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Volumn 191, Issue 1-3, 2011, Pages 330-338

Aldose reductase inhibition suppresses oxidative stress-induced inflammatory disorders

Author keywords

Aldose reductase; Asthma; Colon cancer; Inflammation; Oxidative stress; Uveitis

Indexed keywords

ALDEHYDE REDUCTASE; ALDEHYDE REDUCTASE INHIBITOR; ENZYME INHIBITOR; FIDARESTAT; SORBINIL; UNCLASSIFIED DRUG;

EID: 79957549510     PISSN: 00092797     EISSN: 18727786     Source Type: Journal    
DOI: 10.1016/j.cbi.2011.02.023     Document Type: Conference Paper
Times cited : (158)

References (120)
  • 1
    • 0029562272 scopus 로고
    • Lipid peroxidation product, 4-hydroxynonenal and its conjugate with GSH are excellent substrates of bovine lens aldose reductase
    • S. Srivastava, A. Chandra, A. Bhatnagar, S.K. Srivastava, N.H. Ansari, Lipid peroxidation product, 4-hydroxynonenal and its conjugate with GSH are excellent substrates of bovine lens aldose reductase, Biochem. Biophys. Res. Commun. 217 (1995) 741-746.
    • (1995) Biochem. Biophys. Res. Commun. , vol.217 , pp. 741-746
    • Srivastava, S.1    Chandra, A.2    Bhatnagar, A.3    Srivastava, S.K.4    Ansari, N.H.5
  • 3
    • 34547935418 scopus 로고    scopus 로고
    • The polyol pathway as a mechanism for diabetic retinopathy: Attractive, elusive, and resilient
    • M. Lorenzi, The polyol pathway as a mechanism for diabetic retinopathy: attractive, elusive, and resilient, Exp. Diabetes Res. 2007 (2007) 61038.
    • (2007) Exp. Diabetes Res. , vol.2007 , pp. 61038
    • Lorenzi, M.1
  • 4
    • 38849177363 scopus 로고    scopus 로고
    • Aldose reductase, still a compelling target for diabetic neuropathy
    • DOI 10.2174/138945008783431781
    • P.J. Oates, Aldose reductase, still a compelling target for diabetic neuropathy, Curr. Drug Targets 9 (2008) 14-36. (Pubitemid 351201678)
    • (2008) Current Drug Targets , vol.9 , Issue.1 , pp. 14-36
    • Oates, P.J.1
  • 5
    • 0033857113 scopus 로고    scopus 로고
    • Aldose reductase and the role of the polyol pathway in diabetic nephropathy
    • M. Dunlop, Aldose reductase and the role of the polyol pathway in diabetic nephropathy, Kidney Int. Suppl. 77 (2000) S3-12.
    • (2000) Kidney Int. Suppl. , vol.77
    • Dunlop, M.1
  • 6
    • 21544463410 scopus 로고    scopus 로고
    • Aldose reductase in diabetic microvascular complications
    • DOI 10.2174/1389450054021891
    • S.S. Chung, S.K. Chung, Aldose reductase in diabetic microvascular complications, Curr. Drug Targets 6 (2005) 475-486. (Pubitemid 40921713)
    • (2005) Current Drug Targets , vol.6 , Issue.4 , pp. 475-486
    • Chung, S.S.M.1    Chung, S.K.2
  • 8
    • 18844369302 scopus 로고    scopus 로고
    • Role of aldose reductase and oxidative damage in diabetes and the consequent potential for therapeutic options
    • S.K. Srivastava, K.V. Ramana, A. Bhatnagar, Role of aldose reductase and oxidative damage in diabetes and the consequent potential for therapeutic options, Endocr. Rev. 26 (2005) 380-392.
    • (2005) Endocr. Rev. , vol.26 , pp. 380-392
    • Srivastava, S.K.1    Ramana, K.V.2    Bhatnagar, A.3
  • 9
    • 0028946316 scopus 로고
    • Demonstration that polyol accumulation is responsible for diabetic cataract by the use of transgenic mice expressing the aldose reductase gene in the lens
    • A.Y. Lee, S.K. Chung, S.S. Chung, Demonstration that polyol accumulation is responsible for diabetic cataract by the use of transgenic mice expressing the aldose reductase gene in the lens, Proc. Natl. Acad. Sci. U. S. A. 92 (1995) 2780-2784.
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 2780-2784
    • Lee, A.Y.1    Chung, S.K.2    Chung, S.S.3
  • 10
    • 0042309876 scopus 로고    scopus 로고
    • Recent studies of aldose reductase enzyme inhibition for diabetic complications
    • S. Suzen, E. Buyukbingol, Recent studies of aldose reductase enzyme inhibition for diabetic complications, Curr. Med. Chem. 10 (2003) 1329-1352. (Pubitemid 36896564)
    • (2003) Current Medicinal Chemistry , vol.10 , Issue.15 , pp. 1329-1352
    • Suzen, S.1    Buyukbingol, E.2
  • 11
    • 0027400468 scopus 로고
    • Aldose reductase and its inhibition in the control of diabetic complications
    • S. Narayanan, Aldose reductase and its inhibition in the control of diabetic complications, Ann. Clin. Lab. Sci. 23 (1993) 148-158. (Pubitemid 23093793)
    • (1993) Annals of Clinical and Laboratory Science , vol.23 , Issue.2 , pp. 148-158
    • Narayanan, S.1
  • 12
    • 0025373003 scopus 로고
    • Potential use of aldose reductase inhibitors to prevent diabetic complications
    • G.J. Zenon 3rd, C.V. Abobo, B.L. Carter, D.W. Ball, Potential use of aldose reductase inhibitors to prevent diabetic complications, Clin. Pharm. 9 (1990) 446-457.
    • (1990) Clin. Pharm. , vol.9 , pp. 446-457
    • Zenon III, G.J.1    Abobo, C.V.2    Carter, B.L.3    Ball, D.W.4
  • 13
    • 0032958288 scopus 로고    scopus 로고
    • Contributions of polyol pathway to oxidative stress in diabetic cataract
    • A.Y. Lee, S.S. Chung, Contributions of polyol pathway to oxidative stress in diabetic cataract, FASEB J. 13 (1999) 23-30. (Pubitemid 29038271)
    • (1999) FASEB Journal , vol.13 , Issue.1 , pp. 23-30
    • Lee, A.Y.W.1    Chung, S.S.M.2
  • 16
    • 0023806489 scopus 로고
    • Prevention of sugar-induced cataractogenesis in rats by butylated hydroxytoluene
    • S.K. Srivastava, N.H. Ansari, Prevention of sugar-induced cataractogenesis in rats by butylated hydroxytoluene, Diabetes 37 (1988) 1505-1508.
    • (1988) Diabetes , vol.37 , pp. 1505-1508
    • Srivastava, S.K.1    Ansari, N.H.2
  • 17
    • 3042596594 scopus 로고    scopus 로고
    • Mass spectrometry for detection of 4- hydroxy-trans-2-nonenal (HNE) adducts with peptides and proteins
    • M. Carini, G. Aldini, R.M. Facino, Mass spectrometry for detection of 4- hydroxy-trans-2-nonenal (HNE) adducts with peptides and proteins, Mass Spectrom. Rev. 23 (2004) 281-305.
    • (2004) Mass Spectrom. Rev. , vol.23 , pp. 281-305
    • Carini, M.1    Aldini, G.2    Facino, R.M.3
  • 18
    • 0033051392 scopus 로고    scopus 로고
    • Atherogenic lipoproteins, oxidative stress, and cell death
    • J. Galle, K. Heermeier, C. Wanner, Atherogenic lipoproteins, oxidative stress, and cell death, Kidney Int. Suppl. 71 (1999) S62-65.
    • (1999) Kidney Int. Suppl. , vol.71
    • Galle, J.1    Heermeier, K.2    Wanner, C.3
  • 19
    • 0032426602 scopus 로고    scopus 로고
    • Inflammation, lipids, and free radicals: Lessons learned from the atherogenic process
    • M.E. Rosenfeld, Inflammation, lipids, and free radicals: lessons learned from the atherogenic process, Semin. Reprod. Endocrinol. 16 (1998) 249-261.
    • (1998) Semin. Reprod. Endocrinol. , vol.16 , pp. 249-261
    • Rosenfeld, M.E.1
  • 20
    • 0034775456 scopus 로고    scopus 로고
    • Apoptosis in atherosclerosis: Focus on oxidized lipids and inflammation
    • DOI 10.1097/00041433-200110000-00009
    • W. Martinet, M.M. Kockx, Apoptosis in atherosclerosis: focus on oxidized lipids and inflammation, Curr. Opin. Lipidol. 12 (2001) 535-541. (Pubitemid 32980302)
    • (2001) Current Opinion in Lipidology , vol.12 , Issue.5 , pp. 535-541
    • Martinet, W.1    Kockx, M.M.2
  • 22
    • 0021019603 scopus 로고
    • LDL-induced cytotoxicity and its inhibition by anti-oxidant treatment in cultured human endothelial cells and fibroblasts
    • S.A. Evensen, K.S. Galdal, E. Nilsen, LDL-induced cytotoxicity and its inhibition by anti-oxidant treatment in culturedhumanendothelial cells and fibroblasts, Atherosclerosis 49 (1983) 23-30. (Pubitemid 14227972)
    • (1983) Atherosclerosis , vol.49 , Issue.1 , pp. 23-30
    • Evensen, S.A.1    Galdal, K.S.2    Nilsen, E.3
  • 23
    • 0031857786 scopus 로고    scopus 로고
    • Regulation of tumour cell sensitivity to TNF-induced oxidative stress and cytotoxicity: Role of glutathione
    • E. Obrador, J. Navarro, J. Mompo, M. Asensi, J.A. Pellicer, J.M. Estrela, Regulation of tumour cell sensitivity to TNF-α-induced oxidative stress and cytotoxicity: role of glutathione, Biofactors 8 (1998) 23-26. (Pubitemid 28332780)
    • (1998) BioFactors , vol.8 , Issue.1-2 , pp. 23-26
    • Obrador, E.1    Navarro, J.2    Mompo, J.3    Asensi, M.4    Pellicer, J.A.5    Estrela, J.M.6
  • 24
    • 54949151846 scopus 로고    scopus 로고
    • Novel role of curcumin in the prevention of cytokine-induced islet death in vitro and diabetogenesis in vivo
    • M. Kanitkar, K. Gokhale, S. Galande, R.R. Bhonde, Novel role of curcumin in the prevention of cytokine-induced islet death in vitro and diabetogenesis in vivo, Br. J. Pharmacol. 155 (2008) 702-713.
    • (2008) Br. J. Pharmacol. , vol.155 , pp. 702-713
    • Kanitkar, M.1    Gokhale, K.2    Galande, S.3    Bhonde, R.R.4
  • 28
    • 33745892100 scopus 로고    scopus 로고
    • Mitogenic responses of vascular smooth muscle cells to lipid peroxidation-derived aldehyde 4-hydroxy-trans-2-nonenal (HNE): Role of aldose reductase-catalyzed reduction of the HNE-glutathione conjugates in regulating cell growth
    • K.V. Ramana, A. Bhatnagar, S. Srivastava, U.C. Yadav, S. Awasthi, Y.C. Awasthi, S.K. Srivastava, Mitogenic responses of vascular smooth muscle cells to lipid peroxidation-derived aldehyde 4-hydroxy-trans-2-nonenal (HNE): role of aldose reductase-catalyzed reduction of the HNE-glutathione conjugates in regulating cell growth, J. Biol. Chem. 281 (2006) 17652-17660.
    • (2006) J. Biol. Chem. , vol.281 , pp. 17652-17660
    • Ramana, K.V.1    Bhatnagar, A.2    Srivastava, S.3    Yadav, U.C.4    Awasthi, S.5    Awasthi, Y.C.6    Srivastava, S.K.7
  • 31
    • 57249095767 scopus 로고    scopus 로고
    • Lipid peroxidation of membrane phospholipids generates hydroxy-alkenals and oxidized phospholipids active in physiological and/or pathological conditions
    • A. Catalá, Lipid peroxidation of membrane phospholipids generates hydroxy-alkenals and oxidized phospholipids active in physiological and/or pathological conditions, Chem. Phys. Lipids 157 (2009) 1-11.
    • (2009) Chem. Phys. Lipids , vol.157 , pp. 1-11
    • Catalá, A.1
  • 38
    • 0032008127 scopus 로고    scopus 로고
    • Identification of cardiac oxidoreductase(s) involved in the metabolism of the lipid peroxidation-derived aldehyde-4-hydroxynonenal
    • S. Srivastava, A. Chandra, N.H. Ansari, S.K. Srivastava, A. Bhatnagar, Identification of cardiac oxidoreductase(s) involved in the metabolism of the lipid peroxidation-derived aldehyde-4-hydroxynonenal, Biochem. J. 329 (1998) 469-475. (Pubitemid 28055167)
    • (1998) Biochemical Journal , vol.329 , Issue.3 , pp. 469-475
    • Srivastava, S.1    Chandra, A.2    Ansari, N.H.3    Srivastava, S.K.4    Bhatnagar, A.5
  • 39
    • 0031020377 scopus 로고    scopus 로고
    • Aldose reductase induction: A novel response to oxidative stress of smooth muscle cells
    • S.E. Spycher, S. Tabataba-Vakili, V.B. O'Donnell, L. Palomba, A. Azzi, Aldose reductase induction: a novel response to oxidative stress of smooth muscle cells, FASEB J. 11 (1997) 181-188. (Pubitemid 27097592)
    • (1997) FASEB Journal , vol.11 , Issue.2 , pp. 181-188
    • Spycher, S.E.1    Tabataba-Vakili, S.2    O'Donnell, V.B.3    Palomba, L.4    Azzi, A.5
  • 40
    • 0030722406 scopus 로고    scopus 로고
    • Differential control of murine aldose reductase and fibroblast growth factor (FGF)-regulated-1 gene expression in NIH 3T3 cells by FGF-1 treatment and hyperosmotic stress
    • D.K. Hsu, Y. Guo, K.A. Peifley, J.A. Winkles, Differential control of murine aldose reductase and fibroblast growth factor (FGF)-regulated-1 gene expression in NIH 3T3 cells by FGF-1 treatment and hyperosmotic stress, Biochem. J. 328 (1997) 593-598. (Pubitemid 27515605)
    • (1997) Biochemical Journal , vol.328 , Issue.2 , pp. 593-598
    • Hsu, D.K.W.1    Guo, Y.2    Peifley, K.A.3    Winkles, J.A.4
  • 41
    • 0031172530 scopus 로고    scopus 로고
    • Regulation of aldose reductase expression in rat astrocytes in culture
    • DOI 10.1002/(SICI)1098-1136(199706)20:2<135::AID-GLIA5>3.0.CO;2-8
    • C. Jacquin-Becker, G. Labourdette, Regulation of aldose reductase expression in rat astrocytes in culture, Glia 20 (1997) 135-144. (Pubitemid 27253206)
    • (1997) GLIA , vol.20 , Issue.2 , pp. 135-144
    • Jacquin-Becker, C.1    Labourdette, G.2
  • 43
    • 0029127117 scopus 로고
    • Elevation of aldose reductase gene expression in rat primary hepatoma and hepatoma cell lines: Implication in detoxification of cytotoxic aldehydes
    • M. Takahashi, J. Fujii, E. Miyoshi, A. Hoshi, N. Taniguchi, Elevation of aldose reductase gene expression in rat primary hepatoma and hepatoma cell lines: implication in detoxification of cytotoxic aldehydes, Int. J. Cancer 62 (1995) 749-754.
    • (1995) Int. J. Cancer , vol.62 , pp. 749-754
    • Takahashi, M.1    Fujii, J.2    Miyoshi, E.3    Hoshi, A.4    Taniguchi, N.5
  • 44
    • 0030750775 scopus 로고    scopus 로고
    • Further characterization of a rat hepatoma-derived aldose-reductase-like protein - Organ distribution and modulation in vitro
    • E. Zeindl-Eberhart, P.R. Jungblut, A. Otto, R. Kerler, H.M. Rabes, Further characterization of a rat hepatoma-derived aldose-reductase-like protein - organ distribution and modulation in vitro, Eur. J. Biochem. 247 (1997) 792-800.
    • (1997) Eur. J. Biochem. , vol.247 , pp. 792-800
    • Zeindl-Eberhart, E.1    Jungblut, P.R.2    Otto, A.3    Kerler, R.4    Rabes, H.M.5
  • 46
    • 0028274814 scopus 로고
    • Abnormal expression of aldose reductase mRNA in fiber cells of cataractous rat lens. Analysis by in situ hybridization
    • S. Shi, I. Bekhor, Abnormal expression of aldose reductase mRNA in fiber cells of cataractous rat lens. Analysis by in situ hybridization, Mol. Cell. Biochem. 131 (1994) 35-41. (Pubitemid 24139173)
    • (1994) Molecular and Cellular Biochemistry , vol.131 , Issue.1 , pp. 35-41
    • Shi, S.1    Bekhor, I.2
  • 47
    • 0034816167 scopus 로고    scopus 로고
    • Identification of biochemical pathways for the metabolism of oxidized low-density lipoprotein derived aldehyde-4-hydroxy trans-2-nonenal in vascular smooth muscle cells
    • DOI 10.1016/S0021-9150(01)00454-3, PII S0021915001004543
    • S. Srivastava, D.J. Conklin, S.Q. Liu, N. Prakash, P.J. Boor, S.K. Srivastava, A. Bhatnagar, Identification of biochemical pathways for the metabolism of oxidized low-density lipoprotein derived aldehyde-4-hydroxy trans-2-nonenal in vascular smooth muscle cells, Atherosclerosis 158 (2001) 339-350. (Pubitemid 32913643)
    • (2001) Atherosclerosis , vol.158 , Issue.2 , pp. 339-350
    • Srivastava, S.1    Conklin, D.J.2    Liu, S.-Q.3    Prakash, N.4    Boor, P.J.5    Srivastava, S.K.6    Bhatnagar, A.7
  • 48
    • 0032947546 scopus 로고    scopus 로고
    • Aldose reductase functions as a detoxification system for lipid peroxidation products in vasculitis
    • H.L. Rittner, V. Hafner, P.A. Klimiuk, L.I. Szweda, J.J. Goronzy, C.M. Weyand, Aldose reductase functions as a detoxification system for lipid peroxidation products in vasculitis, J. Clin. Invest. 103 (1999) 1007-1013.
    • (1999) J. Clin. Invest. , vol.103 , pp. 1007-1013
    • Rittner, H.L.1    Hafner, V.2    Klimiuk, P.A.3    Szweda, L.I.4    Goronzy, J.J.5    Weyand, C.M.6
  • 51
    • 0029869189 scopus 로고    scopus 로고
    • Mechanisms involved in the generation of free radicals
    • B. Halliwell, Mechanisms involved in the generation of free radicals, Pathol. Biol. (Paris) 44 (1996) 6-13. (Pubitemid 26088472)
    • (1996) Pathologie Biologie , vol.44 , Issue.1 , pp. 6-13
    • Halliwell, B.1
  • 52
    • 0034782946 scopus 로고    scopus 로고
    • Redox signaling in macrophages
    • H.J. Forman, M. Torres, Redox signaling in macrophages, Mol. Aspects Med. 22 (2001) 189-216.
    • (2001) Mol. Aspects Med. , vol.22 , pp. 189-216
    • Forman, H.J.1    Torres, M.2
  • 53
    • 67650720510 scopus 로고    scopus 로고
    • Immune and inflammatory mechanisms of atherosclerosis
    • E. Galkina, K. Ley, Immune and inflammatory mechanisms of atherosclerosis, Annu. Rev. Immunol. 27 (2009) 165-197.
    • (2009) Annu. Rev. Immunol. , vol.27 , pp. 165-197
    • Galkina, E.1    Ley, K.2
  • 54
    • 33645285957 scopus 로고    scopus 로고
    • Regulation of NADPH oxidases: The role of Rac proteins
    • P.L. Hordijk, Regulation of NADPH oxidases: the role of Rac proteins, Circ. Res. 98 (2006) 453-462.
    • (2006) Circ. Res. , vol.98 , pp. 453-462
    • Hordijk, P.L.1
  • 55
    • 69149091574 scopus 로고    scopus 로고
    • Naturally occurring flavonoids attenuate high glucose-induced expression of proinflammatory cytokines in human monocytic THP-1 cells
    • C.H. Wu, C.F. Wu, H.W. Huang, Y.C. Jao, G.C. Yen, Naturally occurring flavonoids attenuate high glucose-induced expression of proinflammatory cytokines in human monocytic THP-1 cells, Mol. Nutr. Food Res. 53 (2009) 984-995.
    • (2009) Mol. Nutr. Food Res. , vol.53 , pp. 984-995
    • Wu, C.H.1    Wu, C.F.2    Huang, H.W.3    Jao, Y.C.4    Yen, G.C.5
  • 56
    • 65949102522 scopus 로고    scopus 로고
    • p47phox, the phagocyte NADPH oxidase/NOX2 organizer: Structure, phosphorylation and implication in diseases
    • J. El-Benna, P.M. Dang, M.A. Gougerot-Pocidalo, J.C. Marie, F. Braut-Boucher, p47phox, the phagocyte NADPH oxidase/NOX2 organizer: structure, phosphorylation and implication in diseases, Exp. Mol. Med. 41 (2009) 217-225.
    • (2009) Exp. Mol. Med. , vol.41 , pp. 217-225
    • El-Benna, J.1    Dang, P.M.2    Gougerot-Pocidalo, M.A.3    Marie, J.C.4    Braut-Boucher, F.5
  • 57
    • 79955635908 scopus 로고    scopus 로고
    • NADPH oxidase versus mitochondria-derived ROS in glucose-induced apoptosis of pericytes in early diabetic retinopathy
    • doi:10.1155/2010/746978 (Article ID: 746978)
    • N.M. Mustapha, M.T. Joanna, E.M. Kohner, R. Chibber, NADPH oxidase versus mitochondria-derived ROS in glucose-induced apoptosis of pericytes in early diabetic retinopathy, J. Ophthalmol. (2010), doi:10.1155/2010/746978 (Article ID: 746978).
    • (2010) J. Ophthalmol.
    • Mustapha, N.M.1    Joanna, M.T.2    Kohner, E.M.3    Chibber, R.4
  • 58
    • 33745202365 scopus 로고    scopus 로고
    • NADPH oxidase-dependent redox signalling in cardiac hypertrophy, remodelling and failure
    • C.E. Murdoch, M. Zhang, A.C. Cave, A.M. Shah, NADPH oxidase-dependent redox signalling in cardiac hypertrophy, remodelling and failure, Cardiovasc. Res. 71 (2006) 208-215.
    • (2006) Cardiovasc. Res. , vol.71 , pp. 208-215
    • Murdoch, C.E.1    Zhang, M.2    Cave, A.C.3    Shah, A.M.4
  • 60
    • 0032844258 scopus 로고    scopus 로고
    • Supplementation of N-acetylcysteine inhibits NFkappaB activation and protects against alloxan-induced diabetes in CD-1 mice
    • E. Ho, G. Chen, T.M. Bray, Supplementation of N-acetylcysteine inhibits NFkappaB activation and protects against alloxan-induced diabetes in CD-1 mice, FASEB J. 13 (1999) 1845-1854. (Pubitemid 29473348)
    • (1999) FASEB Journal , vol.13 , Issue.13 , pp. 1845-1854
    • Ho, E.1    Chen, G.2    Bray, T.M.3
  • 61
    • 0032998598 scopus 로고    scopus 로고
    • Intracellular oxidation/reduction status in the regulation of transcription factors NF-kappaB and AP-1
    • D. Gius, A. Botero, S. Shah, H.A. Curry, Intracellular oxidation/reduction status in the regulation of transcription factors NF-kappaB and AP-1, Toxicol. Lett. 106 (1999) 93-106.
    • (1999) Toxicol. Lett. , vol.106 , pp. 93-106
    • Gius, D.1    Botero, A.2    Shah, S.3    Curry, H.A.4
  • 62
    • 0036139794 scopus 로고    scopus 로고
    • AP-1: Linking hydrogen peroxide and oxidative stress to the control of cell proliferation and death
    • M. Karin, E. Shaulian, AP-1: linking hydrogen peroxide and oxidative stress to the control of cell proliferation and death, IUBMB Life 52 (2001) 17-24. (Pubitemid 33769664)
    • (2001) IUBMB Life , vol.52 , Issue.1-2 , pp. 17-24
    • Karin, M.1    Shaulian, E.2
  • 63
    • 0029032249 scopus 로고
    • The regulation of AP-1 activity by mitogen-activated protein kinases
    • M. Karin, The regulation of AP-1 activity by mitogen-activated protein kinases, J. Biol. Chem. 270 (1995) 16483-16486.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16483-16486
    • Karin, M.1
  • 64
    • 0034456018 scopus 로고    scopus 로고
    • 4-Hydroxynonenal in the pathomechanisms of oxidative stress
    • DOI 10.1080/15216540051081092
    • G. Poli, R.J. Schaur, 4-Hydroxynonenal in the pathomechanisms of oxidative stress, IUBMB Life 50 (2000) 315-321. (Pubitemid 32289090)
    • (2000) IUBMB Life , vol.50 , Issue.4-5 , pp. 315-321
    • Poli, G.1    Schaur, R.J.2
  • 65
    • 0033188494 scopus 로고    scopus 로고
    • 4-Hydroxynonenal as a biological signal: Molecular basis and pathophysiological implications
    • M. Parola, G. Bellomo, G. Robino, G. Barrera, M.U. Dianzani, 4-Hydroxynonenal as a biological signal: molecular basis and pathophysiological implications, Antioxid. Redox Signal. 1 (1999) 255-284.
    • (1999) Antioxid. Redox Signal. , vol.1 , pp. 255-284
    • Parola, M.1    Bellomo, G.2    Robino, G.3    Barrera, G.4    Dianzani, M.U.5
  • 66
    • 33744993153 scopus 로고    scopus 로고
    • Circulating 4-hydroxynonenal-protein thioether adducts assessed by gas chromatography-mass spectrometry are increased with disease progression and aging in spontaneously hypertensive rats
    • DOI 10.1016/j.freeradbiomed.2006.03.011, PII S0891584906001869
    • C. Asselin, B. Bouchard, J.C. Tardif, C. Des Rosiers, Circulating 4- hydroxynonenal-protein thioether adducts assessed by gas chromatography-mass spectrometry are increased with disease progression and aging in spontaneously hypertensive rats, Free Radic. Biol. Med. 41 (2006) 97-105. (Pubitemid 43866456)
    • (2006) Free Radical Biology and Medicine , vol.41 , Issue.1 , pp. 97-105
    • Asselin, C.1    Bouchard, B.2    Tardif, J.-C.3    Des, R.C.4
  • 67
    • 0028897831 scopus 로고
    • Structural definition of early lysine and histidine adduction chemistry of 4-hydroxynonenal
    • D.V. Nadkarni, L.M. Sayre, Structural definition of early lysine and histidine adduction chemistry of 4-hydroxynonenal, Chem. Res. Toxicol. 8 (1995) 284-291.
    • (1995) Chem. Res. Toxicol. , vol.8 , pp. 284-291
    • Nadkarni, D.V.1    Sayre, L.M.2
  • 68
    • 0026739577 scopus 로고
    • In vitro activation of heat shock transcription factor by 4-hydroxynonenal
    • F. Cajone, M. Crescente, In vitro activation of heat shock transcription factor by 4-hydroxynonenal, Chem. Biol. Interact. 84 (1992) 97-112.
    • (1992) Chem. Biol. Interact. , vol.84 , pp. 97-112
    • Cajone, F.1    Crescente, M.2
  • 69
    • 0027319341 scopus 로고
    • Cytotoxicity and genotoxicity of lipid-oxidation products
    • H. Esterbauer, Cytotoxicity and genotoxicity of lipid-oxidation products, Am. J. Clin. Nutr. 57 (Suppl. 5) (1993) 779S-785S.
    • (1993) Am. J. Clin. Nutr. , vol.57 , Issue.SUPPL. 5
    • Esterbauer, H.1
  • 73
    • 0042671405 scopus 로고    scopus 로고
    • Genotoxicity of HNE
    • P.M. Eckl, Genotoxicity of HNE, Mol. Aspects Med. 24 (2003) 161-165.
    • (2003) Mol. Aspects Med. , vol.24 , pp. 161-165
    • Eckl, P.M.1
  • 75
    • 59049086019 scopus 로고    scopus 로고
    • Role of human aldo-keto-reductase AKR1B10 in the protection against toxic aldehydes
    • H.J. Martin, E. Maser, Role of human aldo-keto-reductase AKR1B10 in the protection against toxic aldehydes, Chem. Biol. Interact. 178 (2009) 145-150.
    • (2009) Chem. Biol. Interact. , vol.178 , pp. 145-150
    • Martin, H.J.1    Maser, E.2
  • 76
    • 33845962827 scopus 로고    scopus 로고
    • Aldose reductase mediates the lipopolysaccharide-induced release of inflammatory mediators in RAW264.7 murine macrophages
    • K.V. Ramana, A.A. Fadl, R. Tammali, A.B. Reddy, A.K. Chopra, S.K. Srivastava, Aldose reductase mediates the lipopolysaccharide-induced release of inflammatory mediators in RAW264.7 murine macrophages, J. Biol. Chem. 281 (2006) 33019-33029.
    • (2006) J. Biol. Chem. , vol.281 , pp. 33019-33029
    • Ramana, K.V.1    Fadl, A.A.2    Tammali, R.3    Reddy, A.B.4    Chopra, A.K.5    Srivastava, S.K.6
  • 77
    • 34250902930 scopus 로고    scopus 로고
    • Targeting the protein kinase C family: Are we there yet?
    • DOI 10.1038/nrc2168, PII NRC2168
    • H.J. Mackay, C.J. Twelves, Targeting the protein kinase C family: are we there yet? Nat. Rev. Cancer 7 (2007) 554-562. (Pubitemid 46985395)
    • (2007) Nature Reviews Cancer , vol.7 , Issue.7 , pp. 554-562
    • Mackay, H.J.1    Twelves, C.J.2
  • 78
    • 0034221202 scopus 로고    scopus 로고
    • The role of protein kinase C isoforms in cell proliferation and apoptosis
    • M. Musashi, S. Ota, N. Shiroshita, The role of protein kinase C isoforms in cell proliferation and apoptosis, Int. J. Hematol. 72 (2000) 12-19.
    • (2000) Int. J. Hematol. , vol.72 , pp. 12-19
    • Musashi, M.1    Ota, S.2    Shiroshita, N.3
  • 79
    • 0043172499 scopus 로고    scopus 로고
    • Role of PKC-dependent pathways in HNE-induced cell protein transport and secretion
    • U.M.Marinari, M. Nitti, M.A. Pronzato, C. Domenicotti, Role of PKC-dependent pathways in HNE-induced cell protein transport and secretion, Mol. Aspects Med. 24 (2003) 205-211.
    • (2003) Mol. Aspects Med. , vol.24 , pp. 205-211
    • Marinari, U.M.1    Nitti, M.2    Pronzato, M.A.3    Domenicotti, C.4
  • 80
    • 14644387496 scopus 로고    scopus 로고
    • Requirement of aldose reductase for the hyperglycemic activation of protein kinase C and formation of diacylglycerol in vascular smooth muscle cells
    • DOI 10.2337/diabetes.54.3.818
    • K.V. Ramana, B. Friedrich, R. Tammali, M.B. West, A. Bhatnagar, S.K. Srivastava, Requirement of aldose reductase for the hyperglycemic activation of protein kinase C and formation of diacylglycerol in vascular smooth muscle cells, Diabetes 54 (2005) 818-829. (Pubitemid 40322087)
    • (2005) Diabetes , vol.54 , Issue.3 , pp. 818-829
    • Ramana, K.V.1    Friedrich, B.2    Tammali, R.3    West, M.B.4    Bhatnagar, A.5    Srivastava, S.K.6
  • 82
    • 34249732513 scopus 로고    scopus 로고
    • Aldose reductase regulates TNF-alpha-induced PGE2 production in human colon cancer cells
    • DOI 10.1016/j.canlet.2007.01.001, PII S0304383507000134
    • R. Tammali, K.V. Ramana, S.K. Srivastava, Aldose reductase regulates TNF-alpha-induced PGE2 production in human colon cancer cells, Cancer Lett. 252 (2007) 299-306. (Pubitemid 46823949)
    • (2007) Cancer Letters , vol.252 , Issue.2 , pp. 299-306
    • Tammali, R.1    Ramana, K.V.2    Srivastava, S.K.3
  • 83
    • 3142646780 scopus 로고    scopus 로고
    • Aldose reductase regulates TNF-alpha-induced cell signaling and apoptosis in vascular endothelial cells
    • DOI 10.1016/j.febslet.2004.06.046, PII S0014579304007975
    • K.V. Ramana, A. Bhatnagar, S.K. Srivastava, Aldose reductase regulates TNF-alpha- induced cell signaling and apoptosis in vascular endothelial cells, FEBS Lett. 570 (2004) 189-194. (Pubitemid 38900980)
    • (2004) FEBS Letters , vol.570 , Issue.1-3 , pp. 189-194
    • Ramana, K.V.1    Bhatnagar, A.2    Srivastava, S.K.3
  • 84
    • 0037313234 scopus 로고    scopus 로고
    • Aldose reductase mediates cytotoxic signals of hyperglycemia and TNF-alpha in human lens epithelial cells
    • K.V. Ramana, B. Friedrich, A. Bhatnagar, S.K. Srivastava, Aldose reductase mediates cytotoxic signals of hyperglycemia and TNF-alpha in human lens epithelial cells, FASEB J. 17 (2003) 315-317.
    • (2003) FASEB J. , vol.17 , pp. 315-317
    • Ramana, K.V.1    Friedrich, B.2    Bhatnagar, A.3    Srivastava, S.K.4
  • 85
    • 0028321899 scopus 로고
    • Cellular and molecular abnormalities in the vascular endothelium of diabetes mellitus
    • DOI 10.1146/annurev.med.45.1.179
    • G.L. King, T. Shiba, J. Oliver, T. Inoguchi, S.E. Bursell, Cellular and molecular abnormalities in the vascular endothelium of diabetes mellitus, Annu. Rev. Med. 45 (1994) 179-188. (Pubitemid 24158154)
    • (1994) Annual Review of Medicine , vol.45 , pp. 179-188
    • King, G.L.1    Shiba, T.2    Oliver, J.3    Inoguchi, T.4    Bursell, S.-E.5
  • 86
    • 0035856980 scopus 로고    scopus 로고
    • Biochemistry and molecular cell biology of diabetic complications
    • DOI 10.1038/414813a
    • M. Brownlee, Biochemistry and molecular cell biology of diabetic complications, Nature 414 (2001) 813-820. (Pubitemid 34000785)
    • (2001) Nature , vol.414 , Issue.6865 , pp. 813-820
    • Brownlee, M.1
  • 87
    • 0026615871 scopus 로고
    • 3H]inositol uptake by glucose and sorbitol in cultured bovine lens epithelial cells: II. Characterization of high- And low-affinity myo-inositol transport sites
    • P.R. Cammarata, H.Q. Chen, J. Yang, T. Yorio, Modulation of myo-[3H]inositol uptake by glucose and sorbitol in cultured bovine lens epithelial cells. II. Characterization of high- and low-affinity myo-inositol transport sites, Invest. Ophthalmol. Vis. Sci. 33 (1992) 3572-3580. (Pubitemid 23001373)
    • (1992) Investigative Ophthalmology and Visual Science , vol.33 , Issue.13 , pp. 3572-3580
    • Cammarata, P.R.1    Chen, H.-Q.2    Yang, J.3    Yorio, T.4
  • 90
    • 7644241006 scopus 로고    scopus 로고
    • Interaction between the polyol pathway and non-enzymatic glycation on aortic smooth muscle cell migration and monocyte adhesion
    • DOI 10.1016/j.lfs.2004.09.010, PII S0024320504008392
    • Q. Dan, R. Wong, S.K. Chung, S.S. Chung, K.S. Lam, Interaction between the polyol pathway and non-enzymatic glycation on aortic smooth muscle cell migration and monocyte adhesion, Life Sci. 76 (2004) 445-459. (Pubitemid 39458312)
    • (2004) Life Sciences , vol.76 , Issue.4 , pp. 445-459
    • Dan, Q.1    Wong, R.2    Chung, S.K.3    Chung, S.S.M.4    Lam, K.S.L.5
  • 91
    • 0030581630 scopus 로고    scopus 로고
    • Rapid formation of advanced glycation end products by intermediate metabolites of glycolytic pathway and polyol pathway
    • DOI 10.1006/bbrc.1996.1695
    • Y. Hamada, N. Araki, N. Koh, J. Nakamura, S. Horiuchi, N. Hotta, Rapid formation of advanced glycation end products by intermediate metabolites of glycolytic pathway and polyol pathway, Biochem. Biophys. Res. Commun. 228 (1996) 539-543. (Pubitemid 26396108)
    • (1996) Biochemical and Biophysical Research Communications , vol.228 , Issue.2 , pp. 539-543
    • Hamada, Y.1    Araki, N.2    Koh, N.3    Nakamura, J.4    Horiuchi, S.5    Hotta, N.6
  • 92
    • 0028267237 scopus 로고
    • Suppression of pentosidine formation in galactosemic rat lens by an inhibitor of aldose reductase
    • R.H. Nagaraj, M. Prabhakaram, B.J. Ortwerth, V.M. Monnier, Suppression of pentosidine formation in galactosemic rat lens by an inhibitor of aldose reductase, Diabetes 43 (1994) 580-586. (Pubitemid 24096300)
    • (1994) Diabetes , vol.43 , Issue.4 , pp. 580-586
    • Nagaraj, R.H.1    Prabhakaram, M.2    Ortwerth, B.J.3    Monnier, V.M.4
  • 95
    • 0037451929 scopus 로고    scopus 로고
    • The epidemiology of sepsis in the United States from 1979 through 2000
    • G.S. Martin, D.M. Mannino, S. Eaton, M. Moss, The epidemiology of sepsis in the United States from 1979 through 2000, N. Engl. J. Med. 348 (2003) 1546-1554.
    • (2003) N. Engl. J. Med. , vol.348 , pp. 1546-1554
    • Martin, G.S.1    Mannino, D.M.2    Eaton, S.3    Moss, M.4
  • 97
    • 70350023106 scopus 로고    scopus 로고
    • Anti-inflammatory effect of aldose reductase inhibition in murine polymicrobial sepsis
    • A.B. Reddy, S.K. Srivastava, K.V. Ramana, Anti-inflammatory effect of aldose reductase inhibition in murine polymicrobial sepsis, Cytokine 48 (2009) 170-176.
    • (2009) Cytokine , vol.48 , pp. 170-176
    • Reddy, A.B.1    Srivastava, S.K.2    Ramana, K.V.3
  • 98
    • 33750561283 scopus 로고    scopus 로고
    • Endotoxin-induced cardiomyopathy and systemic inflammation in mice is prevented by aldose reductase inhibition
    • DOI 10.1161/CIRCULATIONAHA.106.630830, PII 0000301720061024000010
    • K.V. Ramana, M.S. Willis, M.D. White, J.W. Horton, J.M. DiMaio, D. Srivastava, A. Bhatnagar, S.K. Srivastava, Endotoxin-induced cardiomyopathy and systemic inflammation in mice is prevented by aldose reductase inhibition, Circulation 114 (2006) 1838-1846. (Pubitemid 44673359)
    • (2006) Circulation , vol.114 , Issue.17 , pp. 1838-1846
    • Ramana, K.V.1    Willis, M.S.2    White, M.D.3    Horton, J.W.4    Dimaio, J.M.5    Srivastava, D.6    Bhatnagar, A.7    Srivastava, S.K.8
  • 99
    • 33746294223 scopus 로고    scopus 로고
    • The global burden of asthma
    • S.S. Braman, The global burden of asthma, Chest 130 (Suppl. 1) (2006) 4S-12S.
    • (2006) Chest , vol.130 , Issue.SUPPL. 1
    • Braman, S.S.1
  • 101
  • 102
    • 0042921284 scopus 로고    scopus 로고
    • Understanding asthma pathophysiology
    • P. Fireman, Understanding asthma pathophysiology, Allergy Asthma Proc. 24 (2003) 79-83. (Pubitemid 37034191)
    • (2003) Allergy and Asthma Proceedings , vol.24 , Issue.2 , pp. 79-83
    • Fireman, P.1
  • 105
    • 70449719352 scopus 로고    scopus 로고
    • Aldose reductase inhibition suppresses the expression of Th2 cytokines and airway inflammation in ovalbumin-induced asthma in mice
    • U.C. Yadav, A.S. Naura, L. Aguilera-Aguirre, K.V. Ramana, I. Boldogh, S. Sur, H.A. Boulares, S.K. Srivastava, Aldose reductase inhibition suppresses the expression of Th2 cytokines and airway inflammation in ovalbumin-induced asthma in mice, J. Immunol. 183 (2009) 4723-4732.
    • (2009) J. Immunol. , vol.183 , pp. 4723-4732
    • Yadav, U.C.1    Naura, A.S.2    Aguilera-Aguirre, L.3    Ramana, K.V.4    Boldogh, I.5    Sur, S.6    Boulares, H.A.7    Srivastava, S.K.8
  • 109
    • 0036484856 scopus 로고    scopus 로고
    • Chronic inflammation and cancer
    • E. Shacter, S.A. Weitzman, Chronic inflammation and cancer, Oncology 16 (2002) 217-226.
    • (2002) Oncology , vol.16 , pp. 217-226
    • Shacter, E.1    Weitzman, S.A.2
  • 110
    • 68849127181 scopus 로고    scopus 로고
    • Inflammation and colorectal cancer
    • S. Kraus, N. Arber, Inflammation and colorectal cancer, Curr. Opin. Pharmacol. 9 (2009) 405-410.
    • (2009) Curr. Opin. Pharmacol. , vol.9 , pp. 405-410
    • Kraus, S.1    Arber, N.2
  • 111
    • 33750286521 scopus 로고    scopus 로고
    • Aldose reductase regulates growth factor-induced cyclooxygenase-2 expression and prostaglandin E2 production in human colon cancer cells
    • DOI 10.1158/0008-5472.CAN-06-2105
    • R. Tammali, K.V. Ramana, S.S. Singhal, S. Awasthi, S.K. Srivastava, Aldose reductase regulates growth factor-induced cyclooxygenase-2 expression and prostaglandin E2 production in human colon cancer cells, Cancer Res. 66 (2006) 9705-9713. (Pubitemid 44623671)
    • (2006) Cancer Research , vol.66 , Issue.19 , pp. 9705-9713
    • Tammali, R.1    Ramana, K.V.2    Singhal, S.S.3    Awasthi, S.4    Srivastava, S.K.5
  • 112
    • 0035084463 scopus 로고    scopus 로고
    • Regulatory role of phosphatidylinositol 3-kinase on TNF-α-induced cyclooxygenase 2 expression in colonic epithelial cells
    • S.A. Weaver, M.P. Russo, K.L. Wright, G. Kolios, C. Jobin, D.A. Robertson, S.G. Ward, Regulatory role of phosphatidylinositol 3-kinase on TNF-α-induced cyclooxygenase 2 expression in colonic epithelial cells, Gastroenterology 120 (2001) 1117-1127. (Pubitemid 32246666)
    • (2001) Gastroenterology , vol.120 , Issue.5 , pp. 1117-1127
    • Weaver, S.A.1    Russo, M.P.2    Wright, K.L.3    Kolios, G.4    Jobin, C.5    Robertson, D.A.F.6    Ward, S.G.7
  • 113
    • 23944476094 scopus 로고    scopus 로고
    • Involvement of IL-6 in the pathogenesis of inflammatory bowel disease and colon cancer
    • R. Atreya, M.F. Neurath, Involvement of IL-6 in the pathogenesis of inflammatory bowel disease and colon cancer, Clin. Rev. Allergy Immunol. 28 (2005) 187-196.
    • (2005) Clin. Rev. Allergy Immunol. , vol.28 , pp. 187-196
    • Atreya, R.1    Neurath, M.F.2
  • 115
    • 31544441350 scopus 로고    scopus 로고
    • Redox-sensitive transcription factors as prime targets for chemoprevention with anti-inflammatory and antioxidative phytochemicals
    • Y.J. Surh, J.K. Kundu, H.K. Na, J.S. Lee, Redox-sensitive transcription factors as prime targets for chemoprevention with anti-inflammatory and antioxidative phytochemicals, J. Nutr. 135 (2005) 2993S-3001S.
    • (2005) J. Nutr. , vol.135
    • Surh, Y.J.1    Kundu, J.K.2    Na, H.K.3    Lee, J.S.4
  • 116
    • 77950830294 scopus 로고    scopus 로고
    • Inhibition of aldose reductase prevents growth factor-induced G1-S phase transition through the AKT/phosphoinositide 3-kinase/E2F-1 pathway in human colon cancer cells
    • K.V. Ramana, R. Tammali, S.K. Srivastava, Inhibition of aldose reductase prevents growth factor-induced G1-S phase transition through the AKT/phosphoinositide 3-kinase/E2F-1 pathway in human colon cancer cells, Mol. Cancer Ther. 9 (2010) 813-824.
    • (2010) Mol. Cancer Ther. , vol.9 , pp. 813-824
    • Ramana, K.V.1    Tammali, R.2    Srivastava, S.K.3
  • 117
    • 65549117476 scopus 로고    scopus 로고
    • Aldose reductase deficiency in mice prevents azoxymethane-induced colonic preneoplastic aberrant crypt foci formation
    • R. Tammali, A.B. Reddy, K.V. Ramana, J.M. Petrash, S.K. Srivastava, Aldose reductase deficiency in mice prevents azoxymethane-induced colonic preneoplastic aberrant crypt foci formation, Carcinogenesis 30 (2009) 799-807.
    • (2009) Carcinogenesis , vol.30 , pp. 799-807
    • Tammali, R.1    Reddy, A.B.2    Ramana, K.V.3    Petrash, J.M.4    Srivastava, S.K.5
  • 119
    • 0035097039 scopus 로고    scopus 로고
    • Overexpression of aldose reductase in liver cancers may contribute to drug resistance
    • DOI 10.1097/00001813-200102000-00005
    • K.W. Lee, B.C. Ko, Z. Jiang, D. Cao, S.S. Chung, Overexpression of aldose reductase in liver cancers may contribute to drug resistance, Anticancer Drugs 12 (2001) 129-132. (Pubitemid 32207361)
    • (2001) Anti-Cancer Drugs , vol.12 , Issue.2 , pp. 129-132
    • Lee, K.W.Y.1    Ko, B.C.B.2    Jiang, Z.3    Cao, D.4    Chung, S.S.M.5


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