메뉴 건너뛰기




Volumn 111-112, Issue , 1998, Pages 137-151

Glutathione-dependent detoxification of α-oxoaldehydes by the glyoxalase system: Involvement in disease mechanisms and antiproliferative activity of glyoxalase I inhibitors

Author keywords

Apoptosis; Cytokine; Disease mechanisms; Glycation; Glyoxalase; Therapeutic agents

Indexed keywords

ALPHA OXOALDEHYDE; AMINOGUANIDINE; CYTOKINE; ENZYME INHIBITOR; GLUTATHIONE; GLYOXAL; GLYOXALASE I INHIBITOR; HYDROXYACYLGLUTATHIONE HYDROLASE; LACTOYLGLUTATHIONE LYASE; METHYLGLYOXAL; UNCLASSIFIED DRUG;

EID: 4244040278     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0009-2797(97)00157-9     Document Type: Article
Times cited : (297)

References (50)
  • 1
    • 0027454552 scopus 로고
    • The glyoxalase system in health and disease
    • Thornalley P.J. The glyoxalase system in health and disease. Mol. Asp. Med. 14:1993;287-371.
    • (1993) Mol. Asp. Med. , vol.14 , pp. 287-371
    • Thornalley, P.J.1
  • 3
    • 0028951461 scopus 로고
    • Mechanism of autoxidative glycosylation: Identification of glyoxal and arabinose as intermediates in the autoxidative modification of proteins by glucose
    • Wells-Knecht K.J., Zyzak D.V., Litchfield J.E., Thorpe S.R., Baynes J.W. Mechanism of autoxidative glycosylation: Identification of glyoxal and arabinose as intermediates in the autoxidative modification of proteins by glucose. J. Am. Chem. Soc. 34:1995;3702-3709.
    • (1995) J. Am. Chem. Soc. , vol.34 , pp. 3702-3709
    • Wells-Knecht, K.J.1    Zyzak, D.V.2    Litchfield, J.E.3    Thorpe, S.R.4    Baynes, J.W.5
  • 4
    • 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. 276:1995;10017-10025.
    • (1995) J. Biol. Chem. , vol.276 , pp. 10017-10025
    • Glomb, M.A.1    Monnier, V.M.2
  • 5
    • 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
  • 6
    • 0025276041 scopus 로고
    • Stabilization of a reaction intermediate as a catalytic device: Definition of the functional role of the flexible loop in triosephosphate isomerase
    • Pompliano D.L., Peyman A., Knowles J.R. Stabilization of a reaction intermediate as a catalytic device: Definition of the functional role of the flexible loop in triosephosphate isomerase. Biochemistry. 29:1990;3186-3194.
    • (1990) Biochemistry , vol.29 , pp. 3186-3194
    • Pompliano, D.L.1    Peyman, A.2    Knowles, J.R.3
  • 7
    • 0019888193 scopus 로고
    • Isolation of methylglyoxal synthase goat liver
    • Ray S., Ray M. Isolation of methylglyoxal synthase goat liver. J. Biol. Chem. 256:1981;6230-6234.
    • (1981) J. Biol. Chem. , vol.256 , pp. 6230-6234
    • Ray, S.1    Ray, M.2
  • 8
    • 0022367655 scopus 로고
    • Identification of ethanol-inducible P-450 isozyme 3a as the acetone and acetol monooxygenase of rabbit microsomes
    • Koop D.R., Casazza J.P. Identification of ethanol-inducible P-450 isozyme 3a as the acetone and acetol monooxygenase of rabbit microsomes. J. Biol. Chem. 260:1985;13607-13612.
    • (1985) J. Biol. Chem. , vol.260 , pp. 13607-13612
    • Koop, D.R.1    Casazza, J.P.2
  • 9
    • 0026603415 scopus 로고
    • The metabolism of aminoacetone to methylglyoxal by semicarbazide-sensitive amino oxidase in human umbilical artery
    • Lyles G.A., Chalmers J. The metabolism of aminoacetone to methylglyoxal by semicarbazide-sensitive amino oxidase in human umbilical artery. Biochem. Pharmacol. 43:1992;1409-1414.
    • (1992) Biochem. Pharmacol. , vol.43 , pp. 1409-1414
    • Lyles, G.A.1    Chalmers, J.2
  • 10
    • 0015804201 scopus 로고
    • Dioxovalerate as a substrate for the glyoxalase enzyme system
    • Jerzykowski T., Winter R., Matuszewski W. Dioxovalerate as a substrate for the glyoxalase enzyme system. Biochemistry. 135:1979;713-719.
    • (1979) Biochemistry , vol.135 , pp. 713-719
    • Jerzykowski, T.1    Winter, R.2    Matuszewski, W.3
  • 11
    • 0029912862 scopus 로고    scopus 로고
    • Negative association of red blood cell reduced glutathione with diabetic complications
    • Thornalley P.J., McLellan A.C., Lo T.W.C., Benn J., Sönksen P.H. Negative association of red blood cell reduced glutathione with diabetic complications. Clin. Sci. 91:1996;575-582.
    • (1996) Clin. Sci. , vol.91 , pp. 575-582
    • Thornalley, P.J.1    McLellan, A.C.2    Lo, T.W.C.3    Benn, J.4    Sönksen, P.H.5
  • 12
    • 0028292698 scopus 로고
    • The glyoxalase system in clinical diabetes mellitus and correlation with diabetic complications
    • McLellan A.C., Thornalley P.J., Benn J., Sönksen P.H. The glyoxalase system in clinical diabetes mellitus and correlation with diabetic complications. Clin. Sci. 87:1994;21-29.
    • (1994) Clin. Sci. , vol.87 , pp. 21-29
    • McLellan, A.C.1    Thornalley, P.J.2    Benn, J.3    Sönksen, P.H.4
  • 13
    • 0028988415 scopus 로고
    • 2-(1-carboxyethyl)guanine (CEG) as a guanine advanced glycosylation endproduct
    • 2-(1-carboxyethyl)guanine (CEG) as a guanine advanced glycosylation endproduct. Biochemistry. 34:1995;648-655.
    • (1995) Biochemistry , vol.34 , pp. 648-655
    • Papoulis, A.1    Al-Abed, Y.2    Bucala, R.3
  • 14
    • 0028168184 scopus 로고
    • 32P-postlabelling technique for the analysis of 2′-deoxyguanosine-3′-monophosphate and DNA of methylglyoxal
    • 32P-postlabelling technique for the analysis of 2′-deoxyguanosine-3′-monophosphate and DNA of methylglyoxal. Carcinogenesis. 15:1994;1887-1894.
    • (1994) Carcinogenesis , vol.15 , pp. 1887-1894
    • Vaca, C.E.1    Fang, J.2    Conradi, M.3    Hou, S.4
  • 16
    • 0029005896 scopus 로고
    • Advances in glyoxalase research. Glyoxalase expression in malignancy, anti-proliferative effects of methylglyoxal, glyoxalase I inhibitor diesters and S-D-lactoylglutathione, and methylglyoxal-modified protein binding and endocytosis by the advanced glycation endproduct receptor
    • Thornalley P.J. Advances in glyoxalase research. Glyoxalase expression in malignancy, anti-proliferative effects of methylglyoxal, glyoxalase I inhibitor diesters and S-D-lactoylglutathione, and methylglyoxal-modified protein binding and endocytosis by the advanced glycation endproduct receptor. Crit. Rev. Oncol. Haematol. 20:1995;99-128.
    • (1995) Crit. Rev. Oncol. Haematol. , vol.20 , pp. 99-128
    • Thornalley, P.J.1
  • 18
    • 0029871594 scopus 로고    scopus 로고
    • Mechanism of oxidative DNA damage induced by δ-aminolevulinic acid in the presence of copper ion
    • Hiraku Y., Shosuke K. Mechanism of oxidative DNA damage induced by δ-aminolevulinic acid in the presence of copper ion. Cancer Res. 56:1997;1786-1793.
    • (1997) Cancer Res. , vol.56 , pp. 1786-1793
    • Hiraku, Y.1    Shosuke, K.2
  • 19
    • 0014665769 scopus 로고
    • Glyoxalase inhibitors as potential anticancer agents
    • Vince R., Wadd W.B. Glyoxalase inhibitors as potential anticancer agents. Biochem. Biophys. Res. Commun. 35:1969;593-598.
    • (1969) Biochem. Biophys. Res. Commun. , vol.35 , pp. 593-598
    • Vince, R.1    Wadd, W.B.2
  • 20
    • 0026620761 scopus 로고
    • Inhibition of proliferation of human leukemia 60 cells by diethyl esters of glyoxalase inhibitors in vitro
    • Lo T.W.C., Thornalley P.J. Inhibition of proliferation of human leukemia 60 cells by diethyl esters of glyoxalase inhibitors in vitro. Biochem. Pharmacol. 44:1992;2357-2363.
    • (1992) Biochem. Pharmacol. , vol.44 , pp. 2357-2363
    • Lo, T.W.C.1    Thornalley, P.J.2
  • 21
    • 0029767940 scopus 로고    scopus 로고
    • Antitumour activity of S-p-bromobenzylglutathione diesters in vitro: A structure activity study
    • Thornalley P.J., Ladan M.J., Ridgway S.J.S., Kang Y. Antitumour activity of S-p-bromobenzylglutathione diesters in vitro: a structure activity study. J. Med. Chem. 39:1996;3409-3411.
    • (1996) J. Med. Chem. , vol.39 , pp. 3409-3411
    • Thornalley, P.J.1    Ladan, M.J.2    Ridgway, S.J.S.3    Kang, Y.4
  • 22
    • 0029878798 scopus 로고    scopus 로고
    • Antitumour activity of S-p-bromobenzylglutathione cyclopentyl diester in vitro and in vivo. Inhibition of glyoxalase I and induction of apoptosis
    • Thornalley P.J., Edwards L.G., Kang Y., Wyatt C., Davies N., Ladan M.J., Double J. Antitumour activity of S-p-bromobenzylglutathione cyclopentyl diester in vitro and in vivo. Inhibition of glyoxalase I and induction of apoptosis. Biochem. Pharmacol. 51:1996;1365-1372.
    • (1996) Biochem. Pharmacol. , vol.51 , pp. 1365-1372
    • Thornalley, P.J.1    Edwards, L.G.2    Kang, Y.3    Wyatt, C.4    Davies, N.5    Ladan, M.J.6    Double, J.7
  • 24
    • 0010480577 scopus 로고
    • Anti-malarial activity in vitro of the glyoxalase I inhibitor diester, S-p-bromobenzylglutathione diethyl ester
    • Thornalley P.J., Strath M., Wilson R.J.M. Anti-malarial activity in vitro of the glyoxalase I inhibitor diester, S-p-bromobenzylglutathione diethyl ester. Biochem. Pharmacol. 268:1994;14189-14825.
    • (1994) Biochem. Pharmacol. , vol.268 , pp. 14189-14825
    • Thornalley, P.J.1    Strath, M.2    Wilson, R.J.M.3
  • 25
    • 0023778433 scopus 로고
    • Modification of the glyoxalase system in human red blood cells by glucose in vitro
    • Thornalley P.J. Modification of the glyoxalase system in human red blood cells by glucose in vitro. Biochem. J. 254:1988;751-755.
    • (1988) Biochem. J. , vol.254 , pp. 751-755
    • Thornalley, P.J.1
  • 26
    • 0027185979 scopus 로고
    • Modification of the glyoxalase system in streptozotocin-induced diabetic rats; Effect of the aldose reductase inhibitor Statil
    • Phillips S.A., Mirrlees D., Thornalley P.J. Modification of the glyoxalase system in streptozotocin-induced diabetic rats; effect of the aldose reductase inhibitor Statil. Biochem. Pharmacol. 46:1993;805-811.
    • (1993) Biochem. Pharmacol. , vol.46 , pp. 805-811
    • Phillips, S.A.1    Mirrlees, D.2    Thornalley, P.J.3
  • 28
    • 0000822619 scopus 로고    scopus 로고
    • Overexpression of glyoxalase I inhibits intracellular advanced glycation endproduct (AGE) formation
    • Shinohara M., Giardino I., Brownlee M. Overexpression of glyoxalase I inhibits intracellular advanced glycation endproduct (AGE) formation. Diabetes. 45:1996;126A.
    • (1996) Diabetes , vol.45
    • Shinohara, M.1    Giardino, I.2    Brownlee, M.3
  • 29
    • 0028019673 scopus 로고
    • Reaction of methylglyoxal with aminoguanidine under physiological conditions and prevention of methylglyoxal binding to plasma proteins
    • Lo T.W.C., Selwood T., Thornalley P.J. Reaction of methylglyoxal with aminoguanidine under physiological conditions and prevention of methylglyoxal binding to plasma proteins. Biochem. Pharmacol. 48:1994;1865-1870.
    • (1994) Biochem. Pharmacol. , vol.48 , pp. 1865-1870
    • Lo, T.W.C.1    Selwood, T.2    Thornalley, P.J.3
  • 30
    • 0029743039 scopus 로고    scopus 로고
    • Advanced glycation and the development of diabetic complications. Unifying the involvement of glucose, methylglyoxal and oxidative stress
    • Thornalley P.J. Advanced glycation and the development of diabetic complications. Unifying the involvement of glucose, methylglyoxal and oxidative stress. Endocrinol. Metab. 3:1996;149-166.
    • (1996) Endocrinol. Metab. , vol.3 , pp. 149-166
    • Thornalley, P.J.1
  • 32
    • 0003039181 scopus 로고
    • Detection and identification of a protein-bound imidazolone resulting from the reaction of arginine residues and methylglyoxal
    • Henle T., Walter A., Haebner R., Klostermeryer H. Detection and identification of a protein-bound imidazolone resulting from the reaction of arginine residues and methylglyoxal. Z. Lebensm. Unters. Forsch. 199:1994;55-58.
    • (1994) Z. Lebensm. Unters. Forsch , vol.199 , pp. 55-58
    • Henle, T.1    Walter, A.2    Haebner, R.3    Klostermeryer, H.4
  • 33
    • 0029760932 scopus 로고    scopus 로고
    • Protein cross-linking by the Maillard reaction. Isolation, characterization, and in vivo detection of a lysine-lysine cross-link derived from methylglyoxal
    • Nagaraj R.H., Shipanova I.N., Faust F.M. Protein cross-linking by the Maillard reaction. Isolation, characterization, and in vivo detection of a lysine-lysine cross-link derived from methylglyoxal. J. Biol. Chem. 271:1996;19338-19345.
    • (1996) J. Biol. Chem. , vol.271 , pp. 19338-19345
    • Nagaraj, R.H.1    Shipanova, I.N.2    Faust, F.M.3
  • 34
    • 0030919275 scopus 로고    scopus 로고
    • ε-(2-Carboxyethyl)lysine, a product of chemical modification of proteins by methylglyoxal, increases with age in human lens proteins
    • ε-(2-Carboxyethyl)lysine, a product of 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    Thorpe, S.R.3    Baynes, J.W.4
  • 35
    • 0019321209 scopus 로고
    • The apparent glutathione oxidase activity of gamma-glutamyl transpeptidase
    • Griffith O.W., Tate S.S. The apparent glutathione oxidase activity of gamma-glutamyl transpeptidase. J. Biol. Chem. 255:1980;5011-5014.
    • (1980) J. Biol. Chem. , vol.255 , pp. 5011-5014
    • Griffith, O.W.1    Tate, S.S.2
  • 36
    • 0026786580 scopus 로고
    • The assay of methylglyoxal in biological systems by derivatization with 1,2-diamino-4,5-dimethoxybenzene
    • McLellan A.C., Phillips S.A., Thornalley P.J. The assay of methylglyoxal in biological systems by derivatization with 1,2-diamino-4,5-dimethoxybenzene. Anal. Biochem. 206:1992;17-23.
    • (1992) Anal. Biochem. , vol.206 , pp. 17-23
    • McLellan, A.C.1    Phillips, S.A.2    Thornalley, P.J.3
  • 37
    • 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., 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
  • 38
    • 0029950666 scopus 로고    scopus 로고
    • Induction of synthesis and secretion of interleukin 1( in the human monocytic leukaemia THP-1 cells by human serum albumins modified with methylglyoxal and advanced glycation endproducts
    • Westwood M.E., Thornalley P.J. Induction of synthesis and secretion of interleukin 1( in the human monocytic leukaemia THP-1 cells by human serum albumins modified with methylglyoxal and advanced glycation endproducts. Immunol. Lett. 50:1996;17-21.
    • (1996) Immunol. Lett. , vol.50 , pp. 17-21
    • Westwood, M.E.1    Thornalley, P.J.2
  • 39
    • 0028597991 scopus 로고
    • Receptor-mediated endocytic uptake of methylglyoxal-modified proteins
    • Westwood M.E., McLellan A.C., Thornalley P.J. Receptor-mediated endocytic uptake of methylglyoxal-modified proteins. J. Biol. Chem. 269:1994;32293-32298.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32293-32298
    • Westwood, M.E.1    McLellan, A.C.2    Thornalley, P.J.3
  • 40
    • 85007869545 scopus 로고
    • Uptake of proteins modified with 3-deoxyglucosone, a Maillard reaction intermediate, by the type I macrophage scavenger receptor
    • Shinoda T., Hayase F., Van Chuyen N., Kato H. Uptake of proteins modified with 3-deoxyglucosone, a Maillard reaction intermediate, by the type I macrophage scavenger receptor. Biosci. Biotech. Biochem. 57:1993;1826-1831.
    • (1993) Biosci. Biotech. Biochem. , vol.57 , pp. 1826-1831
    • Shinoda, T.1    Hayase, F.2    Van Chuyen, N.3    Kato, H.4
  • 41
    • 0029020336 scopus 로고
    • Macrophage scavenger receptor mediates the endocytic uptake and degradation of advanced glycation end-products of the Maillard reaction
    • Araki N., Higashi T., Mori T., Shibayama R., Kawabe Y., Kodama T., Takahashi K., Shichiri M., Horiuchi S. Macrophage scavenger receptor mediates the endocytic uptake and degradation of advanced glycation end-products of the Maillard reaction. Eur. J. Biochem. 230:1995;408-415.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 408-415
    • Araki, N.1    Higashi, T.2    Mori, T.3    Shibayama, R.4    Kawabe, Y.5    Kodama, T.6    Takahashi, K.7    Shichiri, M.8    Horiuchi, S.9
  • 42
    • 0028233384 scopus 로고
    • The endothelial cell binding site for advanced glycation endproducts consists of a complex: An integral membrane protein and a lactoferrin-like polypeptide
    • Schmidt A.M., Mora R., Cao R., Yan S., Brett J., Ramakrishnan R., Tsang T.E., Simionescu M., Stern D. The endothelial cell binding site for advanced glycation endproducts consists of a complex: An integral membrane protein and a lactoferrin-like polypeptide. J. Biol. Chem. 269:1994;9882-9888.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9882-9888
    • Schmidt, A.M.1    Mora, R.2    Cao, R.3    Yan, S.4    Brett, J.5    Ramakrishnan, R.6    Tsang, T.E.7    Simionescu, M.8    Stern, D.9
  • 43
    • 0030273623 scopus 로고    scopus 로고
    • Synthesis and secretion of macrophage colony stimulating factor by mature human monocytes and human monocytic THP-1 cells induced by human serum albumin derivatives modified with methylglyoxal and glucose-derived advanced glycation endproducts
    • Abordo E.A., Westwood M.E., Thornalley P.J. Synthesis and secretion of macrophage colony stimulating factor by mature human monocytes and human monocytic THP-1 cells induced by human serum albumin derivatives modified with methylglyoxal and glucose-derived advanced glycation endproducts. Immunol. Lett. 53:1996;7-13.
    • (1996) Immunol. Lett. , vol.53 , pp. 7-13
    • Abordo, E.A.1    Westwood, M.E.2    Thornalley, P.J.3
  • 44
    • 4243401865 scopus 로고    scopus 로고
    • Human serum albumin minimally-modified by methylglyoxal but not by glucose-derived advanced glycation endproducts induced the synthesis and secretion of tumour necrosis factor-α (TNFα) by human monocytic THP-1 cells in vitro
    • Abordo E., Argirov O.K., Thornalley P.J. Human serum albumin minimally-modified by methylglyoxal but not by glucose-derived advanced glycation endproducts induced the synthesis and secretion of tumour necrosis factor-α (TNFα) by human monocytic THP-1 cells in vitro. Diabetes. 45:1996;129A.
    • (1996) Diabetes , vol.45
    • Abordo, E.1    Argirov, O.K.2    Thornalley, P.J.3
  • 46
    • 0025892834 scopus 로고
    • Role of glycation in modification of lens crystallins in diabetic and nondiabetic senile cataracts
    • Lyons T.J., Silvestri G., Dunn J.A., Dyer D.G., Baynes J.W. Role of glycation in modification of lens crystallins in diabetic and nondiabetic senile cataracts. Diabetes. 40:1991;1010-1015.
    • (1991) Diabetes , vol.40 , pp. 1010-1015
    • Lyons, T.J.1    Silvestri, G.2    Dunn, J.A.3    Dyer, D.G.4    Baynes, J.W.5
  • 47
    • 0027049697 scopus 로고
    • Exogenous advanced glycosylation end products induce complex vascular dysfunction in normal animals: A model for diabetic and aging complications
    • Vlassara H., Fuh H., Makita Z., Krungkrai S., Cerami A., Bucala R. Exogenous advanced glycosylation end products induce complex vascular dysfunction in normal animals: A model for diabetic and aging complications. Proc. Natl. Acad. Sci. USA. 89:1992;12043-12047.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 12043-12047
    • Vlassara, H.1    Fuh, H.2    Makita, Z.3    Krungkrai, S.4    Cerami, A.5    Bucala, R.6
  • 50
    • 0024597762 scopus 로고
    • Free radical generation during δ-aminolevulinic acid autooxiadtion: Induction by hemoglobin and connections with porphyrinopathies
    • Monteiro H.P., Abdalla D.S.P., Augusto O., Bechara E.J.H. Free radical generation during δ-aminolevulinic acid autooxiadtion: induction by hemoglobin and connections with porphyrinopathies. Arch. Biochem. Biophys. 271:1989;206-216.
    • (1989) Arch. Biochem. Biophys. , vol.271 , pp. 206-216
    • Monteiro, H.P.1    Abdalla, D.S.P.2    Augusto, O.3    Bechara, E.J.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.