메뉴 건너뛰기




Volumn 22, Issue 3, 2011, Pages 318-325

Glyoxalase in tumourigenesis and multidrug resistance

Author keywords

Cancer; DNA damage; Gene amplification; Methylglyoxal; Multidrug resistance

Indexed keywords

ANTINEOPLASTIC AGENT; BIOLOGICAL MARKER; CISPLATIN; DOXORUBICIN; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; GLYOXALASE; HYDROXYACYLGLUTATHIONE HYDROLASE; LACTIC ACID; LACTOYLGLUTATHIONE LYASE; METHYLGLYOXAL; MITOMYCIN C; NUCLEOTIDE; PHOSPHOLIPID; PROTEIN;

EID: 79955945922     PISSN: 10849521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.semcdb.2011.02.006     Document Type: Review
Times cited : (151)

References (83)
  • 2
    • 0001489682 scopus 로고
    • An enzyme concerned with the formation of hydroxy acids from ketonic aldehydes
    • Dakin H.D., Dudley H.W. An enzyme concerned with the formation of hydroxy acids from ketonic aldehydes. J Biol Chem 1913, 14:155-157.
    • (1913) J Biol Chem , vol.14 , pp. 155-157
    • Dakin, H.D.1    Dudley, H.W.2
  • 3
    • 0001740246 scopus 로고
    • The destruction of lactic aldehyde and methylglyoxal by animal organs
    • Neuberg C. The destruction of lactic aldehyde and methylglyoxal by animal organs. Biochem Z 1913, 49:502-506.
    • (1913) Biochem Z , vol.49 , pp. 502-506
    • Neuberg, C.1
  • 4
    • 0001483173 scopus 로고
    • Metabolism of tumours
    • Warburg O. Metabolism of tumours. Biochem Z 1923, 142:317-333.
    • (1923) Biochem Z , vol.142 , pp. 317-333
    • Warburg, O.1
  • 5
    • 0001739947 scopus 로고
    • The mechanism of action of glyoxalase
    • Racker E. The mechanism of action of glyoxalase. J Biol Chem 1951, 190:685-696.
    • (1951) J Biol Chem , vol.190 , pp. 685-696
    • Racker, E.1
  • 6
    • 84879005500 scopus 로고
    • Glutathione as coenzyme in intermediary metabolism
    • Academic Press, New York, S. Colowick, A. Lazarow, E. Racker, D.R. Schwarz, E. Stadtman, H. Waelsch (Eds.)
    • Racker E. Glutathione as coenzyme in intermediary metabolism. Glutathione 1954, 208. Academic Press, New York. S. Colowick, A. Lazarow, E. Racker, D.R. Schwarz, E. Stadtman, H. Waelsch (Eds.).
    • (1954) Glutathione , pp. 208
    • Racker, E.1
  • 7
    • 0015937958 scopus 로고
    • The stereochemical configuration of the lactoyl group of S-lactoylglutathione formed by the action of glyoxalase I from porcine erythrocytes and yeast
    • Ekwall K., Mannervik B. The stereochemical configuration of the lactoyl group of S-lactoylglutathione formed by the action of glyoxalase I from porcine erythrocytes and yeast. Biochim Biophys Acta 1973, 297:297-299.
    • (1973) Biochim Biophys Acta , vol.297 , pp. 297-299
    • Ekwall, K.1    Mannervik, B.2
  • 8
    • 79955951318 scopus 로고
    • Glyoxalase: II. The distribution of glyoxalase in tissues of normal and cancerous albino rats
    • Platt M.E., Schroeder E.F. Glyoxalase: II. The distribution of glyoxalase in tissues of normal and cancerous albino rats. J Biol Chem 1934, 106:179-190.
    • (1934) J Biol Chem , vol.106 , pp. 179-190
    • Platt, M.E.1    Schroeder, E.F.2
  • 9
    • 79955954391 scopus 로고
    • The glyoxalase activity of tissues
    • Jowett M., Quastel J.H. The glyoxalase activity of tissues. Biochem J 1934, 28:162-172.
    • (1934) Biochem J , vol.28 , pp. 162-172
    • Jowett, M.1    Quastel, J.H.2
  • 10
    • 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 1994, 15:1887-1894.
    • (1994) Carcinogenesis , vol.15 , pp. 1887-1894
    • Vaca, C.E.1    Fang, J.-L.2    Conradi, M.3    Hou, S.-M.4
  • 12
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • Hanahan D., Weinberg R.A. The hallmarks of cancer. Cell 2000, 100:57-70.
    • (2000) Cell , vol.100 , pp. 57-70
    • Hanahan, D.1    Weinberg, R.A.2
  • 13
    • 0000463968 scopus 로고
    • Arrest of cancer in mice by therapy with normal metabolites. I. 2-Oxopropanal (NSC-79019)
    • Apple M.A., Greenberg D.M. Arrest of cancer in mice by therapy with normal metabolites. I. 2-Oxopropanal (NSC-79019). Cancer Chemother Rep 1967, 51:455-464.
    • (1967) Cancer Chemother Rep , vol.51 , pp. 455-464
    • Apple, M.A.1    Greenberg, D.M.2
  • 14
    • 0014665769 scopus 로고
    • Glyoxalase inhibitors as potential anticancer agents
    • Vince R., Wadd W.B. Glyoxalase inhibitors as potential anticancer agents. Biochem Biophys Res Commun 1969, 35:593-598.
    • (1969) Biochem Biophys Res Commun , vol.35 , pp. 593-598
    • Vince, R.1    Wadd, W.B.2
  • 16
    • 0018219280 scopus 로고
    • A re-evaluation on the distribution of glyoxalases in animal and tumor tissues
    • Jerzykowski T., Winter R., Matuszewski W., Piskorska D. A re-evaluation on the distribution of glyoxalases in animal and tumor tissues. Int J Biochem 1978, 9:853-860.
    • (1978) Int J Biochem , vol.9 , pp. 853-860
    • Jerzykowski, T.1    Winter, R.2    Matuszewski, W.3    Piskorska, D.4
  • 17
    • 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 1992, 44:2357-2363.
    • (1992) Biochem Pharmacol , vol.44 , pp. 2357-2363
    • Lo, T.W.C.1    Thornalley, P.J.2
  • 18
    • 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., et al. Antitumour activity of S-p-bromobenzylglutathione cyclopentyl diester in vitro and in vivo. Inhibition of glyoxalase I and induction of apoptosis. Biochem Pharmacol 1996, 51:1365-1372.
    • (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
  • 19
    • 0346422360 scopus 로고    scopus 로고
    • Bivalent transition-state analogue inhibitors of human glyoxalase I
    • Zheng Z.B., Creighton D.J. Bivalent transition-state analogue inhibitors of human glyoxalase I. Org Lett 2003, 5:4855-4858.
    • (2003) Org Lett , vol.5 , pp. 4855-4858
    • Zheng, Z.B.1    Creighton, D.J.2
  • 20
    • 68549094438 scopus 로고    scopus 로고
    • Inhibition of glyoxalase I: the first low-nanomolar tight-binding inhibitors
    • More S.S., Vince R. Inhibition of glyoxalase I: the first low-nanomolar tight-binding inhibitors. J Med Chem 2009, 52:4650-4656.
    • (2009) J Med Chem , vol.52 , pp. 4650-4656
    • More, S.S.1    Vince, R.2
  • 21
    • 0028100866 scopus 로고
    • Enhanced production of tumour necrosis factor α (TNF α) by its precursor on the cell surface of primed THP-1 cells
    • Tanabe Y., Kitahara-Tanabe N., Mizuno D., Soma G.-I. Enhanced production of tumour necrosis factor α (TNF α) by its precursor on the cell surface of primed THP-1 cells. Cytokine 1994, 6:337-348.
    • (1994) Cytokine , vol.6 , pp. 337-348
    • Tanabe, Y.1    Kitahara-Tanabe, N.2    Mizuno, D.3    Soma, G.-I.4
  • 22
    • 0034880918 scopus 로고    scopus 로고
    • Selective activation of apoptosis program by S-p-bromobenzylglutathione cyclopentyl diester in glyoxalase I-overexpressing human lung cancer cells
    • Sakamoto H., Mashima T., Sato S., Hashimoto Y., Yamori T., Tsuruo T. Selective activation of apoptosis program by S-p-bromobenzylglutathione cyclopentyl diester in glyoxalase I-overexpressing human lung cancer cells. Clin Cancer Res 2001, 7:2513-2518.
    • (2001) Clin Cancer Res , vol.7 , pp. 2513-2518
    • Sakamoto, H.1    Mashima, T.2    Sato, S.3    Hashimoto, Y.4    Yamori, T.5    Tsuruo, T.6
  • 23
    • 61849147844 scopus 로고    scopus 로고
    • Dicarbonyl-induced accelerated aging in vitro in human skin fibroblasts
    • Sejersen H., Rattan S. Dicarbonyl-induced accelerated aging in vitro in human skin fibroblasts. Biogerontology 2009, 10:203-211.
    • (2009) Biogerontology , vol.10 , pp. 203-211
    • Sejersen, H.1    Rattan, S.2
  • 24
    • 3042739537 scopus 로고    scopus 로고
    • Activation of antioxidant pathways in Ras-mediated oncogenic transformation of human surface ovarian epithelial cells revealed by functional proteomics and mass spectrometry
    • Young T.W., Mei F.C., Yang G., Thompson-Lanza J.A., Liu J., Cheng X. Activation of antioxidant pathways in Ras-mediated oncogenic transformation of human surface ovarian epithelial cells revealed by functional proteomics and mass spectrometry. Cancer Res 2004, 64:4577-4584.
    • (2004) Cancer Res , vol.64 , pp. 4577-4584
    • Young, T.W.1    Mei, F.C.2    Yang, G.3    Thompson-Lanza, J.A.4    Liu, J.5    Cheng, X.6
  • 25
    • 45149104139 scopus 로고    scopus 로고
    • A subcelluar proteomic investigation into vincristine-resistant gastric cancer cell line
    • Yang Y.X., Chen Z.C., Zhang G.Y., Yi H., Xiao Z.Q. A subcelluar proteomic investigation into vincristine-resistant gastric cancer cell line. J Cell Biochem 2008, 104:1010-1021.
    • (2008) J Cell Biochem , vol.104 , pp. 1010-1021
    • Yang, Y.X.1    Chen, Z.C.2    Zhang, G.Y.3    Yi, H.4    Xiao, Z.Q.5
  • 26
    • 0027454552 scopus 로고
    • The glyoxalase system in health and disease
    • Thornalley P.J. The glyoxalase system in health and disease. Mol Aspects Med 1993, 14:287-371.
    • (1993) Mol Aspects Med , vol.14 , pp. 287-371
    • Thornalley, P.J.1
  • 27
    • 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 1993, 212:101-105.
    • (1993) Eur J Biochem , vol.212 , pp. 101-105
    • Phillips, S.A.1    Thornalley, P.J.2
  • 28
    • 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 1988, 254:751-755.
    • (1988) Biochem J , vol.254 , pp. 751-755
    • Thornalley, P.J.1
  • 30
    • 0347419281 scopus 로고    scopus 로고
    • Glyoxalase I - structure, function and a critical role in the enzymatic defence against glycation
    • Thornalley P.J. Glyoxalase I - structure, function and a critical role in the enzymatic defence against glycation. Biochem Soc Trans 2003, 31:1343-1348.
    • (2003) Biochem Soc Trans , vol.31 , pp. 1343-1348
    • Thornalley, P.J.1
  • 31
    • 0348049818 scopus 로고    scopus 로고
    • The enzymatic defence against glycation in health, disease and therapeutics: a symposium to examine the concept
    • Thornalley P.J. The enzymatic defence against glycation in health, disease and therapeutics: a symposium to examine the concept. Biochem Soc Trans 2003, 31:1343-1348.
    • (2003) Biochem Soc Trans , vol.31 , pp. 1343-1348
    • Thornalley, P.J.1
  • 32
    • 0037093336 scopus 로고    scopus 로고
    • Assay of advanced glycation endproducts (AGEs): surveying AGEs by chromatographic assay with derivatisation by aminoquinolyl-N-hydroxysuccimidyl-carbamate and application to Ne{open}-carboxymethyl-lysine- and Ne{open}-(1-carboxyethyl)lysine-modified albumin
    • Ahmed N., Argirov O.K., Minhas H.S., Cordeiro C.A., Thornalley P.J. Assay of advanced glycation endproducts (AGEs): surveying AGEs by chromatographic assay with derivatisation by aminoquinolyl-N-hydroxysuccimidyl-carbamate and application to Ne{open}-carboxymethyl-lysine- and Ne{open}-(1-carboxyethyl)lysine-modified albumin. Biochem J 2002, 364:1-14.
    • (2002) Biochem J , vol.364 , pp. 1-14
    • Ahmed, N.1    Argirov, O.K.2    Minhas, H.S.3    Cordeiro, C.A.4    Thornalley, P.J.5
  • 33
    • 85029457779 scopus 로고    scopus 로고
    • Methylglyoxal, glyoxalase 1 and the dicarbonyl proteome. Amino Acids, in press.
    • Rabbani N, Thornalley PJ. Methylglyoxal, glyoxalase 1 and the dicarbonyl proteome. Amino Acids, in press.
    • Rabbani, N.1    Thornalley, P.J.2
  • 34
    • 77956522537 scopus 로고    scopus 로고
    • Imidazopurinones are markers of physiological genomic damage linked to DNA instability and glyoxalase 1-associated tumour multidrug resistance
    • Thornalley P.J., Waris S., Fleming T., Santarius T., Larkin S.J., Winklhofer-Roob B.M., et al. Imidazopurinones are markers of physiological genomic damage linked to DNA instability and glyoxalase 1-associated tumour multidrug resistance. Nucleic Acids Res 2010, gkq306.
    • (2010) Nucleic Acids Res
    • Thornalley, P.J.1    Waris, S.2    Fleming, T.3    Santarius, T.4    Larkin, S.J.5    Winklhofer-Roob, B.M.6
  • 35
    • 77956847849 scopus 로고    scopus 로고
    • LC-MS/MS analysis of carboxymethylated and carboxyethylated phosphatidylethanolamines in human erythrocytes and blood plasma
    • Shoji N., Nakagawa K., Asai A., Fujita I., Hashiura A., Nakajima Y., et al. LC-MS/MS analysis of carboxymethylated and carboxyethylated phosphatidylethanolamines in human erythrocytes and blood plasma. J Lipid Res 2010, 51:2445-2453.
    • (2010) J Lipid Res , vol.51 , pp. 2445-2453
    • Shoji, N.1    Nakagawa, K.2    Asai, A.3    Fujita, I.4    Hashiura, A.5    Nakajima, Y.6
  • 36
    • 0242468729 scopus 로고    scopus 로고
    • Quantitative screening of advanced glycation endproducts in cellular and extracellular proteins by tandem mass spectrometry
    • Thornalley P.J., Battah S., Ahmed N., Karachalias N., Agalou S., Babaei-Jadidi R., et al. Quantitative screening of advanced glycation endproducts in cellular and extracellular proteins by tandem mass spectrometry. Biochem J 2003, 375:581-592.
    • (2003) Biochem J , vol.375 , pp. 581-592
    • Thornalley, P.J.1    Battah, S.2    Ahmed, N.3    Karachalias, N.4    Agalou, S.5    Babaei-Jadidi, R.6
  • 37
    • 33747080843 scopus 로고    scopus 로고
    • Increased dicarbonyl metabolism in endothelial cells in hyperglycemia induces anoikis and impairs angiogenesis by RGD and GFOGER motif modification
    • Dobler D., Ahmed N., Song L.J., Eboigbodin K.E., Thornalley P.J. Increased dicarbonyl metabolism in endothelial cells in hyperglycemia induces anoikis and impairs angiogenesis by RGD and GFOGER motif modification. Diabetes 2006, 55:1961-1969.
    • (2006) Diabetes , vol.55 , pp. 1961-1969
    • Dobler, D.1    Ahmed, N.2    Song, L.J.3    Eboigbodin, K.E.4    Thornalley, P.J.5
  • 38
    • 43449094351 scopus 로고    scopus 로고
    • Protein and nucleotide damage by glyoxal and methylglyoxal in physiological systems - role in ageing and disease
    • Thornalley P.J. Protein and nucleotide damage by glyoxal and methylglyoxal in physiological systems - role in ageing and disease. Drug Metab Drug Interact 2008, 23:125-150.
    • (2008) Drug Metab Drug Interact , vol.23 , pp. 125-150
    • Thornalley, P.J.1
  • 39
    • 33847078455 scopus 로고    scopus 로고
    • Apoptotic signaling in methylglyoxal-treated human osteoblasts involves oxidative stress, c-jun N-terminal kinase, caspase-3, and p21-activated kinase 2
    • Chan W.H., Wu H.J., Shiao N.H. Apoptotic signaling in methylglyoxal-treated human osteoblasts involves oxidative stress, c-jun N-terminal kinase, caspase-3, and p21-activated kinase 2. J Cell Biochem 2007, 100:1056-1069.
    • (2007) J Cell Biochem , vol.100 , pp. 1056-1069
    • Chan, W.H.1    Wu, H.J.2    Shiao, N.H.3
  • 40
    • 0027322179 scopus 로고
    • Inhibition of proliferation of human leukaemia 60 cells by methylglyoxal in vitro
    • Ayoub F.M., Allen R.E., Thornalley P.J. Inhibition of proliferation of human leukaemia 60 cells by methylglyoxal in vitro. Leuk Res 1993, 17:397-401.
    • (1993) Leuk Res , vol.17 , pp. 397-401
    • Ayoub, F.M.1    Allen, R.E.2    Thornalley, P.J.3
  • 42
    • 8144228566 scopus 로고    scopus 로고
    • Why do cancers have high aerobic glycolysis?
    • Gatenby R.A., Gillies R.J. Why do cancers have high aerobic glycolysis?. Nat Rev Cancer 2004, 4:891-899.
    • (2004) Nat Rev Cancer , vol.4 , pp. 891-899
    • Gatenby, R.A.1    Gillies, R.J.2
  • 43
    • 77949967131 scopus 로고    scopus 로고
    • Targeting metabolic transformation for cancer therapy
    • Tennant D.A., Duran R.V., Gottlieb E. Targeting metabolic transformation for cancer therapy. Nat Rev Cancer 2010, 10:267-277.
    • (2010) Nat Rev Cancer , vol.10 , pp. 267-277
    • Tennant, D.A.1    Duran, R.V.2    Gottlieb, E.3
  • 45
    • 0029035975 scopus 로고
    • Glyoxalase I in detoxification: studies using a glyoxalase I transfectant cell line
    • Ranganathan S., Walsh E.S., Tew K.D. Glyoxalase I in detoxification: studies using a glyoxalase I transfectant cell line. Biochem J 1995, 309:127-131.
    • (1995) Biochem J , vol.309 , pp. 127-131
    • Ranganathan, S.1    Walsh, E.S.2    Tew, K.D.3
  • 46
    • 0034657445 scopus 로고    scopus 로고
    • Glyoxalase I is involved in resistance of human leukemia cells to antitumour agent-induced apoptosis
    • Sakamoto H., Mashima T., Kazaki A., Dan S., Hashimoto Y., Naito M., et al. Glyoxalase I is involved in resistance of human leukemia cells to antitumour agent-induced apoptosis. Blood 2000, 95:3214-3218.
    • (2000) Blood , vol.95 , pp. 3214-3218
    • Sakamoto, H.1    Mashima, T.2    Kazaki, A.3    Dan, S.4    Hashimoto, Y.5    Naito, M.6
  • 47
    • 0032958532 scopus 로고    scopus 로고
    • Magnetic resonance detects metabolic changes associated with chemotherapy-induced apoptosis
    • Ronen S.M., DiStefano F., McCoy C.L., Robertson D., Smith T.A.D., Al-Saffar N.M., et al. Magnetic resonance detects metabolic changes associated with chemotherapy-induced apoptosis. Brit J Cancer 1999, 80:1035-1041.
    • (1999) Brit J Cancer , vol.80 , pp. 1035-1041
    • Ronen, S.M.1    DiStefano, F.2    McCoy, C.L.3    Robertson, D.4    Smith, T.A.D.5    Al-Saffar, N.M.6
  • 48
    • 22144477159 scopus 로고    scopus 로고
    • S-nitrosylated GAPDH initiates apoptotic cell death by nuclear translocation following Siah1 binding
    • Hara M.R., Agrawal N., Kim S.F., Cascio M.B., Fujimuro M., Ozeki Y., et al. S-nitrosylated GAPDH initiates apoptotic cell death by nuclear translocation following Siah1 binding. Nat Cell Biol 2005, 7:665-740.
    • (2005) Nat Cell Biol , vol.7 , pp. 665-740
    • Hara, M.R.1    Agrawal, N.2    Kim, S.F.3    Cascio, M.B.4    Fujimuro, M.5    Ozeki, Y.6
  • 51
    • 0037096742 scopus 로고    scopus 로고
    • Genotoxic exposure is associated with alterations in glucose uptake and metabolism
    • Zhou R., Vander Heiden M.G., Rudin C.M. Genotoxic exposure is associated with alterations in glucose uptake and metabolism. Cancer Res 2002, 62:3515-3520.
    • (2002) Cancer Res , vol.62 , pp. 3515-3520
    • Zhou, R.1    Vander Heiden, M.G.2    Rudin, C.M.3
  • 52
    • 0025124156 scopus 로고
    • An evaluation of the role of glutathione and its associated enzymes in the expression of differential sensitivities to antitumor agents shown by a range of human tumor-cell lines
    • Hosking L.K., Whelan R.D.H., Shellard S.A., Bedford P., Hill B.T. An evaluation of the role of glutathione and its associated enzymes in the expression of differential sensitivities to antitumor agents shown by a range of human tumor-cell lines. Biochem Pharmacol 1990, 40:1833-1842.
    • (1990) Biochem Pharmacol , vol.40 , pp. 1833-1842
    • Hosking, L.K.1    Whelan, R.D.H.2    Shellard, S.A.3    Bedford, P.4    Hill, B.T.5
  • 53
    • 0033567419 scopus 로고    scopus 로고
    • Accumulation of α-oxoaldehydes during oxidative stress. A role in cytotoxicity
    • Abordo E.A., Minhas H.S., Thornalley P.J. Accumulation of α-oxoaldehydes during oxidative stress. A role in cytotoxicity. Biochem Pharmacol 1999, 58:641-648.
    • (1999) Biochem Pharmacol , vol.58 , pp. 641-648
    • Abordo, E.A.1    Minhas, H.S.2    Thornalley, P.J.3
  • 56
    • 77953470459 scopus 로고    scopus 로고
    • Autophagy: cancer therapy's friend or foe?
    • Grander D., Panaretakis T. Autophagy: cancer therapy's friend or foe?. Future Med Chem 2010, 2:285-297.
    • (2010) Future Med Chem , vol.2 , pp. 285-297
    • Grander, D.1    Panaretakis, T.2
  • 59
    • 0037169509 scopus 로고    scopus 로고
    • Methylglyoxal enhances cisplatin-induced cytotoxicity by activating protein kinase C delta
    • Godbout J.P., Pesavento J., Hartman M.E., Manson S.R., Freund G.G. Methylglyoxal enhances cisplatin-induced cytotoxicity by activating protein kinase C delta. J Biol Chem 2002, 277:2554-2561.
    • (2002) J Biol Chem , vol.277 , pp. 2554-2561
    • Godbout, J.P.1    Pesavento, J.2    Hartman, M.E.3    Manson, S.R.4    Freund, G.G.5
  • 60
    • 0038237433 scopus 로고    scopus 로고
    • Protein kinase C delta is responsible for constitutive and DNA damage-induced phosphorylation of Rad9
    • Yoshida K., Wang H.G., Miki Y., Kufe D. Protein kinase C delta is responsible for constitutive and DNA damage-induced phosphorylation of Rad9. EMBO J 2003, 22:1431-1441.
    • (2003) EMBO J , vol.22 , pp. 1431-1441
    • Yoshida, K.1    Wang, H.G.2    Miki, Y.3    Kufe, D.4
  • 61
    • 33748752328 scopus 로고    scopus 로고
    • Glyoxalase II, a detoxifying enzyme of glycolysis byproduct methylglyoxal and a target of p63 and p73, is a pro-survival factor of the p53 family
    • Xu Y., Chen X. Glyoxalase II, a detoxifying enzyme of glycolysis byproduct methylglyoxal and a target of p63 and p73, is a pro-survival factor of the p53 family. J Biol Chem 2006, 281:26702-26713.
    • (2006) J Biol Chem , vol.281 , pp. 26702-26713
    • Xu, Y.1    Chen, X.2
  • 62
    • 0032787281 scopus 로고    scopus 로고
    • Tissue microarrays for gene amplification surveys in many different tumor types
    • Schraml P., Kononen J., Bubendorf L., Moch H., Bissig H., Nocito A., et al. Tissue microarrays for gene amplification surveys in many different tumor types. Clin Cancer Res 1999, 5:1966-1975.
    • (1999) Clin Cancer Res , vol.5 , pp. 1966-1975
    • Schraml, P.1    Kononen, J.2    Bubendorf, L.3    Moch, H.4    Bissig, H.5    Nocito, A.6
  • 63
    • 33645941224 scopus 로고    scopus 로고
    • Protective effects of garlic sulfur compounds against DNA damage induced by direct- and indirect-acting genotoxic agents in HepG2 cells
    • Belloir C., Singh V., Daurat C., Siess M.H., Le Bon A.M. Protective effects of garlic sulfur compounds against DNA damage induced by direct- and indirect-acting genotoxic agents in HepG2 cells. Food Chem Toxicol 2006, 44:827-834.
    • (2006) Food Chem Toxicol , vol.44 , pp. 827-834
    • Belloir, C.1    Singh, V.2    Daurat, C.3    Siess, M.H.4    Le Bon, A.M.5
  • 64
    • 28644438067 scopus 로고    scopus 로고
    • Proteomic analysis on metastasis-associated proteins of human hepatocellular carcinoma tissues
    • Song H.Y., Liu Y.K., Feng J.T., Cui J.F., Dai Z., Zhang L.J., et al. Proteomic analysis on metastasis-associated proteins of human hepatocellular carcinoma tissues. J Cancer Res Clin Oncol 2006, 132:92-98.
    • (2006) J Cancer Res Clin Oncol , vol.132 , pp. 92-98
    • Song, H.Y.1    Liu, Y.K.2    Feng, J.T.3    Cui, J.F.4    Dai, Z.5    Zhang, L.J.6
  • 65
    • 1842484829 scopus 로고    scopus 로고
    • Genome-wide cDNA microarray analysis of gene expression profiles in pancreatic cancers using populations of tumor cells and normal ductal epithelial cells selected for purity by laser microdissection
    • Nakamura T., Furukawa Y., Nakagawa H., Tsunoda T., Ohigashi H., Murata K., et al. Genome-wide cDNA microarray analysis of gene expression profiles in pancreatic cancers using populations of tumor cells and normal ductal epithelial cells selected for purity by laser microdissection. Oncogene 2004, 23:2385-2400.
    • (2004) Oncogene , vol.23 , pp. 2385-2400
    • Nakamura, T.1    Furukawa, Y.2    Nakagawa, H.3    Tsunoda, T.4    Ohigashi, H.5    Murata, K.6
  • 66
    • 5344234075 scopus 로고    scopus 로고
    • Methotrexate inhibits the glyoxalase system in vivo in children with acute lymphoid leukaemia
    • Bartyik K., Turi S., Orosz F., Karg E. Methotrexate inhibits the glyoxalase system in vivo in children with acute lymphoid leukaemia. Eur J Cancer 2004, 40:2287-2292.
    • (2004) Eur J Cancer , vol.40 , pp. 2287-2292
    • Bartyik, K.1    Turi, S.2    Orosz, F.3    Karg, E.4
  • 67
    • 0015055115 scopus 로고
    • Studies on the inhibition of glyoxalase I by S-substituted glutathione
    • Vince R., Daluge S., Wadd W.B. Studies on the inhibition of glyoxalase I by S-substituted glutathione. J Med Chem 1971, 14:402-404.
    • (1971) J Med Chem , vol.14 , pp. 402-404
    • Vince, R.1    Daluge, S.2    Wadd, W.B.3
  • 68
    • 0028237443 scopus 로고
    • S-(N-aryl-N-hydroxycarbamoyl)glutathione derivatives are tight-binding inhibitors of glyoxalase-I and Slow substrates for glyoxalase-Ii
    • Murthy N.S.R.K., Bakeris T., Kavarana M.J., Hamilton D.S., Lan Y., Creighton D.J. S-(N-aryl-N-hydroxycarbamoyl)glutathione derivatives are tight-binding inhibitors of glyoxalase-I and Slow substrates for glyoxalase-Ii. J Med Chem 1994, 37:2161-2166.
    • (1994) J Med Chem , vol.37 , pp. 2161-2166
    • Murthy, N.S.R.K.1    Bakeris, T.2    Kavarana, M.J.3    Hamilton, D.S.4    Lan, Y.5    Creighton, D.J.6
  • 69
  • 70
    • 0032907791 scopus 로고    scopus 로고
    • Mechanism-based competitive inhibitors of glyoxalase I: intracellular delivery, in vitro antitumor activities, and stabilities in human serum and mouse serum
    • Kavarana M.J., Kovaleva E.G., Creighton D.J., Wollman M.B., Eiseman J.L. Mechanism-based competitive inhibitors of glyoxalase I: intracellular delivery, in vitro antitumor activities, and stabilities in human serum and mouse serum. J Med Chem 1999, 42:221-228.
    • (1999) J Med Chem , vol.42 , pp. 221-228
    • Kavarana, M.J.1    Kovaleva, E.G.2    Creighton, D.J.3    Wollman, M.B.4    Eiseman, J.L.5
  • 71
    • 55649097940 scopus 로고    scopus 로고
    • Curcumin inhibits glyoxalase 1: a possible link to its anti-inflammatory and anti-tumor activity
    • Santel T., Pflug G., Hemdan N.Y.A., Schafer A., Hollenbach M., Buchold M., et al. Curcumin inhibits glyoxalase 1: a possible link to its anti-inflammatory and anti-tumor activity. PLoS One 2008, 3.
    • (2008) PLoS One , pp. 3
    • Santel, T.1    Pflug, G.2    Hemdan, N.Y.A.3    Schafer, A.4    Hollenbach, M.5    Buchold, M.6
  • 72
    • 77953619656 scopus 로고    scopus 로고
    • Glyoxalase-I is a novel target against Bcr-Abl(+) leukemic cells acquiring stem-like characteristics in a hypoxic environment
    • Takeuchi M., Kimura S., Kuroda J., Ashihara E., Kawatani M., Osada H., et al. Glyoxalase-I is a novel target against Bcr-Abl(+) leukemic cells acquiring stem-like characteristics in a hypoxic environment. Cell Death Diff 2010, 17:1211-1220.
    • (2010) Cell Death Diff , vol.17 , pp. 1211-1220
    • Takeuchi, M.1    Kimura, S.2    Kuroda, J.3    Ashihara, E.4    Kawatani, M.5    Osada, H.6
  • 73
    • 79955979357 scopus 로고    scopus 로고
    • Hypoxia-adapted CML cells are more primitive population and are eradicated by glyoxalase-1 inhibitors
    • Takeuchi M., Kimura S., Kuroda J., Ashihara E., Kawatani M., Osada H., et al. Hypoxia-adapted CML cells are more primitive population and are eradicated by glyoxalase-1 inhibitors. Blood 2009, 114:852-853.
    • (2009) Blood , vol.114 , pp. 852-853
    • Takeuchi, M.1    Kimura, S.2    Kuroda, J.3    Ashihara, E.4    Kawatani, M.5    Osada, H.6
  • 74
    • 0036711284 scopus 로고    scopus 로고
    • Differing expression of enzymes of the glyoxalase system in superficial and invasive bladder carcinomas
    • Mearini E., Romani R., Mearini L., Antognelli C., Zucchi A., Baroni T., et al. Differing expression of enzymes of the glyoxalase system in superficial and invasive bladder carcinomas. Eur J Cancer 2002, 38:1946-1950.
    • (2002) Eur J Cancer , vol.38 , pp. 1946-1950
    • Mearini, E.1    Romani, R.2    Mearini, L.3    Antognelli, C.4    Zucchi, A.5    Baroni, T.6
  • 76
    • 28644439593 scopus 로고    scopus 로고
    • Proteomic study reveals that proteins involved in metabolic and detoxification pathways are highly expressed in HER-2/neu-positive breast cancer
    • Zhang D., Tai L.K., Wong L.L., Chiu L.L., Sethi S.K., Koay E.S.C. Proteomic study reveals that proteins involved in metabolic and detoxification pathways are highly expressed in HER-2/neu-positive breast cancer. Mol Cell Proteomics 2005, 4:1686-1696.
    • (2005) Mol Cell Proteomics , vol.4 , pp. 1686-1696
    • Zhang, D.1    Tai, L.K.2    Wong, L.L.3    Chiu, L.L.4    Sethi, S.K.5    Koay, E.S.C.6
  • 77
    • 0011867616 scopus 로고
    • Analysis of glyoxalase I from normal and tumour tissue from human colon
    • Ranganathan S., Tew K.D. Analysis of glyoxalase I from normal and tumour tissue from human colon. Biochim Biophys Acta 1994, 1170:17-24.
    • (1994) Biochim Biophys Acta , vol.1170 , pp. 17-24
    • Ranganathan, S.1    Tew, K.D.2
  • 78
    • 6044263660 scopus 로고    scopus 로고
    • Proteomic analysis of human acute leukemia cells: insight into their classification
    • Cui J.W., Wang J., He K., Jin B.F., Wang H.X., Li W., et al. Proteomic analysis of human acute leukemia cells: insight into their classification. Clin Cancer Res 2004, 10:6887-6896.
    • (2004) Clin Cancer Res , vol.10 , pp. 6887-6896
    • Cui, J.W.1    Wang, J.2    He, K.3    Jin, B.F.4    Wang, H.X.5    Li, W.6
  • 79
    • 0023707797 scopus 로고
    • Modification of the glyoxalase system in human HL60 promyelocytic leukaemia cells during differentiation to neutrophils in vitro
    • Hooper N.I., Tisdale M.J., Thornalley P.J. Modification of the glyoxalase system in human HL60 promyelocytic leukaemia cells during differentiation to neutrophils in vitro. Biochim Biophys Acta 1988, 966:362-369.
    • (1988) Biochim Biophys Acta , vol.966 , pp. 362-369
    • Hooper, N.I.1    Tisdale, M.J.2    Thornalley, P.J.3
  • 80
    • 10744219705 scopus 로고    scopus 로고
    • Tissue-wide expression profiling using cDNA subtraction and microarrays to identify tumor-specific genes
    • Amatschek S., Koenig U., Auer H., Steinlein P., Pacher M., Gruenfelder A., et al. Tissue-wide expression profiling using cDNA subtraction and microarrays to identify tumor-specific genes. Cancer Res 2004, 64:844-856.
    • (2004) Cancer Res , vol.64 , pp. 844-856
    • Amatschek, S.1    Koenig, U.2    Auer, H.3    Steinlein, P.4    Pacher, M.5    Gruenfelder, A.6
  • 81
    • 0036210918 scopus 로고    scopus 로고
    • Proteomic analysis and identification of new biomarkers antherpaeutic agents for invasive ovarian cancer
    • Jones M.B., Krutzsch H., Shu H., Zhao Y., Liotta L.A., Kohn E.C., et al. Proteomic analysis and identification of new biomarkers antherpaeutic agents for invasive ovarian cancer. Proteomics 2002, 2:78-84.
    • (2002) Proteomics , vol.2 , pp. 78-84
    • Jones, M.B.1    Krutzsch, H.2    Shu, H.3    Zhao, Y.4    Liotta, L.A.5    Kohn, E.C.6
  • 82
    • 0033074352 scopus 로고    scopus 로고
    • Glyoxalase I activity in human prostate cancer: a potential marker and importance in chemotherapy
    • Davidson S.D., Cherry J.P., Choudhury M.S., Tazaki H., Mallouh C., Konno S. Glyoxalase I activity in human prostate cancer: a potential marker and importance in chemotherapy. J Urol 1999, 161:690-691.
    • (1999) J Urol , vol.161 , pp. 690-691
    • Davidson, S.D.1    Cherry, J.P.2    Choudhury, M.S.3    Tazaki, H.4    Mallouh, C.5    Konno, S.6
  • 83
    • 0027513983 scopus 로고
    • A simplified method for the purification of human red blood cell glyoxalase I. Characteristics, immunoblotting and inhibitor studies
    • Allen R.E., Lo T.W.C., Thornalley P.J. A simplified method for the purification of human red blood cell glyoxalase I. Characteristics, immunoblotting and inhibitor studies. J Prot Chem 1993, 12:111-119.
    • (1993) J Prot Chem , vol.12 , pp. 111-119
    • Allen, R.E.1    Lo, T.W.C.2    Thornalley, P.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.