메뉴 건너뛰기




Volumn 34, Issue 2, 2012, Pages 117-126

Methylglyoxal has deleterious effects on thioredoxin in human aortic endothelial cells

Author keywords

Apoptosis; Human aortic endothelial cells; Methylglyoxal; Oxidative stress; Peroxiredoxin; Thioredoxin

Indexed keywords

CYTOCHROME C; LIPOCORTIN 5; METHYLGLYOXAL; PEROXIREDOXIN; PROPIDIUM IODIDE; REACTIVE OXYGEN METABOLITE; THIOREDOXIN; MESSENGER RNA; 3 DEOXYGLUCOSONE; GLYOXAL; HYDROETHIDINE;

EID: 84859736570     PISSN: 13826689     EISSN: 18727077     Source Type: Journal    
DOI: 10.1016/j.etap.2012.03.007     Document Type: Article
Times cited : (19)

References (48)
  • 2
    • 67349155642 scopus 로고    scopus 로고
    • The oligomeric conformation of peroxiredoxins links redox state to function
    • Barranco-Medina, S., Lazaro, J.J., Dietz, K.J., 2009. The oligomeric conformation of peroxiredoxins links redox state to function. FEBS Lett. 583, 1809-1816.
    • (2009) FEBS Lett , vol.583 , pp. 1809-1816
    • Barranco-Medina, S.1    Lazaro, J.J.2    Dietz, K.J.3
  • 4
    • 33847746679 scopus 로고    scopus 로고
    • Thiol-based mechanisms of the thioredoxin and glutaredoxin systems: implications for diseases in the cardiovascular system
    • Berndt, C., Lillig, C.H., Holmgren, A., 2007. Thiol-based mechanisms of the thioredoxin and glutaredoxin systems: implications for diseases in the cardiovascular system. Am. J. Physiol. Heart Circ. Physiol. 292, H1227-H1236.
    • (2007) Am. J. Physiol. Heart Circ. Physiol. , vol.292
    • Berndt, C.1    Lillig, C.H.2    Holmgren, A.3
  • 6
    • 0035856980 scopus 로고    scopus 로고
    • Biochemistry and molecular cell biology of diabetic complications
    • Brownlee, M., 2001. Biochemistry and molecular cell biology of diabetic complications. Nature 414, 813-820.
    • (2001) Nature , vol.414 , pp. 813-820
    • Brownlee, M.1
  • 7
    • 35248871238 scopus 로고    scopus 로고
    • Methylglyoxal induces advanced glycation end product (AGEs) formation and dysfunction of PDGF receptor-beta: implications for diabetic atherosclerosis
    • Cantero, A.V., Portero-Otín, M., Ayala, V., Auge, N., Sanson, M., Elbaz, M., Thiers, J.C., Pamplona, R., Salvayre, R., Nègre-Salvayre, A., 2007. Methylglyoxal induces advanced glycation end product (AGEs) formation and dysfunction of PDGF receptor-beta: implications for diabetic atherosclerosis. FASEB J. 21, 3096-3106.
    • (2007) FASEB J , vol.21 , pp. 3096-3106
    • Cantero, A.V.1    Portero-Otín, M.2    Ayala, V.3    Auge, N.4    Sanson, M.5    Elbaz, M.6    Thiers, J.C.7    Pamplona, R.8    Salvayre, R.9    Nègre-Salvayre, A.10
  • 8
    • 33748578688 scopus 로고    scopus 로고
    • Controlling oxidative stress as a novel molecular approach to protecting the vascular wall in diabetes
    • Ceriello, A., 2006. Controlling oxidative stress as a novel molecular approach to protecting the vascular wall in diabetes. Curr. Opin. Lipidol. 17, 510-518.
    • (2006) Curr. Opin. Lipidol. , vol.17 , pp. 510-518
    • Ceriello, A.1
  • 9
    • 34248162057 scopus 로고    scopus 로고
    • Methylglyoxal, oxidative stress, and hypertension
    • Chang, T., Wu, L., 2006. Methylglyoxal, oxidative stress, and hypertension. Can. J. Physiol. Pharmacol. 84, 1229-1238.
    • (2006) Can. J. Physiol. Pharmacol. , vol.84 , pp. 1229-1238
    • Chang, T.1    Wu, L.2
  • 10
    • 0032510747 scopus 로고    scopus 로고
    • Evidence of high levels of methylglyoxal in cultured Chinese hamster ovary cells
    • Chaplen, F.W., Fahl, W.E., Cameron, D.C., 1998. Evidence of high levels of methylglyoxal in cultured Chinese hamster ovary cells. Proc. Natl. Acad. Sci. U.S.A. 95, 5533-5538.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 5533-5538
    • Chaplen, F.W.1    Fahl, W.E.2    Cameron, D.C.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. The involvement of reactive oxygen species formation and a possible implication for atherogenesis in diabetes
    • Che, W., Asahi, M., Takahashi, M., Kaneto, H., Okado, A., Higashiyama, S., Taniguchi, N., 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, 18453-18459.
    • (1997) J. Biol. Chem. , vol.272 , pp. 18453-18459
    • Che, W.1    Asahi, M.2    Takahashi, M.3    Kaneto, H.4    Okado, A.5    Higashiyama, S.6    Taniguchi, N.7
  • 12
    • 0022614962 scopus 로고
    • Determination of the number of endothelial cells in culture using an acid phosphatase assay
    • Connolly, D.T., Knight, M.B., Harakas, N.K., Wittwer, A.J., Feder, J., 1986. Determination of the number of endothelial cells in culture using an acid phosphatase assay. Anal. Biochem. 152, 136-140.
    • (1986) Anal. Biochem. , vol.152 , pp. 136-140
    • Connolly, D.T.1    Knight, M.B.2    Harakas, N.K.3    Wittwer, A.J.4    Feder, J.5
  • 14
    • 39949083765 scopus 로고    scopus 로고
    • Oxidation of mitochondrial peroxiredoxin 3 during the initiation of receptor-mediated apoptosis
    • Cox, A.G., Pullar, J.M., Hughes, G., Ledgerwood, E.C., Hampton, M.B., 2008. Oxidation of mitochondrial peroxiredoxin 3 during the initiation of receptor-mediated apoptosis. Free Radic. Biol. Med. 44, 1001-1009.
    • (2008) Free Radic. Biol. Med. , vol.44 , pp. 1001-1009
    • Cox, A.G.1    Pullar, J.M.2    Hughes, G.3    Ledgerwood, E.C.4    Hampton, M.B.5
  • 15
  • 18
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • Green, D.R., Reed, J.C., 1998. Mitochondria and apoptosis. Science 281, 1309-1312.
    • (1998) Science , vol.281 , pp. 1309-1312
    • Green, D.R.1    Reed, J.C.2
  • 19
    • 33745288178 scopus 로고    scopus 로고
    • Antibodies and Fab fragments protect Cu, Zn-SOD against methylglyoxal-induced inactivation
    • Jabeen, R., Mohammad, A.A., Elefano, E.C., Petersen, J.R., Saleemuddin, M., 2006. Antibodies and Fab fragments protect Cu, Zn-SOD against methylglyoxal-induced inactivation. Biochim. Biophys. Acta 1760, 1167-1174.
    • (2006) Biochim. Biophys. Acta , vol.1760 , pp. 1167-1174
    • Jabeen, R.1    Mohammad, A.A.2    Elefano, E.C.3    Petersen, J.R.4    Saleemuddin, M.5
  • 21
    • 43449101902 scopus 로고    scopus 로고
    • Methylglyoxal and glucose metabolism: a historical perspective and future avenues for research
    • Kalapos, M.P., 2008. Methylglyoxal and glucose metabolism: a historical perspective and future avenues for research. Drug Metabol. Drug Interact. 23, 69-91.
    • (2008) Drug Metabol. Drug Interact. , vol.23 , pp. 69-91
    • Kalapos, M.P.1
  • 22
    • 0042807630 scopus 로고    scopus 로고
    • The thioredoxin-thioredoxin reductase system: over-expression in human cancer
    • Lincoln, D.T., Ali Emadi, E.M., Tonissen, K.F., Clarke, F.M., 2003. The thioredoxin-thioredoxin reductase system: over-expression in human cancer. Anticancer Res. 23, 2425-2433.
    • (2003) Anticancer Res , vol.23 , pp. 2425-2433
    • Lincoln, D.T.1    Ali Emadi, E.M.2    Tonissen, K.F.3    Clarke, F.M.4
  • 23
    • 0037188936 scopus 로고    scopus 로고
    • Thioredoxin promotes ASK1 ubiquitination and degradation to inhibit ASK1-mediated apoptosis in a redox activity-independent manner
    • Liu, Y., Min, W., 2002. Thioredoxin promotes ASK1 ubiquitination and degradation to inhibit ASK1-mediated apoptosis in a redox activity-independent manner. Circ. Res. 90, 1259-1266.
    • (2002) Circ. Res. , vol.90 , pp. 1259-1266
    • Liu, Y.1    Min, W.2
  • 24
    • 0028292698 scopus 로고
    • Glyoxalase system in clinical diabetes mellitus and correlation with diabetic complications
    • McLellan, A.C., Thornalley, P.J., Benn, J., Sonksen, P.H., 1994. Glyoxalase system in clinical diabetes mellitus and correlation with diabetic complications. Clin. Sci. (Lond.) 87, 21-29.
    • (1994) Clin. Sci. (Lond.) , vol.87 , pp. 21-29
    • McLellan, A.C.1    Thornalley, P.J.2    Benn, J.3    Sonksen, P.H.4
  • 25
    • 36349027005 scopus 로고    scopus 로고
    • Determination of glyoxal and methylglyoxal in the serum of diabetic patients by MEKC using stilbenediamine as derivatizing reagent
    • Mirza, M.A., Kandhro, A.J., Memon, S.Q., Khuhawar, M.Y., Arain, R., 2007. Determination of glyoxal and methylglyoxal in the serum of diabetic patients by MEKC using stilbenediamine as derivatizing reagent. Electrophoresis 28, 3940-3947.
    • (2007) Electrophoresis , vol.28 , pp. 3940-3947
    • Mirza, M.A.1    Kandhro, A.J.2    Memon, S.Q.3    Khuhawar, M.Y.4    Arain, R.5
  • 26
    • 65449117618 scopus 로고    scopus 로고
    • Methylglyoxal inhibits smooth muscle contraction in isolated blood vessels
    • Mukohda, M., Yamawaki, H., Nomura, H., Okada, M., Hara, Y., 2009. Methylglyoxal inhibits smooth muscle contraction in isolated blood vessels. J. Pharmacol. Sci. 109, 305-310.
    • (2009) J. Pharmacol. Sci. , vol.109 , pp. 305-310
    • Mukohda, M.1    Yamawaki, H.2    Nomura, H.3    Okada, M.4    Hara, Y.5
  • 27
    • 58649096345 scopus 로고    scopus 로고
    • The effects of acrolein on peroxiredoxins, thioredoxins, and thioredoxin reductase in human bronchial epithelial cells
    • Myers, C.R., Myers, J.M., 2009. The effects of acrolein on peroxiredoxins, thioredoxins, and thioredoxin reductase in human bronchial epithelial cells. Toxicology 257, 95-104.
    • (2009) Toxicology , vol.257 , pp. 95-104
    • Myers, C.R.1    Myers, J.M.2
  • 30
    • 0033525849 scopus 로고    scopus 로고
    • Increase in three α,β-dicarbonyl compound levels in human uremic plasma: specific in vivo determination of intermediates in advanced Maillard reaction
    • Odani, H., Shinzato, T., Matsumoto, Y., Usami, J., Maeda, K., 1999. Increase in three α,β-dicarbonyl compound levels in human uremic plasma: specific in vivo determination of intermediates in advanced Maillard reaction. Biochem. Biophys. Res. Commun. 256, 89-93.
    • (1999) Biochem. Biophys. Res. Commun. , vol.256 , pp. 89-93
    • Odani, H.1    Shinzato, T.2    Matsumoto, Y.3    Usami, J.4    Maeda, K.5
  • 33
    • 0037306962 scopus 로고    scopus 로고
    • Identification of the binding site of methylglyoxal on glutathione peroxidase: methylglyoxal inhibits glutathione peroxidase activity via binding to glutathione binding sites Arg 184 and 185
    • Park, Y.S., Koh, Y.H., Takahashi, M., Miyamoto, Y., Suzuki, K., Dohmae, N., Takio, K., Honke, K., Taniguchi, N., 2003. Identification of the binding site of methylglyoxal on glutathione peroxidase: methylglyoxal inhibits glutathione peroxidase activity via binding to glutathione binding sites Arg 184 and 185. Free Radic. Res. 37, 205-211.
    • (2003) Free Radic. Res , vol.37 , pp. 205-211
    • Park, Y.S.1    Koh, Y.H.2    Takahashi, M.3    Miyamoto, Y.4    Suzuki, K.5    Dohmae, N.6    Takio, K.7    Honke, K.8    Taniguchi, N.9
  • 36
    • 62149135335 scopus 로고    scopus 로고
    • N- terminal 2, 3-diaminopropionic acid (Dap) peptides as efficient methylglyoxal scavengers to inhibit advanced glycation endproduct (AGE) formation
    • Sasaki, N.A., Garcia-Alvarez, M.C., Wang, Q., Ermolenko, L., Franck, G., Nhiri, N., Martin, M.T., Audic, N., Potier, P., 2009. N-terminal 2,3-diaminopropionic acid (Dap) peptides as efficient methylglyoxal scavengers to inhibit advanced glycation endproduct (AGE) formation. Bioorg. Med. Chem. 17, 2310-2320.
    • (2009) Bioorg. Med. Chem. , vol.17 , pp. 2310-2320
    • Sasaki, N.A.1    Garcia-Alvarez, M.C.2    Wang, Q.3    Ermolenko, L.4    Franck, G.5    Nhiri, N.6    Martin, M.T.7    Audic, N.8    Potier, P.9
  • 37
    • 3142751251 scopus 로고    scopus 로고
    • Hyperglycemia promotes oxidative stress through inhibition of thioredoxin function by thioredoxin-interacting protein
    • Schulze, P.C., Yoshioka, J., Takahashi, T., He, Z., King, G.L., Lee, R.T., 2004. Hyperglycemia promotes oxidative stress through inhibition of thioredoxin function by thioredoxin-interacting protein. J. Biol. Chem. 279, 30369-30374.
    • (2004) J. Biol. Chem. , vol.279 , pp. 30369-30374
    • Schulze, P.C.1    Yoshioka, J.2    Takahashi, T.3    He, Z.4    King, G.L.5    Lee, R.T.6
  • 39
    • 0032032578 scopus 로고    scopus 로고
    • Overexpression of glyoxalase-I in bovine endothelial cells inhibits intracellular advanced glycation endproduct formation and prevents hyperglycemia-induced increases in macromolecular endocytosis
    • Shinohara, M., Thornalley, P.J., Giardino, I., Beisswenger, P., Thorpe, S.R., Onorato, J., Brownlee, M., 1998. Overexpression of glyoxalase-I in bovine endothelial cells inhibits intracellular advanced glycation endproduct formation and prevents hyperglycemia-induced increases in macromolecular endocytosis. J. Clin. Invest. 101, 1142-1147.
    • (1998) J. Clin. Invest. , vol.101 , pp. 1142-1147
    • Shinohara, M.1    Thornalley, P.J.2    Giardino, I.3    Beisswenger, P.4    Thorpe, S.R.5    Onorato, J.6    Brownlee, M.7
  • 41
    • 74849111826 scopus 로고    scopus 로고
    • Methylglyoxal causes dysfunction of thioredoxin and thioredoxin reductase in endothelial cells
    • Tatsunami, R., Oba, T., Takahashi, K., Tampo, Y., 2009. Methylglyoxal causes dysfunction of thioredoxin and thioredoxin reductase in endothelial cells. J. Pharmacol. Sci. 111, 426-432.
    • (2009) J. Pharmacol. Sci. , vol.111 , pp. 426-432
    • Tatsunami, R.1    Oba, T.2    Takahashi, K.3    Tampo, Y.4
  • 44
    • 0344875019 scopus 로고    scopus 로고
    • Thioredoxin: a key regulator of cardiovascular homeostasis
    • Yamawaki, H., Haendeler, J., Berk, B.C., 2003. Thioredoxin: a key regulator of cardiovascular homeostasis. Circ. Res. 93, 1029-1033.
    • (2003) Circ. Res. , vol.93 , pp. 1029-1033
    • Yamawaki, H.1    Haendeler, J.2    Berk, B.C.3
  • 45
    • 57349096428 scopus 로고    scopus 로고
    • Methylglyoxal mediates vascular inflammation via JNK and p38 in human endothelial cells
    • Yamawaki, H., Saito, K., Okada, M., Hara, Y., 2008. Methylglyoxal mediates vascular inflammation via JNK and p38 in human endothelial cells. Am. J. Physiol. Cell Physiol. 295, C1510-C1517.
    • (2008) Am. J. Physiol. Cell Physiol. , vol.295
    • Yamawaki, H.1    Saito, K.2    Okada, M.3    Hara, Y.4
  • 46
    • 0142182386 scopus 로고    scopus 로고
    • The role of thioredoxin in the aging process: involvement of oxidative stress
    • Yoshida, T., Oka, S., Masutani, H., Nakamura, H., Yodoi, J., 2003. The role of thioredoxin in the aging process: involvement of oxidative stress. Antioxid. Redox Signal. 5, 563-570.
    • (2003) Antioxid. Redox Signal. , vol.5 , pp. 563-570
    • Yoshida, T.1    Oka, S.2    Masutani, H.3    Nakamura, H.4    Yodoi, J.5
  • 48
    • 0030745646 scopus 로고    scopus 로고
    • Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3
    • Zou, H., Henzel, W.J., Liu, X., Lutschg, A., Wang, X., 1997. Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3. Cell 90, 405-413.
    • (1997) Cell , vol.90 , pp. 405-413
    • Zou, H.1    Henzel, W.J.2    Liu, X.3    Lutschg, A.4    Wang, X.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.