메뉴 건너뛰기




Volumn 25, Issue SUPPL. 1, 1997, Pages

Oxidants, transcription factors, and intestinal inflammation

Author keywords

Activator protein 1; B cell lymphoma leukemia 2; Nitric oxide; Nuclear transcription factor B; Reactive oxygen metabolites

Indexed keywords

CYTOKINE; FREE RADICAL; GENE PRODUCT; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; NITRIC OXIDE; OXIDIZING AGENT; REACTIVE OXYGEN METABOLITE; TRANSCRIPTION FACTOR AP 1;

EID: 0031423504     PISSN: 01920790     EISSN: None     Source Type: Journal    
DOI: 10.1097/00004836-199700001-00011     Document Type: Conference Paper
Times cited : (34)

References (117)
  • 1
    • 0027959253 scopus 로고
    • Oxidants and free radicals in inflammatory bowel disease
    • Grisham MB. Oxidants and free radicals in inflammatory bowel disease. Lancet 1994;344:859-61.
    • (1994) Lancet , vol.344 , pp. 859-861
    • Grisham, M.B.1
  • 2
    • 0001010783 scopus 로고    scopus 로고
    • Role of reactive metabolites of oxygen and nitrogen in lymphocyte bowel disease: Toxins, mediators, and modulators of gene expression
    • Conner EM, Brand SJ, Davis JM, Kang DY, Grisham MB. Role of reactive metabolites of oxygen and nitrogen in lymphocyte bowel disease: toxins, mediators, and modulators of gene expression. Inflam Bowel Dis 1996;2:133-47.
    • (1996) Inflam Bowel Dis , vol.2 , pp. 133-147
    • Conner, E.M.1    Brand, S.J.2    Davis, J.M.3    Kang, D.Y.4    Grisham, M.B.5
  • 3
    • 0028466383 scopus 로고
    • Oxygen and the control of gene expression
    • Heike L, Baeuerle PA. Oxygen and the control of gene expression. BioEssays 1994;16:497-502.
    • (1994) BioEssays , vol.16 , pp. 497-502
    • Heike, L.1    Baeuerle, P.A.2
  • 5
    • 0027251053 scopus 로고
    • The pecking order of free radicals and anti-oxidants: Lipid peroxidation, α-tocopherol, and ascorbate
    • Buettner GR. The pecking order of free radicals and anti-oxidants: lipid peroxidation, α-tocopherol, and ascorbate. Arch Biochem Biophys 1993;300:535-43.
    • (1993) Arch Biochem Biophys , vol.300 , pp. 535-543
    • Buettner, G.R.1
  • 6
    • 0025776071 scopus 로고
    • Perhydroxyl radical initiated lipid peroxidation. the role of fatty acid hydroperoxides
    • Aikens J, Dix TA. Perhydroxyl radical initiated lipid peroxidation. The role of fatty acid hydroperoxides. J Biol Chem 1991;266:15091-8.
    • (1991) J Biol Chem , vol.266 , pp. 15091-15098
    • Aikens, J.1    Dix, T.A.2
  • 7
    • 0022559216 scopus 로고
    • Oxy-radicals and related species: Their formation, lifetimes, and reactions
    • Pryor WA. Oxy-radicals and related species: their formation, lifetimes, and reactions. Annu Rev Physiol 1986;48:657-67.
    • (1986) Annu Rev Physiol , vol.48 , pp. 657-667
    • Pryor, W.A.1
  • 8
    • 0023028228 scopus 로고
    • Stimulated human neutrophils limit iron-catalyzed hydroxyl radical formation as detected by spin-trapping techniques
    • Britigan BE, Rosen GM, Thompson BY, Chai Y, Cohen MS. Stimulated human neutrophils limit iron-catalyzed hydroxyl radical formation as detected by spin-trapping techniques. J Biol Chem 1986;261:17026-32.
    • (1986) J Biol Chem , vol.261 , pp. 17026-17032
    • Britigan, B.E.1    Rosen, G.M.2    Thompson, B.Y.3    Chai, Y.4    Cohen, M.S.5
  • 9
    • 0025129868 scopus 로고
    • Ferritin-dependent lipid peroxidation by stimulated neutrophils: Inhibition by myeloperoxidase-derived hypochlorous acid but not by endogenous lactoferrin
    • Winterbourn CC, Monteiro HP, Galilee CF. Ferritin-dependent lipid peroxidation by stimulated neutrophils: inhibition by myeloperoxidase-derived hypochlorous acid but not by endogenous lactoferrin. Biochhn Biophys Acta 1990; 1055:179-85.
    • (1990) Biochhn Biophys Acta , vol.1055 , pp. 179-185
    • Winterbourn, C.C.1    Monteiro, H.P.2    Galilee, C.F.3
  • 10
    • 0025189864 scopus 로고
    • Apparent hydroxyl radical production by peroxynitrite: Implication for endothelial injury from nitric oxide and superoxide
    • Beckman JS, Beckman TW, Chen J, Marshall PA, Freeman BA. Apparent hydroxyl radical production by peroxynitrite: implication for endothelial injury from nitric oxide and superoxide. Proc Natl Acad Sci USA 1990;87:1620.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 1620
    • Beckman, J.S.1    Beckman, T.W.2    Chen, J.3    Marshall, P.A.4    Freeman, B.A.5
  • 11
    • 0025730414 scopus 로고
    • Peroxynitrite oxidation of sulfhydryls: The cytotoxic potential of superoxide and nitric oxide
    • Radi R, Beckman JS, Bush KM, Freeman BA. Peroxynitrite oxidation of sulfhydryls: the cytotoxic potential of superoxide and nitric oxide. J Biol Chem 1991;266:4244.
    • (1991) J Biol Chem , vol.266 , pp. 4244
    • Radi, R.1    Beckman, J.S.2    Bush, K.M.3    Freeman, B.A.4
  • 12
    • 0028151406 scopus 로고
    • Nitric oxide regulation of superoxide and peroxynitrite-dependent lipid peroxidation: Formation of novel nitrogen-containing oxidized lipid derivatives
    • Rubbo H, Radi R, Trujillo M, et al. Nitric oxide regulation of superoxide and peroxynitrite-dependent lipid peroxidation: formation of novel nitrogen-containing oxidized lipid derivatives. J Biol Chem 1994;269:26066.
    • (1994) J Biol Chem , vol.269 , pp. 26066
    • Rubbo, H.1    Radi, R.2    Trujillo, M.3
  • 13
    • 0025874048 scopus 로고
    • Peroxynitrite-induced membrane lipid peroxidation: The cytotoxic potential of superoxide and nitric oxide
    • Radi R, Beckman JS, Bush KM, Freeman BA. Peroxynitrite-induced membrane lipid peroxidation: the cytotoxic potential of superoxide and nitric oxide. Arch Biochem Biophys 1991;288:481.
    • (1991) Arch Biochem Biophys , vol.288 , pp. 481
    • Radi, R.1    Beckman, J.S.2    Bush, K.M.3    Freeman, B.A.4
  • 16
    • 0026453418 scopus 로고
    • Peroxynitrite formation from macrophage-derived nitric oxide
    • Ischiropoulos H, Zhu L, Beckman JS. Peroxynitrite formation from macrophage-derived nitric oxide. Arch Biochem Biophys 1992;298:446-51.
    • (1992) Arch Biochem Biophys , vol.298 , pp. 446-451
    • Ischiropoulos, H.1    Zhu, L.2    Beckman, J.S.3
  • 19
    • 0027397892 scopus 로고
    • Increased nitric oxide synthesis in ulcerative colitis
    • Middleton SJ, Shorthouse M, Hunter JO. Increased nitric oxide synthesis in ulcerative colitis. Lancet 1993;341:465-6.
    • (1993) Lancet , vol.341 , pp. 465-466
    • Middleton, S.J.1    Shorthouse, M.2    Hunter, J.O.3
  • 20
    • 0027411517 scopus 로고
    • Mucosal injury and inflammation in a model of chronic granulomatous colitis in rats
    • Yamada T, Sartor RB, Marshall S, Specian RD, Grisham MB. Mucosal injury and inflammation in a model of chronic granulomatous colitis in rats. Gastroenterology 1993;104: 759-71.
    • (1993) Gastroenterology , vol.104 , pp. 759-771
    • Yamada, T.1    Sartor, R.B.2    Marshall, S.3    Specian, R.D.4    Grisham, M.B.5
  • 21
    • 0027255461 scopus 로고
    • Nitric oxide synthase activity in ulcerative colitis and Crohn's disease
    • Boughton-Smith NK, Evans SM, Hawkey CJ, et al. Nitric oxide synthase activity in ulcerative colitis and Crohn's disease. Lancet 1993;342:338-40.
    • (1993) Lancet , vol.342 , pp. 338-340
    • Boughton-Smith, N.K.1    Evans, S.M.2    Hawkey, C.J.3
  • 22
    • 0028072869 scopus 로고
    • Effects of nitric oxide synthase inhibition on the pathophysiology observed in a model of chronic granulomatous colitis
    • Grisham MB, Specian RD, Zimmerman TE. Effects of nitric oxide synthase inhibition on the pathophysiology observed in a model of chronic granulomatous colitis. J Pharmacol Exp Ther 1994;271:1114.
    • (1994) J Pharmacol Exp Ther , vol.271 , pp. 1114
    • Grisham, M.B.1    Specian, R.D.2    Zimmerman, T.E.3
  • 23
    • 0027752805 scopus 로고
    • The L-arginine-nitric oxide pathway
    • Moncada S, Higgs A. The L-arginine-nitric oxide pathway. N Engl J Med 1993;329:2002.
    • (1993) N Engl J Med , vol.329 , pp. 2002
    • Moncada, S.1    Higgs, A.2
  • 25
    • 0028810868 scopus 로고
    • Nitric oxide synthase in circulating vs. extravasated polymorphonuclear leukocytes
    • Miles AM, Owens MW, Milligan S, et al. Nitric oxide synthase in circulating vs. extravasated polymorphonuclear leukocytes. J Leukocyte Biol 1995;58:616.
    • (1995) J Leukocyte Biol , vol.58 , pp. 616
    • Miles, A.M.1    Owens, M.W.2    Milligan, S.3
  • 26
    • 0029133539 scopus 로고
    • Human mononuclear phagocyte inducible nitric oxide synthase (iNOS): Analysis of iNOS mRNA, iNOS protein, biopterin, and nitric oxide production by blood monocytes and peritonial macrophages
    • Weinberg JB, Misukonis MA, Shami PJ, et al. Human mononuclear phagocyte inducible nitric oxide synthase (iNOS): analysis of iNOS mRNA, iNOS protein, biopterin, and nitric oxide production by blood monocytes and peritonial macrophages. Blood 1995;86:1184.
    • (1995) Blood , vol.86 , pp. 1184
    • Weinberg, J.B.1    Misukonis, M.A.2    Shami, P.J.3
  • 27
    • 0019726454 scopus 로고
    • Oxidation of nitrogen oxide-by bound dioxygen in hemoproteins
    • Doyle MP, Hoekstra JW. Oxidation of nitrogen oxide-by bound dioxygen in hemoproteins. J Inorgan Blochem 1981; 14:351-8.
    • (1981) J Inorgan Blochem , vol.14 , pp. 351-358
    • Doyle, M.P.1    Hoekstra, J.W.2
  • 28
    • 0028132836 scopus 로고
    • Redox signalling: Nitrosylation and related target interactions of nitric oxide
    • Stamler J. Redox signalling: nitrosylation and related target interactions of nitric oxide. Cell 1994;78:931-6.
    • (1994) Cell , vol.78 , pp. 931-936
    • Stamler, J.1
  • 30
    • 0028804235 scopus 로고
    • Reactive oxygen and nitrogen metabolites as mediators of secretory diarrhea
    • Gaginella TS, Kachur JF, Tamai H, Keshavarzian A. Reactive oxygen and nitrogen metabolites as mediators of secretory diarrhea. Gastroenterology 1995;109:2019.
    • (1995) Gastroenterology , vol.109 , pp. 2019
    • Gaginella, T.S.1    Kachur, J.F.2    Tamai, H.3    Keshavarzian, A.4
  • 31
    • 0024602827 scopus 로고
    • Tissue destruction by neutrophils
    • Weiss SJ. Tissue destruction by neutrophils. N Engl J Med 1989;320:365.
    • (1989) N Engl J Med , vol.320 , pp. 365
    • Weiss, S.J.1
  • 34
    • 0023900998 scopus 로고    scopus 로고
    • Neutrophil-mediated mucosal injury: Role of reactive oxygen metabolites
    • Grisham MB, Granger DN. Neutrophil-mediated mucosal injury: role of reactive oxygen metabolites. Dig Dis Sci 1998; 33:6s-15s.
    • (1998) Dig Dis Sci , vol.33
    • Grisham, M.B.1    Granger, D.N.2
  • 35
    • 0026629065 scopus 로고
    • Excessive production of reactive oxygen metabolites by inflamed colon: Analysis by chemiluminescence probe
    • Keshavarzian A, Sedghi S, Kanofsky J, et al. Excessive production of reactive oxygen metabolites by inflamed colon: analysis by chemiluminescence probe. Gastroenterology 1992;103:177-85.
    • (1992) Gastroenterology , vol.103 , pp. 177-185
    • Keshavarzian, A.1    Sedghi, S.2    Kanofsky, J.3
  • 36
    • 0026748627 scopus 로고
    • Chemiluminescence assay of mucosal reactive oxygen metabolites in inflammatory bowel disease
    • Simmonds NJ, Allen RE, Stevens TRJ, et al. Chemiluminescence assay of mucosal reactive oxygen metabolites in inflammatory bowel disease. Gastroenterology 1992;103:186-96.
    • (1992) Gastroenterology , vol.103 , pp. 186-196
    • Simmonds, N.J.1    Allen, R.E.2    Stevens, T.R.J.3
  • 37
    • 0027283397 scopus 로고
    • Location of superoxide anion generation in human colonic mucosa obtained by biopsy
    • Oshitani N, Kitano A, Okabe H, Nakamura S, Matumoto T, Kobayashi K. Location of superoxide anion generation in human colonic mucosa obtained by biopsy. Gut 1993;34: 936-8.
    • (1993) Gut , vol.34 , pp. 936-938
    • Oshitani, N.1    Kitano, A.2    Okabe, H.3    Nakamura, S.4    Matumoto, T.5    Kobayashi, K.6
  • 39
    • 4243868837 scopus 로고
    • Colonic epithelial cell glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a target of oxidative injury in inflammatory bowel disease (IBD)
    • McKenzi SJ, Buffinton GD, Baker MS, Doe WF. Colonic epithelial cell glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a target of oxidative injury in inflammatory bowel disease (IBD) [Abstract]. Gastroenterology 1993;104: A741.
    • (1993) Gastroenterology , vol.104
    • McKenzi, S.J.1    Buffinton, G.D.2    Baker, M.S.3    Doe, W.F.4
  • 40
    • 0029071036 scopus 로고
    • Spontaneous intestinal inflammation and nitric oxide metabolism in HLA-B27 transgenic rats
    • Aiko S, Grisham MB. Spontaneous intestinal inflammation and nitric oxide metabolism in HLA-B27 transgenic rats. Gastroenterology 1995;109:142-50.
    • (1995) Gastroenterology , vol.109 , pp. 142-150
    • Aiko, S.1    Grisham, M.B.2
  • 41
    • 0028069352 scopus 로고
    • Cytokines in intestinal inflammation. Pathophysiologic and clinical considerations
    • Sartor RB. Cytokines in intestinal inflammation. Pathophysiologic and clinical considerations. Gastroenterology 1994;106:533-7.
    • (1994) Gastroenterology , vol.106 , pp. 533-537
    • Sartor, R.B.1
  • 43
    • 0026075996 scopus 로고
    • Decrease in two intestinal copper/ zinc containing proteins with antioxidant function in inflammatory bowel disease
    • Mulder TPJ, Verspaget HW, Janssens AR, de Bruin PAF, Pena AS, Lamers CBHW. Decrease in two intestinal copper/ zinc containing proteins with antioxidant function in inflammatory bowel disease. Gut 1991;32:1146.
    • (1991) Gut , vol.32 , pp. 1146
    • Mulder, T.P.J.1    Verspaget, H.W.2    Janssens, A.R.3    De Bruin, P.A.F.4    Pena, A.S.5    Lamers, C.B.H.W.6
  • 44
    • 0028883592 scopus 로고
    • Depleted mucosal antioxidant defences in inflammatory bowel disease
    • Buffinton GD, Doe WF. Depleted mucosal antioxidant defences in inflammatory bowel disease. Free Rad Biol Med 1995;19:911.
    • (1995) Free Rad Biol Med , vol.19 , pp. 911
    • Buffinton, G.D.1    Doe, W.F.2
  • 47
    • 34548004905 scopus 로고
    • Orally administered oxygen radical scavenger (vitamin E) reduces mucosal damage in a rat model of inflammatory colitis
    • Blumerstein BJ, Ma CK, Zhang X, Hadzijahic N, Fogel R. Orally administered oxygen radical scavenger (vitamin E) reduces mucosal damage in a rat model of inflammatory colitis [Abstract]. Gastroenterology 1994;105:A2011.
    • (1994) Gastroenterology , vol.105
    • Blumerstein, B.J.1    Ma, C.K.2    Zhang, X.3    Hadzijahic, N.4    Fogel, R.5
  • 48
    • 0024440111 scopus 로고
    • Phase II trial of copper zinc superoxide dismutase (CuZnSOD) in treatment of Crohn's disease
    • Emerit J, Pelletier S, Tosoni-Verilignue D, Mollete M. Phase II trial of copper zinc superoxide dismutase (CuZnSOD) in treatment of Crohn's disease. Free Rad Biol Med 1989;7:145.
    • (1989) Free Rad Biol Med , vol.7 , pp. 145
    • Emerit, J.1    Pelletier, S.2    Tosoni-Verilignue, D.3    Mollete, M.4
  • 49
    • 0024510535 scopus 로고
    • 5-aminosalicylic acid concentration in mucosal interstitium of cat small and large intestine
    • Grisham MB, Granger DN. 5-aminosalicylic acid concentration in mucosal interstitium of cat small and large intestine. Dig Dis Sci 1989;34:573.
    • (1989) Dig Dis Sci , vol.34 , pp. 573
    • Grisham, M.B.1    Granger, D.N.2
  • 50
    • 0025606773 scopus 로고
    • Antioxidant properties of 5-ASA: Potential mechanism for its antiinflammatory activity
    • Yamada T, Volkmer C, Grisham MB. Antioxidant properties of 5-ASA: potential mechanism for its antiinflammatory activity. Can J Gastroenterol 1990;4:295-302.
    • (1990) Can J Gastroenterol , vol.4 , pp. 295-302
    • Yamada, T.1    Volkmer, C.2    Grisham, M.B.3
  • 51
  • 52
  • 53
    • 15444347454 scopus 로고
    • Effect of acute and chronic NOS inhibition on splanchnic organ blood flow: Implications in gut and liver pathophysiology
    • Aiko S, Benoit JN, Davis JM, Grisham MB. Effect of acute and chronic NOS inhibition on splanchnic organ blood flow: implications in gut and liver pathophysiology [Abstract]. Gastroenterology 1995;108:A268.
    • (1995) Gastroenterology , vol.108
    • Aiko, S.1    Benoit, J.N.2    Davis, J.M.3    Grisham, M.B.4
  • 56
    • 0025008984 scopus 로고
    • Effects of neutrophil-derived oxidants on intestinal permeability. Electrolyte transport and cell viability
    • Grisham MB, Gaginella TS, von Ritter C, Tamai H, Be RM, Granger DN. Effects of neutrophil-derived oxidants on intestinal permeability. Electrolyte transport and cell viability. Inflammation 1990;14:531-42.
    • (1990) Inflammation , vol.14 , pp. 531-542
    • Grisham, M.B.1    Gaginella, T.S.2    Von Ritter, C.3    Tamai, H.4    Be, R.M.5    Granger, D.N.6
  • 57
    • 0028174061 scopus 로고
    • Function and activation of NF-κB in the immune system
    • Baeuerle PA, Henkle T. Function and activation of NF-κB in the immune system. Annu Rev Immunol 1994;12:141-79.
    • (1994) Annu Rev Immunol , vol.12 , pp. 141-179
    • Baeuerle, P.A.1    Henkle, T.2
  • 58
    • 0028985037 scopus 로고
    • NF-κB and Rel proteins in an innate immunity
    • Kopp E, Ghosh S. NF-κB and Rel proteins in an innate immunity. Adv Immunol 1994;58:1-27.
    • (1994) Adv Immunol , vol.58 , pp. 1-27
    • Kopp, E.1    Ghosh, S.2
  • 59
    • 0346011011 scopus 로고
    • IκB: A specific inhibitor of the NF-κB transcription factor
    • Baeuerle PA, Baltimore D. IκB: a specific inhibitor of the NF-κB transcription factor. Science 1995;268:522-3.
    • (1995) Science , vol.268 , pp. 522-523
    • Baeuerle, P.A.1    Baltimore, D.2
  • 60
    • 0025343895 scopus 로고
    • Activation of interleukin-6 gene expression through the NF-κB transcription factor
    • Lieberman TA, Baltimore D. Activation of interleukin-6 gene expression through the NF-κB transcription factor. Mol Cell Biol 1990;10:2327-34.
    • (1990) Mol Cell Biol , vol.10 , pp. 2327-2334
    • Lieberman, T.A.1    Baltimore, D.2
  • 61
    • 0028961951 scopus 로고
    • Endothelial IRF-1 cooperates with NF-κB as a transcriptional activator of vascular cell adhesion molecule-1
    • Neish AS, Read MA, Thanos D, Pine R, Maniatis T, Collins T. Endothelial IRF-1 cooperates with NF-κB as a transcriptional activator of vascular cell adhesion molecule-1. Mol Cell Biol 1995;19:2558-69.
    • (1995) Mol Cell Biol , vol.19 , pp. 2558-2569
    • Neish, A.S.1    Read, M.A.2    Thanos, D.3    Pine, R.4    Maniatis, T.5    Collins, T.6
  • 62
    • 0028238576 scopus 로고
    • Oxidative stress induced NF-κB binding and inducible NOS mRNA in human epithelial cells
    • Adcock IM, Brown CR, Kwon O, Barnes PJ. Oxidative stress induced NF-κB binding and inducible NOS mRNA in human epithelial cells. Biochem Biophys Res Commun 1994; 199:1518-24.
    • (1994) Biochem Biophys Res Commun , vol.199 , pp. 1518-1524
    • Adcock, I.M.1    Brown, C.R.2    Kwon, O.3    Barnes, P.J.4
  • 63
    • 0027959628 scopus 로고
    • Inhibition by N-acetyl-L-cysteine of interleukin-6 mRNA induction and activation of NF-κB by tumor necrosis factor α in a mouse fibroblastic cell line, Balb/3T3
    • Shibanuma M, Kuroki T, Nose K. Inhibition by N-acetyl-L-cysteine of interleukin-6 mRNA induction and activation of NF-κB by tumor necrosis factor α in a mouse fibroblastic cell line, Balb/3T3. FEBS Lett 1994;353:62-6.
    • (1994) FEBS Lett , vol.353 , pp. 62-66
    • Shibanuma, M.1    Kuroki, T.2    Nose, K.3
  • 64
    • 0027310696 scopus 로고
    • Inhibition of NF-κB by vitamin e derivatives
    • Suzuki YJ, Packer L. Inhibition of NF-κB by vitamin E derivatives. Biochem Biophys Res Commun 1993;193:277-83.
    • (1993) Biochem Biophys Res Commun , vol.193 , pp. 277-283
    • Suzuki, Y.J.1    Packer, L.2
  • 65
    • 0027076462 scopus 로고
    • α-lipoic acid as a potent inhibitors of NF-κB activation in human T cells
    • Suzuki YJ, Aggarwal BB, Packer L. α-lipoic acid as a potent inhibitors of NF-κB activation in human T cells. Biochem Biophys Res Commun 1992;189:1709-15.
    • (1992) Biochem Biophys Res Commun , vol.189 , pp. 1709-1715
    • Suzuki, Y.J.1    Aggarwal, B.B.2    Packer, L.3
  • 66
    • 0026590541 scopus 로고
    • Dithiocarbamates as potent inhibitor of nuclear factor κB in intact cells
    • Schreck R, Meier B, Mannel DN, Droge W, Baeuerle PA. Dithiocarbamates as potent inhibitor of nuclear factor κB in intact cells. J Exp Med 1992;175:11810.
    • (1992) J Exp Med , vol.175 , pp. 11810
    • Schreck, R.1    Meier, B.2    Mannel, D.N.3    Droge, W.4    Baeuerle, P.A.5
  • 67
    • 0342742310 scopus 로고
    • TNF-α and interleukin-1 stimulate the human immunodeficiency virus enhancer by activation of the NF-κB
    • Osborn L, Kunkel S, Nabel GJ. TNF-α and interleukin-1 stimulate the human immunodeficiency virus enhancer by activation of the NF-κB. Proc Natl Acad Sci USA 1989;86: 2336-40.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 2336-2340
    • Osborn, L.1    Kunkel, S.2    Nabel, G.J.3
  • 68
    • 0028099150 scopus 로고
    • Signal transduction for nuclear factor-kB activation. Proposed location of antioxidant-inhibitable step
    • Suzuki YJ, Mizuno M, Packer L. Signal transduction for nuclear factor-kB activation. Proposed location of antioxidant-inhibitable step. J Immunol 1994;153:5008-15.
    • (1994) J Immunol , vol.153 , pp. 5008-5015
    • Suzuki, Y.J.1    Mizuno, M.2    Packer, L.3
  • 69
    • 0026970404 scopus 로고
    • NF-κB: An oxidative stress responsive transcription factor of eukaryotic cells
    • Schreck R, Albermann K, Baeuerle PA. NF-κB: an oxidative stress responsive transcription factor of eukaryotic cells. Free Rad Res Commun 1992;17:221-37.
    • (1992) Free Rad Res Commun , vol.17 , pp. 221-237
    • Schreck, R.1    Albermann, K.2    Baeuerle, P.A.3
  • 70
    • 0028945307 scopus 로고
    • Modified low density lipoprotein and its constituents augment cytokine-activated vascular cell adhesion molecule-1 gene expression in human vascular endothlial cells
    • Khan BV, Parthasarathy SS, Alexander RW, Medford RM. Modified low density lipoprotein and its constituents augment cytokine-activated vascular cell adhesion molecule-1 gene expression in human vascular endothlial cells. J Clin Invest 1993;95:1262-70.
    • (1993) J Clin Invest , vol.95 , pp. 1262-1270
    • Khan, B.V.1    Parthasarathy, S.S.2    Alexander, R.W.3    Medford, R.M.4
  • 72
    • 0029200072 scopus 로고
    • Oxidant-sensitive and phosphorylation-dependent activation of NF-κB and AP-1 in endothelial cells
    • Barchowsky A, Munro SR, Morona SJ, Vinceti MP, Treadwell M. Oxidant-sensitive and phosphorylation-dependent activation of NF-κB and AP-1 in endothelial cells. Am J Physiol 1995;269:L829-36.
    • (1995) Am J Physiol , vol.269
    • Barchowsky, A.1    Munro, S.R.2    Morona, S.J.3    Vinceti, M.P.4    Treadwell, M.5
  • 73
    • 0027301991 scopus 로고
    • Conserved cysteine residues are critical for the enzymatic function of the lymphocyte-specific tyrosine protein kinase p56lck
    • Veillette A, Dumont S, Fournel M. Conserved cysteine residues are critical for the enzymatic function of the lymphocyte-specific tyrosine protein kinase p56lck. J Biol Chem 1993;268:17547-53.
    • (1993) J Biol Chem , vol.268 , pp. 17547-17553
    • Veillette, A.1    Dumont, S.2    Fournel, M.3
  • 74
    • 0030004897 scopus 로고    scopus 로고
    • Site-specific phosphorylation of IκBα by a novel ubiquination-dependent protein kinase activity
    • Chen ZJ, Parent L, Maniatis T. Site-specific phosphorylation of IκBα by a novel ubiquination-dependent protein kinase activity. Cell 1996;84:853-62.
    • (1996) Cell , vol.84 , pp. 853-862
    • Chen, Z.J.1    Parent, L.2    Maniatis, T.3
  • 75
    • 0025852479 scopus 로고
    • Modulation of transcription factor NF-κB binding activity by oxidation-reduction in vitro
    • Toledano MN, Leonard WJ. Modulation of transcription factor NF-κB binding activity by oxidation-reduction in vitro. Proc Natl Acad Sci USA 1991;88:4328-32.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 4328-4332
    • Toledano, M.N.1    Leonard, W.J.2
  • 76
    • 0028029457 scopus 로고
    • Functions of glutathione disulfide in immunology and immunopathology
    • Droge W, Schulze-Osthoff K, Mihn S. Functions of glutathione disulfide in immunology and immunopathology. FASEB J 1994;8:1131-8.
    • (1994) FASEB J , vol.8 , pp. 1131-1138
    • Droge, W.1    Schulze-Osthoff, K.2    Mihn, S.3
  • 77
    • 0029011129 scopus 로고
    • Induction and stabilization of IkBα by nitric oxide mediates inhibition of NF-κB
    • Peng H-B, Libby L, Lia JK. Induction and stabilization of IkBα by nitric oxide mediates inhibition of NF-κB. J Biol Chem 1995;270:14214-9.
    • (1995) J Biol Chem , vol.270 , pp. 14214-14219
    • Peng, H.-B.1    Libby, L.2    Lia, J.K.3
  • 78
    • 0029071646 scopus 로고
    • Functions of the proteasome: The lysis at the end of the tunnel
    • Goldberg AL. Functions of the proteasome: the lysis at the end of the tunnel. Science 1995;268:522-3.
    • (1995) Science , vol.268 , pp. 522-523
    • Goldberg, A.L.1
  • 79
    • 0028018268 scopus 로고
    • The ubiquitin-proteasome proteolytic pathway
    • Ciechanover A. The ubiquitin-proteasome proteolytic pathway. Cell 1994;79:13-21.
    • (1994) Cell , vol.79 , pp. 13-21
    • Ciechanover, A.1
  • 80
    • 0027207242 scopus 로고
    • Tumor necrosis factor and interleukin-1 lead to phosphorylation and loss of I-κB
    • Beg AA, Finco TS, Nanternet PV, Baldwin AS. Tumor necrosis factor and interleukin-1 lead to phosphorylation and loss of I-κB. Mol Cell Biol 1993;13:3301-10.
    • (1993) Mol Cell Biol , vol.13 , pp. 3301-3310
    • Beg, A.A.1    Finco, T.S.2    Nanternet, P.V.3    Baldwin, A.S.4
  • 81
    • 0028986075 scopus 로고
    • Control of IκB-α proteolysis by site-specific, signal induced phosphorylation
    • Brown K, Gerstberger S, Carlson L, Franzoso G, Siebenlist U. Control of IκB-α proteolysis by site-specific, signal induced phosphorylation. Science 1995;267:1485-8.
    • (1995) Science , vol.267 , pp. 1485-1488
    • Brown, K.1    Gerstberger, S.2    Carlson, L.3    Franzoso, G.4    Siebenlist, U.5
  • 82
    • 0027980321 scopus 로고
    • The ubiquitin-proteasome pathway is required for processing the NF-κBI precursor protein and the activation of NF-κB
    • Palombella VJ, Rando OJ, Goldberg AL, Maniatis T. The ubiquitin-proteasome pathway is required for processing the NF-κBI precursor protein and the activation of NF-κB. Cell 1994;78:773-85.
    • (1994) Cell , vol.78 , pp. 773-785
    • Palombella, V.J.1    Rando, O.J.2    Goldberg, A.L.3    Maniatis, T.4
  • 83
    • 0025186678 scopus 로고
    • κB-type enhancers are involved in lipopolysaccharide-mediated transcriptional activation of tumor necrosis factor α gene in primary macrophages
    • Shakhov AN, Collart MA, Vassilli P, Nedospasov SA, Jongeneel CV. κB-type enhancers are involved in lipopolysaccharide-mediated transcriptional activation of tumor necrosis factor α gene in primary macrophages. J Exp Med 1990; 171:35-47.
    • (1990) J Exp Med , vol.171 , pp. 35-47
    • Shakhov, A.N.1    Collart, M.A.2    Vassilli, P.3    Nedospasov, S.A.4    Jongeneel, C.V.5
  • 84
    • 0024584166 scopus 로고
    • Kappa-B specific DNA binding proteins: Role in the regulation of human interleukin-2 gene expression
    • Hoyos B, Ballard DW, Bohnlein E, Siekevity M, Greene WC. Kappa-B specific DNA binding proteins: role in the regulation of human interleukin-2 gene expression. Science 1989;244:457-60.
    • (1989) Science , vol.244 , pp. 457-460
    • Hoyos, B.1    Ballard, D.W.2    Bohnlein, E.3    Siekevity, M.4    Greene, W.C.5
  • 85
    • 0028901615 scopus 로고
    • Transcriptional regulation of endothelial cell adhesion molecules: A dominant role for NF-κB
    • Chen CC, Manning AM. Transcriptional regulation of endothelial cell adhesion molecules: a dominant role for NF-κB. Agents Actions 1995;47(suppl.):135-41.
    • (1995) Agents Actions , vol.47 , Issue.SUPPL. , pp. 135-141
    • Chen, C.C.1    Manning, A.M.2
  • 86
    • 0008705813 scopus 로고    scopus 로고
    • Inhibition of chronic granulomatous colitis by a selective proteasome inhibitor: Antagonist of nuclear transcription factor kB (NFkB) activation
    • Connor EM, Brand S, Grisham MB. Inhibition of chronic granulomatous colitis by a selective proteasome inhibitor: antagonist of nuclear transcription factor kB (NFkB) activation [Abstract]. Gastroenterology 1996;110:A886.
    • (1996) Gastroenterology , vol.110
    • Connor, E.M.1    Brand, S.2    Grisham, M.B.3
  • 87
    • 0028986193 scopus 로고
    • NF-κB. A lesson in family values
    • Thanos D, Maniatis T. NF-κB. A lesson in family values. Cell 1995;80:529-32.
    • (1995) Cell , vol.80 , pp. 529-532
    • Thanos, D.1    Maniatis, T.2
  • 88
    • 0025720735 scopus 로고
    • The role of Jun, Fos and the AP-1 complex in cell proliferation and transcription
    • Angel P, Karin M. The role of Jun, Fos and the AP-1 complex in cell proliferation and transcription. Biochim Biophys Acta 1991;1072:129-57.
    • (1991) Biochim Biophys Acta , vol.1072 , pp. 129-157
    • Angel, P.1    Karin, M.2
  • 89
    • 0024276585 scopus 로고
    • DNA binding activities of 3 murine Jun proteins: Stimulation by Fos
    • Nakabeppu Y, Ryder K, Nathans D. DNA binding activities of 3 murine Jun proteins: stimulation by Fos. Cell 1988;55: 907-15.
    • (1988) Cell , vol.55 , pp. 907-915
    • Nakabeppu, Y.1    Ryder, K.2    Nathans, D.3
  • 90
    • 0027269781 scopus 로고
    • 2 and antioxidants have opposite effects on activation of NFκB and AP-1 in intact cells: AP-1 as secondary antioxidant-responsive factor
    • 2 and antioxidants have opposite effects on activation of NFκB and AP-1 in intact cells: AP-1 as secondary antioxidant-responsive factor. EMBO J 1993;12:2005-15.
    • (1993) EMBO J , vol.12 , pp. 2005-2015
    • Meyer, M.1    Schreck, R.2    Baeuerle, P.A.3
  • 91
    • 0029990552 scopus 로고    scopus 로고
    • Role of oxidants and antioxidants in the induction of AP-1, NF-κB, and glutathione S-transferase gene expression
    • Pinkus R, Weiner LM, Daniel V. Role of oxidants and antioxidants in the induction of AP-1, NF-κB, and glutathione S-transferase gene expression. J Biol Chem 1996;271: 13422-9.
    • (1996) J Biol Chem , vol.271 , pp. 13422-13429
    • Pinkus, R.1    Weiner, L.M.2    Daniel, V.3
  • 92
    • 0025173617 scopus 로고
    • Phosphorylation of the C terminus of Fos protein is required for transcriptional transrepression of the c-fos promoter
    • Rivka O, Dwarki VJ, Rashid D, Verma IM. Phosphorylation of the C terminus of Fos protein is required for transcriptional transrepression of the c-fos promoter. Nature 1990; 348:80-2.
    • (1990) Nature , vol.348 , pp. 80-82
    • Rivka, O.1    Dwarki, V.J.2    Rashid, D.3    Verma, I.M.4
  • 93
    • 0026029808 scopus 로고
    • Activation of protein kinase C decreases phosphorylation of c-jun at sites that negatively regulate its DNA-binding activity
    • Boyle WJ, Smeal T, Defize LHK. Activation of protein kinase C decreases phosphorylation of c-jun at sites that negatively regulate its DNA-binding activity. Cell 1991;64:573-84.
    • (1991) Cell , vol.64 , pp. 573-584
    • Boyle, W.J.1    Smeal, T.2    Defize, L.H.K.3
  • 94
    • 0027049804 scopus 로고
    • The mammalian ultraviolet response is triggered by activation of Src tyrosine kinases
    • Devary Y, Gottlieb RA, Smeal T, Karin M. The mammalian ultraviolet response is triggered by activation of Src tyrosine kinases. Cell 1992;71:1061-91.
    • (1992) Cell , vol.71 , pp. 1061-1091
    • Devary, Y.1    Gottlieb, R.A.2    Smeal, T.3    Karin, M.4
  • 95
    • 0025077481 scopus 로고    scopus 로고
    • Redox regulation of Fos and Jun DNA-binding activity in vitro
    • Abate C, Patel L, Rausher III FJ, Curran T. Redox regulation of Fos and Jun DNA-binding activity in vitro. Science 1996;249:1157-61.
    • (1996) Science , vol.249 , pp. 1157-1161
    • Abate, C.1    Patel, L.2    Rausher III, F.J.3    Curran, T.4
  • 96
    • 0026714672 scopus 로고
    • Redox activation of Fos-Jun DNA binding activity is mediated by a DNA repair enzyme
    • Xanthoudakis S, Miao G, Wang F, Pan YE, Curran T. Redox activation of Fos-Jun DNA binding activity is mediated by a DNA repair enzyme. EMBO J 1992;11:3323-35.
    • (1992) EMBO J , vol.11 , pp. 3323-3335
    • Xanthoudakis, S.1    Miao, G.2    Wang, F.3    Pan, Y.E.4    Curran, T.5
  • 97
    • 0028589378 scopus 로고
    • Regulation of cell number in the mammalian gastrointestinal tract: The importance of apoptosis
    • Hall PA, Coates PJ, Ansari B, Hopwood D. Regulation of cell number in the mammalian gastrointestinal tract: the importance of apoptosis. J Cell Sci 1994;107:3569-77.
    • (1994) J Cell Sci , vol.107 , pp. 3569-3577
    • Hall, P.A.1    Coates, P.J.2    Ansari, B.3    Hopwood, D.4
  • 98
    • 0028040019 scopus 로고
    • Bcl-2 and the regulation of programmed cell death
    • Reed JC. Bcl-2 and the regulation of programmed cell death. J Biol Chem 1994;124:1-6.
    • (1994) J Biol Chem , vol.124 , pp. 1-6
    • Reed, J.C.1
  • 101
    • 0027717968 scopus 로고
    • Bcl-2 inhibition of neural death: Decreased generation of reactive oxygen species
    • Kane DJ, Sarafian TA, Anton R. Bcl-2 inhibition of neural death: decreased generation of reactive oxygen species. Science 1993;262:1274-7.
    • (1993) Science , vol.262 , pp. 1274-1277
    • Kane, D.J.1    Sarafian, T.A.2    Anton, R.3
  • 102
    • 0028292480 scopus 로고
    • Identification of a p53-dependent negative response element in the bcl-2 gene
    • Miyashita T, Harigai M, Hanada M, Reed JC. Identification of a p53-dependent negative response element in the bcl-2 gene. Cancer Res 1994;54:3131-5.
    • (1994) Cancer Res , vol.54 , pp. 3131-3135
    • Miyashita, T.1    Harigai, M.2    Hanada, M.3    Reed, J.C.4
  • 103
    • 0025751550 scopus 로고
    • Bcl-2 inhibits multiple forms of apoptosis but not negative selection in thymocytes
    • Sentman CL, Shutter JR, Hockenbery D, Kanagawa O, Korsmeyer SJ. Bcl-2 inhibits multiple forms of apoptosis but not negative selection in thymocytes. Cell 1991;67:879-88.
    • (1991) Cell , vol.67 , pp. 879-888
    • Sentman, C.L.1    Shutter, J.R.2    Hockenbery, D.3    Kanagawa, O.4    Korsmeyer, S.J.5
  • 104
    • 0028910217 scopus 로고
    • The Bcl-2 oncoprotein functions as a prooxidant
    • Steinman HM. The Bcl-2 oncoprotein functions as a prooxidant. J Biol Chem 1995;270:3487-90.
    • (1995) J Biol Chem , vol.270 , pp. 3487-3490
    • Steinman, H.M.1
  • 105
    • 0028036895 scopus 로고
    • Immunohistochemical determination of in vivo distribution of Bax, a dominant inhibitor of Bcl-2
    • Krajewski S, Krajewska M, Shabaik A, Miyashita T, Wang HG, Reed JC. Immunohistochemical determination of in vivo distribution of Bax, a dominant inhibitor of Bcl-2. Am J Pathol 1994;145:1323-36.
    • (1994) Am J Pathol , vol.145 , pp. 1323-1336
    • Krajewski, S.1    Krajewska, M.2    Shabaik, A.3    Miyashita, T.4    Wang, H.G.5    Reed, J.C.6
  • 106
    • 0029048596 scopus 로고
    • Differential expression of Bcl-2 in intestinal epithelia. Correlation with attenuation of apoptosis in colonic crypt cells and the incidence of colonic neoplasia
    • Merrit AJ, Potten CS, Watson AJM, Loh DY, Nakayama K, Hicman JA. Differential expression of Bcl-2 in intestinal epithelia. Correlation with attenuation of apoptosis in colonic crypt cells and the incidence of colonic neoplasia. J Cell Sci 1995;1081:2261-71.
    • (1995) J Cell Sci , vol.1081 , pp. 2261-2271
    • Merrit, A.J.1    Potten, C.S.2    Watson, A.J.M.3    Loh, D.Y.4    Nakayama, K.5    Hicman, J.A.6
  • 107
    • 0029863317 scopus 로고    scopus 로고
    • Cell death by apoptosis: Basic concepts and disease relevance for the gastroenterologist
    • Que FG, Gores GJ. Cell death by apoptosis: basic concepts and disease relevance for the gastroenterologist. Gastroenterology 1996;110:1238-43.
    • (1996) Gastroenterology , vol.110 , pp. 1238-1243
    • Que, F.G.1    Gores, G.J.2
  • 108
    • 0028943734 scopus 로고
    • Apoptosis in the pathogenesis and treatment of disease
    • Thompson C. Apoptosis in the pathogenesis and treatment of disease. Science 1995;267:1456-62.
    • (1995) Science , vol.267 , pp. 1456-1462
    • Thompson, C.1
  • 109
    • 0028941441 scopus 로고
    • Inhibition of apoptosis during development of colorectal cancer
    • Bedi A, Pasricha PJ, Akhtar AJ. Inhibition of apoptosis during development of colorectal cancer. Cancer Res 1995;55: 1811-6.
    • (1995) Cancer Res , vol.55 , pp. 1811-1816
    • Bedi, A.1    Pasricha, P.J.2    Akhtar, A.J.3
  • 110
    • 0028814213 scopus 로고
    • The bcl-2 protooncogene and the gastrointestinal epithelial tumor progression model
    • Bronner MP, Culin C, Reed JC, Furth EE. The bcl-2 protooncogene and the gastrointestinal epithelial tumor progression model. Am J Pathol 1995;146:20-6.
    • (1995) Am J Pathol , vol.146 , pp. 20-26
    • Bronner, M.P.1    Culin, C.2    Reed, J.C.3    Furth, E.E.4
  • 111
    • 0026771382 scopus 로고
    • Follicular lymphomas of the gastrointestinal tract: Pathological features in 31 cases and Bcl-2 oncogenic protein expression
    • LeBrun DP, Kamel OW, Cleary ML, Dorfman RF, Warnke RA. Follicular lymphomas of the gastrointestinal tract: pathological features in 31 cases and Bcl-2 oncogenic protein expression. Am J Pathol 1992;140:1327-35.
    • (1992) Am J Pathol , vol.140 , pp. 1327-1335
    • LeBrun, D.P.1    Kamel, O.W.2    Cleary, M.L.3    Dorfman, R.F.4    Warnke, R.A.5
  • 112
    • 0028335717 scopus 로고
    • Tumor suppressor p53 is a regulator of bcl-2 and bax gene expression in vitro and in vivo
    • Miyashita T, Harigai M, Krajewska M. Tumor suppressor p53 is a regulator of bcl-2 and bax gene expression in vitro and in vivo. Oncogene 1994;9:1799-805.
    • (1994) Oncogene , vol.9 , pp. 1799-1805
    • Miyashita, T.1    Harigai, M.2    Krajewska, M.3
  • 113
    • 0023237958 scopus 로고
    • Colon cancer, dysplasia, and surveillance in patients with ulcerative colitis
    • Collins RH Jr, Feldman M, Fordtran JS. Colon cancer, dysplasia, and surveillance in patients with ulcerative colitis. N Engl J Med 1983;316:1654-5.
    • (1983) N Engl J Med , vol.316 , pp. 1654-1655
    • Collins Jr., R.H.1    Feldman, M.2    Fordtran, J.S.3
  • 114
    • 0025083101 scopus 로고
    • Inflammation and cancer: Role of phagocyte-generated oxidants in carcinogenesis
    • Weitzman SA, Gordon LI. Inflammation and cancer: role of phagocyte-generated oxidants in carcinogenesis. Blood 1990; 76:655-63.
    • (1990) Blood , vol.76 , pp. 655-663
    • Weitzman, S.A.1    Gordon, L.I.2
  • 115
    • 0027074753 scopus 로고
    • Neutrophils, nitrogen oxides and inflammatory bowel disease
    • Grisham MB, Yamada T. Neutrophils, nitrogen oxides and inflammatory bowel disease. Ann NY Acad Sci 1992;664: 103-15.
    • (1992) Ann NY Acad Sci , vol.664 , pp. 103-115
    • Grisham, M.B.1    Yamada, T.2
  • 116
    • 0026754422 scopus 로고
    • Neutrophil-mediated nitrosamine formation: Role of nitric exide in rats
    • Grisham MB, Ware K, Yamada T. Neutrophil-mediated nitrosamine formation: role of nitric exide in rats. Gastroenterology 1992;103:1260-6.
    • (1992) Gastroenterology , vol.103 , pp. 1260-1266
    • Grisham, M.B.1    Ware, K.2    Yamada, T.3
  • 117
    • 4243961275 scopus 로고    scopus 로고
    • Expression of the apoptosis genes Bcl-2 and Bax during the time course of experimental colitis in the rat
    • Reinshagen M, Rohm H, Geerling I, Eysselein VE, Adler G. Expression of the apoptosis genes Bcl-2 and Bax during the time course of experimental colitis in the rat [Abstract]. Gastroenterology 1996;110:A1111.
    • (1996) Gastroenterology , vol.110
    • Reinshagen, M.1    Rohm, H.2    Geerling, I.3    Eysselein, V.E.4    Adler, G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.