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Volumn 41, Issue 5, 2007, Pages 507-514

Methyl glyoxal elevation is associted with oxidative stress in rheumatoid arthritis

Author keywords

Free radical; Methyl glyoxal; Reduced glutathione; Rheumatoid arthritis; Total antioxidant status

Indexed keywords

ANTIOXIDANT; CARBONYL DERIVATIVE; FREE RADICAL; GLUTATHIONE; METHYLGLYOXAL; RHEUMATOID FACTOR; THIOBARBITURIC ACID REACTIVE SUBSTANCE; THIOL;

EID: 34047159990     PISSN: 10715762     EISSN: 10292470     Source Type: Journal    
DOI: 10.1080/10715760601148285     Document Type: Article
Times cited : (9)

References (33)
  • 1
    • 0029039717 scopus 로고
    • Oxygen radicals, nitric oxide and human inflammatory joint disease
    • Halliwell, B. (1995) Oxygen radicals, nitric oxide and human inflammatory joint disease. Ann Rheum Dis, 54, pp. 505-510.
    • (1995) Ann Rheum Dis , vol.54 , pp. 505-510
    • Halliwell, B.1
  • 2
    • 0024746052 scopus 로고
    • Oxygen free radicals, inflammation and synovitis: The current status
    • Merry, P., Winyard, PG, Morris, CJ, Grootveld, M. and Blake, DR (1989) Oxygen free radicals, inflammation and synovitis: The current status. Ann Rheum Dis, 48, pp. 864-870.
    • (1989) Ann Rheum Dis , vol.48 , pp. 864-870
    • Merry, P.1    Winyard, P.G.2    Morris, C.J.3    Grootveld, M.4    Blake, D.R.5
  • 3
    • 0001590580 scopus 로고    scopus 로고
    • Free radicals, other reactive species and disease
    • Oxford University Press, New York
    • Halliwell, B. and Gutteridge, JMC (1999) Free radicals, other reactive species and disease. Free radicals in biology and medicine, p. 667. Oxford University Press, New York
    • (1999) , pp. 667
    • Halliwell, B.1    Gutteridge, J.M.C.2
  • 4
    • 0025787465 scopus 로고
    • Kinetic parameters for the elimination reaction catalyzed by triosephosphate isomerase and an estimation of the reaction's physiological significance
    • Richard, JP (1991) Kinetic parameters for the elimination reaction catalyzed by triosephosphate isomerase and an estimation of the reaction's physiological significance. Biochemistry, 30, pp. 4581-4585.
    • (1991) Biochemistry , vol.30 , pp. 4581-4585
    • Richard, J.P.1
  • 5
    • 0033571012 scopus 로고    scopus 로고
    • Formation of glyoxal, methyl glyoxal and 3 deoxyglucosone in the glycation of protein by glucose
    • Thornalley, PJ, Langbong, A. and Minhas, HS (1999) Formation of glyoxal, methyl glyoxal and 3 deoxyglucosone in the glycation of protein by glucose. Biochem J, 344, pp. 109-116.
    • (1999) Biochem J , vol.344 , pp. 109-116
    • Thornalley, P.J.1    Langbong, A.2    Minhas, H.S.3
  • 6
    • 0033055417 scopus 로고    scopus 로고
    • Immunohistochemical evidence for an increased oxidative stress and carbonyl modification of proteins in diabetic glomerular lesions
    • Suzuki, D., Miyata, T. and Saotome, N. (1999) Immunohistochemical evidence for an increased oxidative stress and carbonyl modification of proteins in diabetic glomerular lesions. J Am Soc Nephrol, 10, pp. 822-832.
    • (1999) J Am Soc Nephrol , vol.10 , pp. 822-832
    • Suzuki, D.1    Miyata, T.2    Saotome, N.3
  • 7
    • 0022494823 scopus 로고
    • Acetone metabolism in humans during diabetic ketoacidosis
    • Reichard, GA, Skutches, CL, Hoeldtke, RD and Owen, OE (1986) Acetone metabolism in humans during diabetic ketoacidosis. Diabetes, 35, pp. 668-674.
    • (1986) Diabetes , vol.35 , pp. 668-674
    • Reichard, G.A.1    Skutches, C.L.2    Hoeldtke, R.D.3    Owen, O.E.4
  • 8
    • 0023644772 scopus 로고
    • Aminoacetone oxidase from goat liver
    • Ray, M. and Ray, S. (1987) Aminoacetone oxidase from goat liver. Formation of methyl glyoxal from aminoacetone. J Biol Chem, 262:13, pp. 5974-5977.
    • (1987) J Biol Chem , vol.262 , Issue.13 , pp. 5974-5977
    • Ray, M.1    Ray, S.2
  • 9
    • 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, PJ (1996) Pharmacology of methylglyoxal: Formation, modification of proteins and nucleic acids, and enzymatic detoxification-a role in pathogenesis and antiproliferative chemotherapy. Gen Pharmacol, 27:4, pp. 565-573.
    • (1996) Gen Pharmacol , vol.27 , Issue.4 , pp. 565-573
    • Thornalley, P.J.1
  • 10
    • 0025096104 scopus 로고
    • Autoxidative glycosylation and possible involvement of peroxides and free radicals in LDL modification by glucose
    • Hunt, JV, Smith, CC and Wolff, SP (1990) Autoxidative glycosylation and possible involvement of peroxides and free radicals in LDL modification by glucose. Diabetes, 39, pp. 1420-1424.
    • (1990) Diabetes , vol.39 , pp. 1420-1424
    • Hunt, J.V.1    Smith, C.C.2    Wolff, S.P.3
  • 11
    • 0030835896 scopus 로고    scopus 로고
    • Selective induction of heparin-binding epidermal growth factor-like growth factor by methylglyoxal and 3-deoxyglucosone in rat aortic smooth muscle cells
    • Che, W., Asahi, M. and Takahashi, M. (1997) Selective induction of heparin-binding epidermal growth factor-like growth factor by methylglyoxal and 3-deoxyglucosone in rat aortic smooth muscle cells. The involvement of reactive oxygen species formation and a possible implication for atherogenesis in diabetes. J Biol Chem, 272, pp. 18453-18459.
    • (1997) J Biol Chem , vol.272 , pp. 18453-18459
    • Che, W.1    Asahi, M.2    Takahashi, M.3
  • 12
    • 0028605299 scopus 로고
    • Binding and modification of proteins by methylglyoxal under physiological conditions
    • Lo, TW, Westwood, ME, McLellan, AC, Selwood, T. and Thornalley, PJ (1994) Binding and modification of proteins by methylglyoxal under physiological conditions. A kinetic and mechanistic study with N alpha-acetylarginine, N alpha-acetylcysteine, and N alpha-acetyllysine, and bovine serum albumin. J Biol Chem, 269:51, pp. 32299-32305.
    • (1994) J Biol Chem , vol.269 , Issue.51 , pp. 32299-32305
    • Lo, T.W.1    Westwood, M.E.2    McLellan, A.C.3    Selwood, T.4    Thornalley, P.J.5
  • 13
    • 0033603599 scopus 로고    scopus 로고
    • Methylglyoxal modification of protein
    • Oya, T., Hattori, N., Mizuno, Y., Miyata, S., Maeda, S., Osawa, T. and Uchida, K. (1999) Methylglyoxal modification of protein. Chemical and immunochemical characterization of methylglyoxal-arginine adducts. J Biol Chem, 274, pp. 18492-18562.
    • (1999) J Biol Chem , vol.274 , pp. 18492-18562
    • Oya, T.1    Hattori, N.2    Mizuno, Y.3    Miyata, S.4    Maeda, S.5    Osawa, T.6    Uchida, K.7
  • 14
    • 0035135246 scopus 로고    scopus 로고
    • Advanced glycation end products: A review
    • Singh, R., Barden, A., Mori, T. and Belin, L. (2001) Advanced glycation end products: A review. Diabetologia, 44, pp. 129-146.
    • (2001) Diabetologia , vol.44 , pp. 129-146
    • Singh, R.1    Barden, A.2    Mori, T.3    Belin, L.4
  • 15
    • 0026786580 scopus 로고
    • The assay of methyl glyoxal in biological systems by derivatisation with 1,2-diamino-4,5-dimethoxybenzene
    • Lellan, AC Mc, Phillips, SA and Thornalley, PJ (1992) The assay of methyl glyoxal in biological systems by derivatisation with 1,2-diamino-4,5-dimethoxybenzene. Anal Biochem, 206, pp. 17-23.
    • (1992) Anal Biochem , vol.206 , pp. 17-23
    • Lellan, A.C.1    Mc Phillips, S.A.2    Thornalley, P.J.3
  • 16
    • 0028265929 scopus 로고
    • Quantitative analysis of cross-links pyridinoline and pentosidine in articular cartilage of patients with bone and joint disorders
    • Takahashi, M., Kushida, K. and Ohishi, T. (1994) Quantitative analysis of cross-links pyridinoline and pentosidine in articular cartilage of patients with bone and joint disorders. Arthritis Rheum, 37, pp. 724-728.
    • (1994) Arthritis Rheum , pp. 724-728
    • Takahashi, M.1    Kushida, K.2    Ohishi, T.3
  • 17
    • 0023945481 scopus 로고
    • The American Rheumatism Association 1987 revised criteria for the classification of rheumatoid arthritis
    • Arnett, FC, Edworthy, SM and Bloch, DA (1988) The American Rheumatism Association 1987 revised criteria for the classification of rheumatoid arthritis. Arthritis Rheum, 31, pp. 315-324.
    • (1988) Arthritis Rheum , vol.31 , pp. 315-324
    • Arnett, F.C.1    Edworthy, S.M.2    Bloch, D.A.3
  • 18
    • 0032982508 scopus 로고    scopus 로고
    • Antioxidant activity applying an improved ABTS radical cation decolorization assay
    • Pellegrini, N., Proteggente, A., Pannala, A., Yang, M. and Rice-Evans, C. (1999) Antioxidant activity applying an improved ABTS radical cation decolorization assay. Free Radic Biol Med, 26, pp. 1231-1237.
    • (1999) Free Radic Biol Med , vol.26 , pp. 1231-1237
    • Pellegrini, N.1    Proteggente, A.2    Pannala, A.3    Yang, M.4    Rice-Evans, C.5
  • 19
    • 0028283301 scopus 로고
    • Measurement of protein thiol groups and glutathione in plasma
    • Hu, ML (1994) Measurement of protein thiol groups and glutathione in plasma. Methods Enzymol, 233, pp. 382-385.
    • (1994) Methods Enzymol , vol.233 , pp. 382-385
    • Hu, M.L.1
  • 20
    • 33746850523 scopus 로고
    • Methyl glyoxal synthase
    • Cooper, RA (1975) Methyl glyoxal synthase. Methods Enzymol, 41, pp. 535-541.
    • (1975) Methods Enzymol , vol.41 , pp. 535-541
    • Cooper, R.A.1
  • 21
    • 33644963032 scopus 로고    scopus 로고
    • In vivo assessment of toxicity and pharmacokinetics of methyl glyoxal
    • Ghosh, M., Talukdar, D., Ghosh, S., Bhattacharya, M., Ray, M. and Ray, S. (2006) In vivo assessment of toxicity and pharmacokinetics of methyl glyoxal. Augmentation of the curative effect of methyl glyoxal on cancer bearing mice by ascorbic acid and creatine. Toxicol Appl Pharmacol, 212, pp. 45-58.
    • (2006) Toxicol Appl Pharmacol , vol.212 , pp. 45-58
    • Ghosh, M.1    Talukdar, D.2    Ghosh, S.3    Bhattacharya, M.4    Ray, M.5    Ray, S.6
  • 22
    • 0030039967 scopus 로고    scopus 로고
    • Methyl glyoxal assay in cells as 2-methylquinoxaline using 1,2-diaminobenzene as derivatizing reagent
    • Cordeiro, C. and Freire, AP (1996) Methyl glyoxal assay in cells as 2-methylquinoxaline using 1,2-diaminobenzene as derivatizing reagent. Anal Biochem, 234, pp. 221-224.
    • (1996) Anal Biochem , vol.234 , pp. 221-224
    • Cordeiro, C.1    Freire, A.P.2
  • 23
    • 0018384650 scopus 로고
    • Assay of lipid peroxides in animal tissues by therbituric acid reaction
    • Ohkawa, H., Ohishi, N. and Yagi, K. (1979) Assay of lipid peroxides in animal tissues by therbituric acid reaction. Anal Biochem, 95, pp. 351-358.
    • (1979) Anal Biochem , vol.95 , pp. 351-358
    • Ohkawa, H.1    Ohishi, N.2    Yagi, K.3
  • 24
    • 0019857959 scopus 로고
    • Free radical oxidation (peroxidation) products in serum and synovial fluid in rheumatoid arthritis
    • Lumec, J., Halloran, SP, White, AG and Dormandy, TL (1981) Free radical oxidation (peroxidation) products in serum and synovial fluid in rheumatoid arthritis. J Rheum, 8, pp. 233-245.
    • (1981) J Rheum , vol.8 , pp. 233-245
    • Lumec, J.1    Halloran, S.P.2    White, A.G.3    Dormandy, T.L.4
  • 26
    • 33746854436 scopus 로고    scopus 로고
    • The role of methyl glyoxal in relation to patho-physiological complications in diabetes mellitus
    • Mukhopadhyay, S., Gachhui, R. and Kar, M. (2006) The role of methyl glyoxal in relation to patho-physiological complications in diabetes mellitus. Biomed Res, 17:2, pp. 111-116.
    • (2006) Biomed Res , vol.17 , Issue.2 , pp. 111-116
    • Mukhopadhyay, S.1    Gachhui, R.2    Kar, M.3
  • 28
    • 0036164004 scopus 로고    scopus 로고
    • Crosslinking by advanced glycation end products increases the stiffness of the collagen network in human articular cartilage: A possible mechanism through which age is a risk factor for osteoarthritis
    • Verzijl, N., DeGroot, J. and Ben, ZC (2002) Crosslinking by advanced glycation end products increases the stiffness of the collagen network in human articular cartilage: A possible mechanism through which age is a risk factor for osteoarthritis. Arthritis Rheum, 46:1, pp. 114-123.
    • (2002) Arthritis Rheum , vol.46 , Issue.1 , pp. 114-123
    • Verzijl, N.1    DeGroot, J.2    Ben, Z.C.3
  • 29
    • 27744536479 scopus 로고    scopus 로고
    • The glycolytic metabolite methylglyoxal activates Pap1 and Sty1 stress responses in Schizosaccharomyces pombe
    • Zuin, A., Vivancos, AP and Sanso, M. (2005) The glycolytic metabolite methylglyoxal activates Pap1 and Sty1 stress responses in Schizosaccharomyces pombe. J Biol Chem, 280:44, pp. 36708-36713.
    • (2005) J Biol Chem , vol.280 , Issue.44 , pp. 36708-36713
    • Zuin, A.1    Vivancos, A.P.2    Sanso, M.3
  • 30
    • 31044438180 scopus 로고    scopus 로고
    • Methyl glyoxal modification of mSin3A links glycolysis to angiopoietin-2 transcription
    • Yao, D., Taguchi, T. and Matsumura, T. (2006) Methyl glyoxal modification of mSin3A links glycolysis to angiopoietin-2 transcription. Cell, 124, pp. 275-286.
    • (2006) Cell , vol.124 , pp. 275-286
    • Yao, D.1    Taguchi, T.2    Matsumura, T.3
  • 31
    • 37049228077 scopus 로고
    • Cancerostatic action of methylglyoxal
    • Egyud, LG and Gyorgyi, S. (1968) Cancerostatic action of methylglyoxal. Science, 160, p. 1140.
    • (1968) Science , vol.160 , pp. 1140
    • Egyud, L.G.1    Gyorgyi, S.2
  • 32
    • 0027964573 scopus 로고
    • Inhibition of electron flow through complex I of the mitochondrial respiratory chain of Ehrlich ascites carcinoma cells by methyl glyoxal
    • Ray, S., Dutta, S., Halder, J. and Ray, M. (1994) Inhibition of electron flow through complex I of the mitochondrial respiratory chain of Ehrlich ascites carcinoma cells by methyl glyoxal. Biochem J, 303, pp. 69-72.
    • (1994) Biochem J , vol.303 , pp. 69-72
    • Ray, S.1    Dutta, S.2    Halder, J.3    Ray, M.4
  • 33
    • 0032777558 scopus 로고    scopus 로고
    • Does redox regulation of cell function explain why antioxidants perform so poorly as therapeutic agents?
    • Gutteridge, JM (1999) Does redox regulation of cell function explain why antioxidants perform so poorly as therapeutic agents?. Redox Rep, 4, p. 129.
    • (1999) Redox Rep , vol.4 , pp. 129
    • Gutteridge, J.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.