    • Generation of glycolaldehyde from guinea pig airway epithelial monolayers exposed to nitrogen dioxide and its effect on sodium pump activity
    • Robinson, T. W., Zhou, H., and Kim, K., Generation of glycolaldehyde from guinea pig airway epithelial monolayers exposed to nitrogen dioxide and its effect on sodium pump activity. J. Environ. Health Perspect., 104, 852-856 (1996).
    • (1996) J. Environ. Health Perspect. , vol.104 , pp. 852-856
    • Robinson, T.W.1    Zhou, H.2    Kim, K.3
  • 29
    • 0030061123 scopus 로고    scopus 로고
    • Mixed dimers formed by crosslinking of native and glycated proteins in the absence of free sugars
    • Liggins, J. and Furth, A. J., Mixed dimers formed by crosslinking of native and glycated proteins in the absence of free sugars. Biochem. Biophys. Res. Commun., 219, 186-190 (1996).
    • (1996) Biochem. Biophys. Res. Commun. , vol.219 , pp. 186-190
    • Liggins, J.1    Furth, A.J.2
  • 30
    • 0026731769 scopus 로고
    • Failure of common glycation assays to detect glycation by fructose
    • Ahmed, N. and Furth, A., Failure of common glycation assays to detect glycation by fructose. J. Clin. Chem., 38, 1301-1303 (1992).
    • (1992) J. Clin. Chem. , vol.38 , pp. 1301-1303
    • Ahmed, N.1    Furth, A.2
  • 31
    • 0029111529 scopus 로고
    • Non-enzymatic glycosylation of the dipeptide L-carnosine, a potential anti-protein-cross-linking agent
    • Hipkiss, A. R., Michaelis, J., and Syrris, P., Non-enzymatic glycosylation of the dipeptide L-carnosine, a potential anti-protein-cross-linking agent. FEBS Lett., 371, 81-85 (1995).
    • (1995) FEBS Lett. , vol.371 , pp. 81-85
    • Hipkiss, A.R.1    Michaelis, J.2    Syrris, P.3
  • 32
    • 0032510414 scopus 로고    scopus 로고
    • Protective effects of carnosine against protein modification mediated by malondial-dehyde and hypochlorite
    • Hipkiss, A. R., Worthington, V. C., Himsworth, D. T. J., and Herwiz, W., Protective effects of carnosine against protein modification mediated by malondial-dehyde and hypochlorite. Biochim. Biophys. Acta, 1380, 46-54 (1998).
    • (1998) Biochim. Biophys. Acta , vol.1380 , pp. 46-54
    • Hipkiss, A.R.1    Worthington, V.C.2    Himsworth, D.T.J.3    Herwiz, W.4
  • 33
    • 0032499880 scopus 로고    scopus 로고
    • Carnosine protects against methylglyoxal-mediated modifications
    • Hipkiss, A. R. and Chana, H., Carnosine protects against methylglyoxal-mediated modifications. Biochem. Biophys. Res. Commun., 248, 28-32 (1998).
    • (1998) Biochem. Biophys. Res. Commun. , vol.248 , pp. 28-32
    • Hipkiss, A.R.1    Chana, H.2
  • 34
    • 0031592750 scopus 로고    scopus 로고
    • Fragmentation of human Cu, Zn-superoxide dismutase by peroxidative reaction
    • Kang, J. H. and Kim, S. M., Fragmentation of human Cu, Zn-superoxide dismutase by peroxidative reaction. Mol. Cell, 7, 553-558 (1997).
    • (1997) Mol. Cell , vol.7 , pp. 553-558
    • Kang, J.H.1    Kim, S.M.2
  • 35
    • 0024788706 scopus 로고
    • Carnosine, homocarnosine and anserine: Could they act as antioxidants in vivo?
    • Aruoma, O. I., Laughton, M. J. and Halliwell, B., Carnosine, homocarnosine and anserine: could they act as antioxidants in vivo? Biochem. J., 264, 863-869 (1989).
    • (1989) Biochem. J. , vol.264 , pp. 863-869
    • Aruoma, O.I.1    Laughton, M.J.2    Halliwell, B.3
  • 36
    • 0002384554 scopus 로고    scopus 로고
    • Antioxidative properties of histidine-containing peptides designed from peptide fragments found in the digests of a soybean protein
    • Chen, H.-M., Muramoto, K., Yamauchi, F., Fujimoto, K., and Nokihara, K., Antioxidative properties of histidine-containing peptides designed from peptide fragments found in the digests of a soybean protein. J. Agric. Food Chem., 46, 49-53 (1998).
    • (1998) J. Agric. Food Chem. , vol.46 , pp. 49-53
    • Chen, H.-M.1    Muramoto, K.2    Yamauchi, F.3    Fujimoto, K.4    Nokihara, K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.