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Volumn 105, Issue , 2017, Pages 16-27

Polyamine- and NADPH-dependent generation of ROS during Helicobacter pylori infection: A blessing in disguise

Author keywords

Gastric cancer; Helicobacter pylori; NADPH oxidase; Polyamines; Reactive oxygen species

Indexed keywords

ARGINASE; ARGININE; BACTERIAL PROTEIN; CAGA PROTEIN; CATALASE; FLAVOPROTEIN; HYDROGEN PEROXIDE; ORNITHINE DECARBOXYLASE; OXIDOREDUCTASE; OXYGEN; PEROXIREDOXIN; POLYAMINE; PROTEIN DUOX2; PROTEIN MDAB; PROTEIN NAPA; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE (PHOSPHATE) DEHYDROGENASE (QUINONE); REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE 1; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE 2; SPERMIDINE; SPERMINE; SPERMINE OXIDASE; SUPEROXIDE DISMUTASE; UNCLASSIFIED DRUG; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

EID: 85008640889     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2016.09.024     Document Type: Review
Times cited : (53)

References (131)
  • 1
    • 42549096146 scopus 로고    scopus 로고
    • Does Helicobacter pylori protect against asthma and allergy?
    • [1] Blaser, M.J., Chen, Y., Reibman, J., Does Helicobacter pylori protect against asthma and allergy?. Gut 57 (2008), 561–567.
    • (2008) Gut , vol.57 , pp. 561-567
    • Blaser, M.J.1    Chen, Y.2    Reibman, J.3
  • 7
    • 84901390048 scopus 로고    scopus 로고
    • Helicobacter pylori eradication therapy to prevent gastric cancer in healthy asymptomatic infected individuals: systematic review and meta-analysis of randomised controlled trials
    • [7] Ford, A.C., Forman, D., Hunt, R.H., Yuan, Y., Moayyedi, P., Helicobacter pylori eradication therapy to prevent gastric cancer in healthy asymptomatic infected individuals: systematic review and meta-analysis of randomised controlled trials. BMJ, 348, 2014, g3174.
    • (2014) BMJ , vol.348 , pp. g3174
    • Ford, A.C.1    Forman, D.2    Hunt, R.H.3    Yuan, Y.4    Moayyedi, P.5
  • 8
    • 84859717291 scopus 로고    scopus 로고
    • c-Src and c-Abl kinases control hierarchic phosphorylation and function of the CagA effector protein in Western and East Asian Helicobacter pylori strains
    • [8] Mueller, D., Tegtmeyer, N., Brandt, S., Yamaoka, Y., De Poire, E., Sgouras, D., Wessler, S., Torres, J., Smolka, A., Backert, S., c-Src and c-Abl kinases control hierarchic phosphorylation and function of the CagA effector protein in Western and East Asian Helicobacter pylori strains. J. Clin. Investig. 122 (2012), 1553–1566.
    • (2012) J. Clin. Investig. , vol.122 , pp. 1553-1566
    • Mueller, D.1    Tegtmeyer, N.2    Brandt, S.3    Yamaoka, Y.4    De Poire, E.5    Sgouras, D.6    Wessler, S.7    Torres, J.8    Smolka, A.9    Backert, S.10
  • 9
    • 33646016600 scopus 로고    scopus 로고
    • Influence of EPIYA-repeat polymorphism on the phosphorylation-dependent biological activity of Helicobacter pylori CagA
    • [9] Naito, M., Yamazaki, T., Tsutsumi, R., Higashi, H., Onoe, K., Yamazaki, S., Azuma, T., Hatakeyama, M., Influence of EPIYA-repeat polymorphism on the phosphorylation-dependent biological activity of Helicobacter pylori CagA. Gastroenterology 130 (2006), 1181–1190.
    • (2006) Gastroenterology , vol.130 , pp. 1181-1190
    • Naito, M.1    Yamazaki, T.2    Tsutsumi, R.3    Higashi, H.4    Onoe, K.5    Yamazaki, S.6    Azuma, T.7    Hatakeyama, M.8
  • 10
    • 84857949710 scopus 로고    scopus 로고
    • J-Western forms of Helicobacter pylori cagA constitute a distinct phylogenetic group with a widespread geographic distribution
    • [10] Duncan, S.S., Valk, P.L., Shaffer, C.L., Bordenstein, S.R., Cover, T.L., J-Western forms of Helicobacter pylori cagA constitute a distinct phylogenetic group with a widespread geographic distribution. J. Bacteriol. 194 (2012), 1593–1604.
    • (2012) J. Bacteriol. , vol.194 , pp. 1593-1604
    • Duncan, S.S.1    Valk, P.L.2    Shaffer, C.L.3    Bordenstein, S.R.4    Cover, T.L.5
  • 12
    • 0032815340 scopus 로고    scopus 로고
    • Relationship between the cagA 3′ repeat region of Helicobacter pylori, gastric histology, and susceptibility to low pH
    • [12] Yamaoka, Y., El-Zimaity, H.M., Gutierrez, O., Figura, N., Kim, J.G., Kodama, T., Kashima, K., Graham, D.Y., Relationship between the cagA 3′ repeat region of Helicobacter pylori, gastric histology, and susceptibility to low pH. Gastroenterology 117 (1999), 342–349.
    • (1999) Gastroenterology , vol.117 , pp. 342-349
    • Yamaoka, Y.1    El-Zimaity, H.M.2    Gutierrez, O.3    Figura, N.4    Kim, J.G.5    Kodama, T.6    Kashima, K.7    Graham, D.Y.8
  • 13
    • 0037169076 scopus 로고    scopus 로고
    • SHP-2 tyrosine phosphatase as an intracellular target of Helicobacter pylori CagA protein
    • [13] Higashi, H., Tsutsumi, R., Muto, S., Sugiyama, T., Azuma, T., Asaka, M., Hatakeyama, M., SHP-2 tyrosine phosphatase as an intracellular target of Helicobacter pylori CagA protein. Science 295 (2002), 683–686.
    • (2002) Science , vol.295 , pp. 683-686
    • Higashi, H.1    Tsutsumi, R.2    Muto, S.3    Sugiyama, T.4    Azuma, T.5    Asaka, M.6    Hatakeyama, M.7
  • 14
    • 0035162820 scopus 로고    scopus 로고
    • Phosphorylation of tyrosine 972 of the Helicobacter pylori CagA protein is essential for induction of a scattering phenotype in gastric epithelial cells
    • [14] Backert, S., Moese, S., Selbach, M., Brinkmann, V., Meyer, T.F., Phosphorylation of tyrosine 972 of the Helicobacter pylori CagA protein is essential for induction of a scattering phenotype in gastric epithelial cells. Mol. Microbiol. 42 (2001), 631–644.
    • (2001) Mol. Microbiol. , vol.42 , pp. 631-644
    • Backert, S.1    Moese, S.2    Selbach, M.3    Brinkmann, V.4    Meyer, T.F.5
  • 16
    • 69249104165 scopus 로고    scopus 로고
    • Helicobacter pylori CagA causes mitotic impairment and induces chromosomal instability
    • [16] Umeda, M., Murata-Kamiya, N., Saito, Y., Ohba, Y., Takahashi, M., Hatakeyama, M., Helicobacter pylori CagA causes mitotic impairment and induces chromosomal instability. J. Biol. Chem. 284 (2009), 22166–22172.
    • (2009) J. Biol. Chem. , vol.284 , pp. 22166-22172
    • Umeda, M.1    Murata-Kamiya, N.2    Saito, Y.3    Ohba, Y.4    Takahashi, M.5    Hatakeyama, M.6
  • 19
    • 84871099648 scopus 로고    scopus 로고
    • Haem oxygenase-1 inhibits phosphorylation of the Helicobacter pylori oncoprotein CagA in gastric epithelial cells
    • [19] Gobert, A.P., Verriere, T., de Sablet, T., Peek, R.M. Jr., Chaturvedi, R., Wilson, K.T., Haem oxygenase-1 inhibits phosphorylation of the Helicobacter pylori oncoprotein CagA in gastric epithelial cells. Cell. Microbiol. 15 (2013), 145–156.
    • (2013) Cell. Microbiol. , vol.15 , pp. 145-156
    • Gobert, A.P.1    Verriere, T.2    de Sablet, T.3    Peek, R.M.4    Chaturvedi, R.5    Wilson, K.T.6
  • 20
    • 0029043658 scopus 로고
    • Infection with Helicobacter pylori strains possessing cagA is associated with an increased risk of developing adenocarcinoma of the stomach
    • [20] Blaser, M.J., Perez-Perez, G.I., Kleanthous, H., Cover, T.L., Peek, R.M., Chyou, P.H., Stemmermann, G.N., Nomura, A., Infection with Helicobacter pylori strains possessing cagA is associated with an increased risk of developing adenocarcinoma of the stomach. Cancer Res. 55 (1995), 2111–2115.
    • (1995) Cancer Res. , vol.55 , pp. 2111-2115
    • Blaser, M.J.1    Perez-Perez, G.I.2    Kleanthous, H.3    Cover, T.L.4    Peek, R.M.5    Chyou, P.H.6    Stemmermann, G.N.7    Nomura, A.8
  • 21
    • 0037087302 scopus 로고    scopus 로고
    • Cutting edge: vaca, a vacuolating cytotoxin of Helicobacter pylori, directly activates mast cells for migration and production of proinflammatory cytokines
    • [21] Supajatura, V., Ushio, H., Wada, A., Yahiro, K., Okumura, K., Ogawa, H., Hirayama, T., Ra, C., Cutting edge: vaca, a vacuolating cytotoxin of Helicobacter pylori, directly activates mast cells for migration and production of proinflammatory cytokines. J. Immunol. 168 (2002), 2603–2607.
    • (2002) J. Immunol. , vol.168 , pp. 2603-2607
    • Supajatura, V.1    Ushio, H.2    Wada, A.3    Yahiro, K.4    Okumura, K.5    Ogawa, H.6    Hirayama, T.7    Ra, C.8
  • 23
    • 0031032033 scopus 로고    scopus 로고
    • Clinical and pathological importance of heterogeneity in vacA, the vacuolating cytotoxin gene of Helicobacter pylori
    • [23] Atherton, J.C., Peek, R.M. Jr., Tham, K.T., Cover, T.L., Blaser, M.J., Clinical and pathological importance of heterogeneity in vacA, the vacuolating cytotoxin gene of Helicobacter pylori. Gastroenterology 112 (1997), 92–99.
    • (1997) Gastroenterology , vol.112 , pp. 92-99
    • Atherton, J.C.1    Peek, R.M.2    Tham, K.T.3    Cover, T.L.4    Blaser, M.J.5
  • 26
    • 0023690989 scopus 로고
    • A human model of gastric carcinogenesis
    • [26] Correa, P., A human model of gastric carcinogenesis. Cancer Res. 48 (1988), 3554–3560.
    • (1988) Cancer Res. , vol.48 , pp. 3554-3560
    • Correa, P.1
  • 28
    • 33646467053 scopus 로고    scopus 로고
    • Arginine transport via cationic amino acid transporter 2 plays a critical regulatory role in classical or alternative activation of macrophages
    • [28] Yeramian, A., Martin, L., Serrat, N., Arpa, L., Soler, C., Bertran, J., McLeod, C., Palacin, M., Modolell, M., Lloberas, J., Celada, A., Arginine transport via cationic amino acid transporter 2 plays a critical regulatory role in classical or alternative activation of macrophages. J. Immunol. 176 (2006), 5918–5924.
    • (2006) J. Immunol. , vol.176 , pp. 5918-5924
    • Yeramian, A.1    Martin, L.2    Serrat, N.3    Arpa, L.4    Soler, C.5    Bertran, J.6    McLeod, C.7    Palacin, M.8    Modolell, M.9    Lloberas, J.10    Celada, A.11
  • 32
    • 77951935192 scopus 로고    scopus 로고
    • Arginase II restricts host defense to Helicobacter pylori by attenuating inducible nitric oxide synthase translation in macrophages
    • [32] Lewis, N.D., Asim, M., Barry, D.P., Singh, K., de Sablet, T., Boucher, J.L., Gobert, A.P., Chaturvedi, R., Wilson, K.T., Arginase II restricts host defense to Helicobacter pylori by attenuating inducible nitric oxide synthase translation in macrophages. J. Immunol. 184 (2010), 2572–2582.
    • (2010) J. Immunol. , vol.184 , pp. 2572-2582
    • Lewis, N.D.1    Asim, M.2    Barry, D.P.3    Singh, K.4    de Sablet, T.5    Boucher, J.L.6    Gobert, A.P.7    Chaturvedi, R.8    Wilson, K.T.9
  • 34
    • 84963705390 scopus 로고    scopus 로고
    • Arginase 2 deletion leads to enhanced M1 macrophage activation and upregulated polyamine metabolism in response to Helicobacter pylori infection, Amino Acids,
    • [34] D.M. Hardbower, M. Asim, T. Murray-Stewart, R.A. Casero, Jr., T. Verriere, N.D. Lewis, R. Chaturvedi, M.B. Piazuelo, K.T. Wilson, Arginase 2 deletion leads to enhanced M1 macrophage activation and upregulated polyamine metabolism in response to Helicobacter pylori infection, Amino Acids, 2016.
    • (2016)
    • Hardbower, D.M.1    Asim, M.2    Murray-Stewart, T.3    Casero, R.A.4    Verriere Jr., T.5    Lewis, N.D.6    Chaturvedi, R.7    Piazuelo, M.B.8    Wilson, K.T.9
  • 35
    • 84963575145 scopus 로고    scopus 로고
    • The immune battle against Helicobacter pylori infection: no offense
    • [35] Gobert, A.P., Wilson, K.T., The immune battle against Helicobacter pylori infection: no offense. Trends Microbiol 24 (2016), 366–376.
    • (2016) Trends Microbiol , vol.24 , pp. 366-376
    • Gobert, A.P.1    Wilson, K.T.2
  • 36
    • 0037280476 scopus 로고    scopus 로고
    • Gene expression of ornithine decarboxylase, cyclooxygenase-2, and gastrin in atrophic gastric mucosa infected with Helicobacter pylori before and after eradication therapy
    • [36] Konturek, P.C., Rembiasz, K., Konturek, S.J., Stachura, J., Bielanski, W., Galuschka, K., Karcz, D., Hahn, E.G., Gene expression of ornithine decarboxylase, cyclooxygenase-2, and gastrin in atrophic gastric mucosa infected with Helicobacter pylori before and after eradication therapy. Dig. Dis. Sci. 48 (2003), 36–46.
    • (2003) Dig. Dis. Sci. , vol.48 , pp. 36-46
    • Konturek, P.C.1    Rembiasz, K.2    Konturek, S.J.3    Stachura, J.4    Bielanski, W.5    Galuschka, K.6    Karcz, D.7    Hahn, E.G.8
  • 37
    • 0029041981 scopus 로고
    • Ornithine decarboxylase as a marker for premalignancy in the stomach
    • [37] Patchett, S.E., Alstead, E.M., Butruk, L., Przytulski, K., Farthing, M.J., Ornithine decarboxylase as a marker for premalignancy in the stomach. Gut 37 (1995), 13–16.
    • (1995) Gut , vol.37 , pp. 13-16
    • Patchett, S.E.1    Alstead, E.M.2    Butruk, L.3    Przytulski, K.4    Farthing, M.J.5
  • 39
    • 0033588540 scopus 로고    scopus 로고
    • Tyrosine kinase and ornithine decarboxylase activation in children with Helicobacter pylori gastritis
    • [39] Elitsur, Y., Majumdar, A.P., Tureaud, J., Dosescu, J., Neace, C., Velusamy, L., Moshier, J.A., Tyrosine kinase and ornithine decarboxylase activation in children with Helicobacter pylori gastritis. Life Sci. 65 (1999), 1373–1380.
    • (1999) Life Sci. , vol.65 , pp. 1373-1380
    • Elitsur, Y.1    Majumdar, A.P.2    Tureaud, J.3    Dosescu, J.4    Neace, C.5    Velusamy, L.6    Moshier, J.A.7
  • 40
    • 0030476712 scopus 로고    scopus 로고
    • Ornithine decarboxylase activity is a marker of premalignancy in longstanding Helicobacter pylori infection
    • [40] Patchett, S.E., Katelaris, P.H., Zhang, Z.W., Alstead, E.M., Domizio, P., Farthing, M.J., Ornithine decarboxylase activity is a marker of premalignancy in longstanding Helicobacter pylori infection. Gut 39 (1996), 807–810.
    • (1996) Gut , vol.39 , pp. 807-810
    • Patchett, S.E.1    Katelaris, P.H.2    Zhang, Z.W.3    Alstead, E.M.4    Domizio, P.5    Farthing, M.J.6
  • 41
    • 0028236794 scopus 로고
    • Decrease in ornithine decarboxylase activity after eradication of Helicobacter pylori
    • [41] Alam, K., Arlow, F.L., Ma, C.K., Schubert, T.T., Decrease in ornithine decarboxylase activity after eradication of Helicobacter pylori. Am. J. Gastroenterol. 89 (1994), 888–893.
    • (1994) Am. J. Gastroenterol. , vol.89 , pp. 888-893
    • Alam, K.1    Arlow, F.L.2    Ma, C.K.3    Schubert, T.T.4
  • 42
    • 0033199366 scopus 로고    scopus 로고
    • Increase in apoptosis and decrease in ornithine decarboxylase activity of the gastric mucosa in patients with atrophic gastritis and gastric ulcer after successful eradication of Helicobacter pylori
    • [42] Hirasawa, R., Tatsuta, M., Iishi, H., Yano, H., Baba, M., Uedo, N., Sakai, N., Increase in apoptosis and decrease in ornithine decarboxylase activity of the gastric mucosa in patients with atrophic gastritis and gastric ulcer after successful eradication of Helicobacter pylori. Am. J. Gastroenterol. 94 (1999), 2398–2402.
    • (1999) Am. J. Gastroenterol. , vol.94 , pp. 2398-2402
    • Hirasawa, R.1    Tatsuta, M.2    Iishi, H.3    Yano, H.4    Baba, M.5    Uedo, N.6    Sakai, N.7
  • 43
    • 0029877611 scopus 로고    scopus 로고
    • Successful eradicating treatment of Helicobacter pylori in patients with chronic gastritis: gastric levels of cytokines, epidermal growth factor and polyamines before and after therapy
    • [43] Messa, C., Di Leo, A., Greco, B., Caradonna, L., Amati, L., Linsalata, M., Giorgio, I., Jirillo, E., Successful eradicating treatment of Helicobacter pylori in patients with chronic gastritis: gastric levels of cytokines, epidermal growth factor and polyamines before and after therapy. Immunopharmacol. Immunotoxicol. 18 (1996), 1–13.
    • (1996) Immunopharmacol. Immunotoxicol. , vol.18 , pp. 1-13
    • Messa, C.1    Di Leo, A.2    Greco, B.3    Caradonna, L.4    Amati, L.5    Linsalata, M.6    Giorgio, I.7    Jirillo, E.8
  • 44
    • 84860586512 scopus 로고    scopus 로고
    • Helicobacter pylori CagA induces ornithine decarboxylase upregulation via Src/MEK/ERK/c-Myc pathway: implication for progression of gastric diseases
    • [44] Xu, X., Liu, Z., Fang, M., Yu, H., Liang, X., Li, X., Liu, X., Chen, C., Jia, J., Helicobacter pylori CagA induces ornithine decarboxylase upregulation via Src/MEK/ERK/c-Myc pathway: implication for progression of gastric diseases. Exp. Biol. Med. 237 (2012), 435–441.
    • (2012) Exp. Biol. Med. , vol.237 , pp. 435-441
    • Xu, X.1    Liu, Z.2    Fang, M.3    Yu, H.4    Liang, X.5    Li, X.6    Liu, X.7    Chen, C.8    Jia, J.9
  • 45
    • 20444491996 scopus 로고    scopus 로고
    • Helicobacter pylori-induced macrophage apoptosis requires activation of ornithine decarboxylase by c-Myc
    • [45] Cheng, Y., Chaturvedi, R., Asim, M., Bussiere, F.I., Scholz, A., Xu, H., Casero, R.A. Jr., Wilson, K.T., Helicobacter pylori-induced macrophage apoptosis requires activation of ornithine decarboxylase by c-Myc. J. Biol. Chem. 280 (2005), 22492–22496.
    • (2005) J. Biol. Chem. , vol.280 , pp. 22492-22496
    • Cheng, Y.1    Chaturvedi, R.2    Asim, M.3    Bussiere, F.I.4    Scholz, A.5    Xu, H.6    Casero, R.A.7    Wilson, K.T.8
  • 46
    • 77953747962 scopus 로고    scopus 로고
    • Helicobacter pylori induces ERK-dependent formation of a phospho-c-Fos.c-Jun activator protein-1 complex that causes apoptosis in macrophages
    • [46] Asim, M., Chaturvedi, R., Hoge, S., Lewis, N.D., Singh, K., Barry, D.P., Algood, H.S., de Sablet, T., Gobert, A.P., Wilson, K.T., Helicobacter pylori induces ERK-dependent formation of a phospho-c-Fos.c-Jun activator protein-1 complex that causes apoptosis in macrophages. J. Biol. Chem. 285 (2010), 20343–20357.
    • (2010) J. Biol. Chem. , vol.285 , pp. 20343-20357
    • Asim, M.1    Chaturvedi, R.2    Hoge, S.3    Lewis, N.D.4    Singh, K.5    Barry, D.P.6    Algood, H.S.7    de Sablet, T.8    Gobert, A.P.9    Wilson, K.T.10
  • 47
    • 4544249197 scopus 로고    scopus 로고
    • Induction of polyamine oxidase 1 by Helicobacter pylori causes macrophage apoptosis by hydrogen peroxide release and mitochondrial membrane depolarization
    • [47] Chaturvedi, R., Cheng, Y., Asim, M., Bussiere, F.I., Xu, H., Gobert, A.P., Hacker, A., Casero, R.A. Jr., Wilson, K.T., Induction of polyamine oxidase 1 by Helicobacter pylori causes macrophage apoptosis by hydrogen peroxide release and mitochondrial membrane depolarization. J. Biol. Chem. 279 (2004), 40161–40173.
    • (2004) J. Biol. Chem. , vol.279 , pp. 40161-40173
    • Chaturvedi, R.1    Cheng, Y.2    Asim, M.3    Bussiere, F.I.4    Xu, H.5    Gobert, A.P.6    Hacker, A.7    Casero, R.A.8    Wilson, K.T.9
  • 48
    • 0035878846 scopus 로고    scopus 로고
    • Cloning and characterization of a human polyamine oxidase that is inducible by polyamine analogue exposure
    • [48] Wang, Y., Devereux, W., Woster, P.M., Stewart, T.M., Hacker, A., Casero, R.A. Jr., Cloning and characterization of a human polyamine oxidase that is inducible by polyamine analogue exposure. Cancer Res. 61 (2001), 5370–5373.
    • (2001) Cancer Res. , vol.61 , pp. 5370-5373
    • Wang, Y.1    Devereux, W.2    Woster, P.M.3    Stewart, T.M.4    Hacker, A.5    Casero, R.A.6
  • 52
    • 0038789165 scopus 로고    scopus 로고
    • Two novel proteins activate superoxide generation by the NADPH oxidase NOX1
    • [52] Banfi, B., Clark, R.A., Steger, K., Krause, K.H., Two novel proteins activate superoxide generation by the NADPH oxidase NOX1. J. Biol. Chem. 278 (2003), 3510–3513.
    • (2003) J. Biol. Chem. , vol.278 , pp. 3510-3513
    • Banfi, B.1    Clark, R.A.2    Steger, K.3    Krause, K.H.4
  • 53
    • 0033637971 scopus 로고    scopus 로고
    • Regulation of growth and apoptosis of cultured guinea pig gastric mucosal cells by mitogenic oxidase 1
    • [53] Teshima, S., Kutsumi, H., Kawahara, T., Kishi, K., Rokutan, K., Regulation of growth and apoptosis of cultured guinea pig gastric mucosal cells by mitogenic oxidase 1. Am. J. Physiol. Gastrointest. Liver Physiol. 279 (2000), G1169–G1176.
    • (2000) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.279 , pp. G1169-G1176
    • Teshima, S.1    Kutsumi, H.2    Kawahara, T.3    Kishi, K.4    Rokutan, K.5
  • 60
    • 84903982922 scopus 로고    scopus 로고
    • Helicobacter pylori protects oncogenically transformed cells from reactive oxygen species-mediated intercellular induction of apoptosis
    • [60] Bauer, G., Bereswill, S., Aichele, P., Glocker, E., Helicobacter pylori protects oncogenically transformed cells from reactive oxygen species-mediated intercellular induction of apoptosis. Carcinogenesis 35 (2014), 1582–1591.
    • (2014) Carcinogenesis , vol.35 , pp. 1582-1591
    • Bauer, G.1    Bereswill, S.2    Aichele, P.3    Glocker, E.4
  • 61
    • 0026452890 scopus 로고
    • Activation of human phagocyte oxidative metabolism by Helicobacter pylori
    • [61] Nielsen, H., Andersen, L.P., Activation of human phagocyte oxidative metabolism by Helicobacter pylori. Gastroenterology 103 (1992), 1747–1753.
    • (1992) Gastroenterology , vol.103 , pp. 1747-1753
    • Nielsen, H.1    Andersen, L.P.2
  • 62
    • 0028241385 scopus 로고
    • Neutrophil activation by Helicobacter pylori lipopolysaccharides
    • [62] Nielsen, H., Birkholz, S., Andersen, L.P., Moran, A.P., Neutrophil activation by Helicobacter pylori lipopolysaccharides. J. Infect. Dis. 170 (1994), 135–139.
    • (1994) J. Infect. Dis. , vol.170 , pp. 135-139
    • Nielsen, H.1    Birkholz, S.2    Andersen, L.P.3    Moran, A.P.4
  • 63
    • 14844355257 scopus 로고    scopus 로고
    • Helicobacter pylori disrupts NADPH oxidase targeting in human neutrophils to induce extracellular superoxide release
    • [63] Allen, L.A., Beecher, B.R., Lynch, J.T., Rohner, O.V., Wittine, L.M., Helicobacter pylori disrupts NADPH oxidase targeting in human neutrophils to induce extracellular superoxide release. J. Immunol. 174 (2005), 3658–3667.
    • (2005) J. Immunol. , vol.174 , pp. 3658-3667
    • Allen, L.A.1    Beecher, B.R.2    Lynch, J.T.3    Rohner, O.V.4    Wittine, L.M.5
  • 67
    • 33845511105 scopus 로고    scopus 로고
    • Dual Roles of Helicobacter pylori NapA in inducing and combating oxidative stress
    • [67] Wang, G., Hong, Y., Olczak, A., Maier, S.E., Maier, R.J., Dual Roles of Helicobacter pylori NapA in inducing and combating oxidative stress. Infect. Immun. 74 (2006), 6839–6846.
    • (2006) Infect. Immun. , vol.74 , pp. 6839-6846
    • Wang, G.1    Hong, Y.2    Olczak, A.3    Maier, S.E.4    Maier, R.J.5
  • 68
    • 0025865390 scopus 로고
    • Soluble surface proteins from Helicobacter pylori activate monocytes/macrophages by lipopolysaccharide-independent mechanism
    • [68] Mai, U.E., Perez-Perez, G.I., Wahl, L.M., Wahl, S.M., Blaser, M.J., Smith, P.D., Soluble surface proteins from Helicobacter pylori activate monocytes/macrophages by lipopolysaccharide-independent mechanism. J. Clin. Investig. 87 (1991), 894–900.
    • (1991) J. Clin. Investig. , vol.87 , pp. 894-900
    • Mai, U.E.1    Perez-Perez, G.I.2    Wahl, L.M.3    Wahl, S.M.4    Blaser, M.J.5    Smith, P.D.6
  • 69
    • 0034773504 scopus 로고    scopus 로고
    • A proinflammatory peptide from Helicobacter pylori activates monocytes to induce lymphocyte dysfunction and apoptosis
    • [69] Betten, A., Bylund, J., Christophe, T., Boulay, F., Romero, A., Hellstrand, K., Dahlgren, C., A proinflammatory peptide from Helicobacter pylori activates monocytes to induce lymphocyte dysfunction and apoptosis. J. Clin. Investig. 108 (2001), 1221–1228.
    • (2001) J. Clin. Investig. , vol.108 , pp. 1221-1228
    • Betten, A.1    Bylund, J.2    Christophe, T.3    Boulay, F.4    Romero, A.5    Hellstrand, K.6    Dahlgren, C.7
  • 70
    • 0021288211 scopus 로고
    • 2 in isolated porcine thyroid follicles
    • 2 in isolated porcine thyroid follicles. Endocrinology 115 (1984), 392–398.
    • (1984) Endocrinology , vol.115 , pp. 392-398
    • Bjorkman, U.1    Ekholm, R.2
  • 72
    • 41349117172 scopus 로고    scopus 로고
    • Helicobacter pylori induces an antimicrobial response in rhesus macaques in a cag pathogenicity island-dependent manner
    • [72] Hornsby, M.J., Huff, J.L., Kays, R.J., Canfield, D.R., Bevins, C.L., Solnick, J.V., Helicobacter pylori induces an antimicrobial response in rhesus macaques in a cag pathogenicity island-dependent manner. Gastroenterology 134 (2008), 1049–1057.
    • (2008) Gastroenterology , vol.134 , pp. 1049-1057
    • Hornsby, M.J.1    Huff, J.L.2    Kays, R.J.3    Canfield, D.R.4    Bevins, C.L.5    Solnick, J.V.6
  • 73
    • 84962660794 scopus 로고    scopus 로고
    • The gastric mucosa from patients infected with CagA+ or VacA+Helicobacter pylori has a lower level of dual oxidase-2 expression than uninfected or infected with CagA-/VacA- H. pylori
    • [73] Li, H., Zhou, Y., Zheng, Y., Guo, H., Gao, L., Chen, P., Feng, D., Wu, L., Yang, M., Qi, Y., Guo, H., Chang, Y., Chu, F.F., Gao, Q., The gastric mucosa from patients infected with CagA+ or VacA+Helicobacter pylori has a lower level of dual oxidase-2 expression than uninfected or infected with CagA-/VacA- H. pylori. Dig. Dis. Sci. 61 (2016), 2328–2337.
    • (2016) Dig. Dis. Sci. , vol.61 , pp. 2328-2337
    • Li, H.1    Zhou, Y.2    Zheng, Y.3    Guo, H.4    Gao, L.5    Chen, P.6    Feng, D.7    Wu, L.8    Yang, M.9    Qi, Y.10    Guo, H.11    Chang, Y.12    Chu, F.F.13    Gao, Q.14
  • 74
    • 0027366226 scopus 로고
    • Purification of Helicobacter pylori superoxide dismutase and cloning and sequencing of the gene
    • [74] Spiegelhalder, C., Gerstenecker, B., Kersten, A., Schiltz, E., Kist, M., Purification of Helicobacter pylori superoxide dismutase and cloning and sequencing of the gene. Infect. Immun. 61 (1993), 5315–5325.
    • (1993) Infect. Immun. , vol.61 , pp. 5315-5325
    • Spiegelhalder, C.1    Gerstenecker, B.2    Kersten, A.3    Schiltz, E.4    Kist, M.5
  • 75
    • 0028222501 scopus 로고
    • Genetic organization and enzymatic activity of a superoxide dismutase from the microaerophilic human pathogen, Helicobacter pylori
    • [75] Pesci, E.C., Pickett, C.L., Genetic organization and enzymatic activity of a superoxide dismutase from the microaerophilic human pathogen, Helicobacter pylori. Gene 143 (1994), 111–116.
    • (1994) Gene , vol.143 , pp. 111-116
    • Pesci, E.C.1    Pickett, C.L.2
  • 76
    • 0028032403 scopus 로고
    • Escherichia coli expresses a copper- and zinc-containing superoxide dismutase
    • [76] Benov, L.T., Fridovich, I., Escherichia coli expresses a copper- and zinc-containing superoxide dismutase. J. Biol. Chem. 269 (1994), 25310–25314.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25310-25314
    • Benov, L.T.1    Fridovich, I.2
  • 77
    • 0035001195 scopus 로고    scopus 로고
    • Superoxide dismutase-deficient mutants of Helicobacter pylori are hypersensitive to oxidative stress and defective in host colonization
    • [77] Seyler, R.W. Jr., Olson, J.W., Maier, R.J., Superoxide dismutase-deficient mutants of Helicobacter pylori are hypersensitive to oxidative stress and defective in host colonization. Infect. Immun. 69 (2001), 4034–4040.
    • (2001) Infect. Immun. , vol.69 , pp. 4034-4040
    • Seyler, R.W.1    Olson, J.W.2    Maier, R.J.3
  • 78
    • 27744563761 scopus 로고    scopus 로고
    • Oxidative stress defense mechanisms to counter iron-promoted DNA damage in Helicobacter pylori
    • [78] Wang, G., Conover, R.C., Olczak, A.A., Alamuri, P., Johnson, M.K., Maier, R.J., Oxidative stress defense mechanisms to counter iron-promoted DNA damage in Helicobacter pylori. Free Radic. Res. 39 (2005), 1183–1191.
    • (2005) Free Radic. Res. , vol.39 , pp. 1183-1191
    • Wang, G.1    Conover, R.C.2    Olczak, A.A.3    Alamuri, P.4    Johnson, M.K.5    Maier, R.J.6
  • 81
    • 0036952436 scopus 로고    scopus 로고
    • Resistance to hydrogen peroxide in Helicobacter pylori: role of catalase (KatA) and Fur, and functional analysis of a novel gene product designated ‘KatA-associated protein’, KapA (HP0874)
    • [81] Harris, A.G., Hinds, F.E., Beckhouse, A.G., Kolesnikow, T., Hazell, S.L., Resistance to hydrogen peroxide in Helicobacter pylori: role of catalase (KatA) and Fur, and functional analysis of a novel gene product designated ‘KatA-associated protein’, KapA (HP0874). Microbiology 148 (2002), 3813–3825.
    • (2002) Microbiology , vol.148 , pp. 3813-3825
    • Harris, A.G.1    Hinds, F.E.2    Beckhouse, A.G.3    Kolesnikow, T.4    Hazell, S.L.5
  • 82
    • 10644290115 scopus 로고    scopus 로고
    • Role of a bacterial organic hydroperoxide detoxification system in preventing catalase inactivation
    • [82] Wang, G., Conover, R.C., Benoit, S., Olczak, A.A., Olson, J.W., Johnson, M.K., Maier, R.J., Role of a bacterial organic hydroperoxide detoxification system in preventing catalase inactivation. J. Biol. Chem. 279 (2004), 51908–51914.
    • (2004) J. Biol. Chem. , vol.279 , pp. 51908-51914
    • Wang, G.1    Conover, R.C.2    Benoit, S.3    Olczak, A.A.4    Olson, J.W.5    Johnson, M.K.6    Maier, R.J.7
  • 83
    • 0346849868 scopus 로고    scopus 로고
    • Localisation of Helicobacter pylori catalase in both the periplasm and cytoplasm, and its dependence on the twin-arginine target protein, KapA, for activity
    • [83] Harris, A.G., Hazell, S.L., Localisation of Helicobacter pylori catalase in both the periplasm and cytoplasm, and its dependence on the twin-arginine target protein, KapA, for activity. FEMS Microbiol. Lett. 229 (2003), 283–289.
    • (2003) FEMS Microbiol. Lett. , vol.229 , pp. 283-289
    • Harris, A.G.1    Hazell, S.L.2
  • 84
    • 84903370967 scopus 로고    scopus 로고
    • Twin-arginine translocation system in Helicobacter pylori: tatc, but not TatB, is essential for viability
    • [84] Benoit, S.L., Maier, R.J., Twin-arginine translocation system in Helicobacter pylori: tatc, but not TatB, is essential for viability. MBio, 5, 2014, e01016-13.
    • (2014) MBio , vol.5 , pp. e01016-13
    • Benoit, S.L.1    Maier, R.J.2
  • 85
    • 0029809179 scopus 로고    scopus 로고
    • Cloning and genetic characterization of Helicobacter pylori catalase and construction of a catalase-deficient mutant strain
    • [85] Odenbreit, S., Wieland, B., Haas, R., Cloning and genetic characterization of Helicobacter pylori catalase and construction of a catalase-deficient mutant strain. J. Bacteriol. 178 (1996), 6960–6967.
    • (1996) J. Bacteriol. , vol.178 , pp. 6960-6967
    • Odenbreit, S.1    Wieland, B.2    Haas, R.3
  • 86
    • 0033820189 scopus 로고    scopus 로고
    • Helicobacter pylori induces but survives the extracellular release of oxygen radicals from professional phagocytes using its catalase activity
    • [86] Ramarao, N., Gray-Owen, S.D., Meyer, T.F., Helicobacter pylori induces but survives the extracellular release of oxygen radicals from professional phagocytes using its catalase activity. Mol. Microbiol. 38 (2000), 103–113.
    • (2000) Mol. Microbiol. , vol.38 , pp. 103-113
    • Ramarao, N.1    Gray-Owen, S.D.2    Meyer, T.F.3
  • 88
    • 0037258943 scopus 로고    scopus 로고
    • Role of the thioredoxin system and the thiol-peroxidases Tpx and Bcp in mediating resistance to oxidative and nitrosative stress in Helicobacter pylori
    • [88] Comtois, S.L., Gidley, M.D., Kelly, D.J., Role of the thioredoxin system and the thiol-peroxidases Tpx and Bcp in mediating resistance to oxidative and nitrosative stress in Helicobacter pylori. Microbiol 149 (2003), 121–129.
    • (2003) Microbiol , vol.149 , pp. 121-129
    • Comtois, S.L.1    Gidley, M.D.2    Kelly, D.J.3
  • 89
    • 0037220694 scopus 로고    scopus 로고
    • Association of Helicobacter pylori antioxidant activities with host colonization proficiency
    • [89] Olczak, A.A., Seyler, R.W. Jr., Olson, J.W., Maier, R.J., Association of Helicobacter pylori antioxidant activities with host colonization proficiency. Infect. Immun. 71 (2003), 580–583.
    • (2003) Infect. Immun. , vol.71 , pp. 580-583
    • Olczak, A.A.1    Seyler, R.W.2    Olson, J.W.3    Maier, R.J.4
  • 90
    • 33644559039 scopus 로고    scopus 로고
    • The antioxidant protein alkylhydroperoxide reductase of Helicobacter pylori switches from a peroxide reductase to a molecular chaperone function
    • [90] Chuang, M.H., Wu, M.S., Lo, W.L., Lin, J.T., Wong, C.H., Chiou, S.H., The antioxidant protein alkylhydroperoxide reductase of Helicobacter pylori switches from a peroxide reductase to a molecular chaperone function. Proc. Natl. Acad. Sci. USA 103 (2006), 2552–2557.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 2552-2557
    • Chuang, M.H.1    Wu, M.S.2    Lo, W.L.3    Lin, J.T.4    Wong, C.H.5    Chiou, S.H.6
  • 91
    • 11144328882 scopus 로고    scopus 로고
    • Contribution of the Helicobacter pylori thiol peroxidase bacterioferritin comigratory protein to oxidative stress resistance and host colonization
    • [91] Wang, G., Olczak, A.A., Walton, J.P., Maier, R.J., Contribution of the Helicobacter pylori thiol peroxidase bacterioferritin comigratory protein to oxidative stress resistance and host colonization. Infect. Immun. 73 (2005), 378–384.
    • (2005) Infect. Immun. , vol.73 , pp. 378-384
    • Wang, G.1    Olczak, A.A.2    Walton, J.P.3    Maier, R.J.4
  • 92
    • 84892366219 scopus 로고    scopus 로고
    • The thioredoxin antioxidant system
    • [92] Lu, J., Holmgren, A., The thioredoxin antioxidant system. Free Radic. Biol. Med. 66 (2014), 75–87.
    • (2014) Free Radic. Biol. Med. , vol.66 , pp. 75-87
    • Lu, J.1    Holmgren, A.2
  • 93
    • 84930986572 scopus 로고    scopus 로고
    • Comparative roles of the two Helicobacter pylori thioredoxins in preventing macromolecule damage
    • [93] Kuhns, L.G., Wang, G., Maier, R.J., Comparative roles of the two Helicobacter pylori thioredoxins in preventing macromolecule damage. Infect. Immun. 83 (2015), 2935–2943.
    • (2015) Infect. Immun. , vol.83 , pp. 2935-2943
    • Kuhns, L.G.1    Wang, G.2    Maier, R.J.3
  • 94
    • 0035108401 scopus 로고    scopus 로고
    • Essential thioredoxin-dependent peroxiredoxin system from Helicobacter pylori: genetic and kinetic characterization
    • [94] Baker, L.M., Raudonikiene, A., Hoffman, P.S., Poole, L.B., Essential thioredoxin-dependent peroxiredoxin system from Helicobacter pylori: genetic and kinetic characterization. J. Bacteriol. 183 (2001), 1961–1973.
    • (2001) J. Bacteriol. , vol.183 , pp. 1961-1973
    • Baker, L.M.1    Raudonikiene, A.2    Hoffman, P.S.3    Poole, L.B.4
  • 96
    • 0036271268 scopus 로고    scopus 로고
    • Oxidative-stress resistance mutants of Helicobacter pylori
    • [96] Olczak, A.A., Olson, J.W., Maier, R.J., Oxidative-stress resistance mutants of Helicobacter pylori. J. Bacteriol. 184 (2002), 3186–3193.
    • (2002) J. Bacteriol. , vol.184 , pp. 3186-3193
    • Olczak, A.A.1    Olson, J.W.2    Maier, R.J.3
  • 97
    • 0038434128 scopus 로고    scopus 로고
    • NapA protects Helicobacter pylori from oxidative stress damage, and its production is influenced by the ferric uptake regulator
    • [97] Cooksley, C., Jenks, P.J., Green, A., Cockayne, A., Logan, R.P., Hardie, K.R., NapA protects Helicobacter pylori from oxidative stress damage, and its production is influenced by the ferric uptake regulator. J. Med. Microbiol. 52 (2003), 461–469.
    • (2003) J. Med. Microbiol. , vol.52 , pp. 461-469
    • Cooksley, C.1    Jenks, P.J.2    Green, A.3    Cockayne, A.4    Logan, R.P.5    Hardie, K.R.6
  • 98
    • 27744530740 scopus 로고    scopus 로고
    • Up-expression of NapA and other oxidative stress proteins is a compensatory response to loss of major Helicobacter pylori stress resistance factors
    • [98] Olczak, A.A., Wang, G., Maier, R.J., Up-expression of NapA and other oxidative stress proteins is a compensatory response to loss of major Helicobacter pylori stress resistance factors. Free Radic. Res. 39 (2005), 1173–1182.
    • (2005) Free Radic. Res. , vol.39 , pp. 1173-1182
    • Olczak, A.A.1    Wang, G.2    Maier, R.J.3
  • 99
    • 1342344978 scopus 로고    scopus 로고
    • An NADPH quinone reductase of Helicobacter pylori plays an important role in oxidative stress resistance and host colonization
    • [99] Wang, G., Maier, R.J., An NADPH quinone reductase of Helicobacter pylori plays an important role in oxidative stress resistance and host colonization. Infect. Immun. 72 (2004), 1391–1396.
    • (2004) Infect. Immun. , vol.72 , pp. 1391-1396
    • Wang, G.1    Maier, R.J.2
  • 101
    • 33845674063 scopus 로고    scopus 로고
    • A paradigm for direct stress-induced mutation in prokaryotes
    • [101] Kang, J.M., Iovine, N.M., Blaser, M.J., A paradigm for direct stress-induced mutation in prokaryotes. FASEB J. 20 (2006), 2476–2485.
    • (2006) FASEB J. , vol.20 , pp. 2476-2485
    • Kang, J.M.1    Iovine, N.M.2    Blaser, M.J.3
  • 104
    • 0033380294 scopus 로고    scopus 로고
    • Analysis of the genetic diversity of Helicobacter pylori: the tale of two genomes
    • [104] Alm, R.A., Trust, T.J., Analysis of the genetic diversity of Helicobacter pylori: the tale of two genomes. J. Mol. Med. 77 (1999), 834–846.
    • (1999) J. Mol. Med. , vol.77 , pp. 834-846
    • Alm, R.A.1    Trust, T.J.2
  • 105
    • 0344406733 scopus 로고    scopus 로고
    • Pathogen DNA as target for host-generated oxidative stress: role for repair of bacterial DNA damage in Helicobacter pylori colonization
    • [105] O'Rourke, E.J., Chevalier, C., Pinto, A.V., Thiberge, J.M., Ielpi, L., Labigne, A., Radicella, J.P., Pathogen DNA as target for host-generated oxidative stress: role for repair of bacterial DNA damage in Helicobacter pylori colonization. Proc. Natl. Acad. Sci. USA 100 (2003), 2789–2794.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 2789-2794
    • O'Rourke, E.J.1    Chevalier, C.2    Pinto, A.V.3    Thiberge, J.M.4    Ielpi, L.5    Labigne, A.6    Radicella, J.P.7
  • 106
    • 0032543425 scopus 로고    scopus 로고
    • Antimutagenic role of base-excision repair enzymes upon free radical-induced DNA damage
    • [106] Laval, J., Jurado, J., Saparbaev, M., Sidorkina, O., Antimutagenic role of base-excision repair enzymes upon free radical-induced DNA damage. Mutat. Res. 402 (1998), 93–102.
    • (1998) Mutat. Res. , vol.402 , pp. 93-102
    • Laval, J.1    Jurado, J.2    Saparbaev, M.3    Sidorkina, O.4
  • 107
    • 26244452150 scopus 로고    scopus 로고
    • The Helicobacter pylori MutS protein confers protection from oxidative DNA damage
    • [107] Wang, G., Alamuri, P., Humayun, M.Z., Taylor, D.E., Maier, R.J., The Helicobacter pylori MutS protein confers protection from oxidative DNA damage. Mol. Microbiol. 58 (2005), 166–176.
    • (2005) Mol. Microbiol. , vol.58 , pp. 166-176
    • Wang, G.1    Alamuri, P.2    Humayun, M.Z.3    Taylor, D.E.4    Maier, R.J.5
  • 109
    • 79960286223 scopus 로고    scopus 로고
    • Signal transduction by reactive oxygen species
    • [109] Finkel, T., Signal transduction by reactive oxygen species. J. Cell Biol. 194 (2011), 7–15.
    • (2011) J. Cell Biol. , vol.194 , pp. 7-15
    • Finkel, T.1
  • 110
    • 84870999066 scopus 로고    scopus 로고
    • Reactive oxygen species-induced autophagic degradation of Helicobacter pylori CagA is specifically suppressed in cancer stem-like cells
    • [110] Tsugawa, H., Suzuki, H., Saya, H., Hatakeyama, M., Hirayama, T., Hirata, K., Nagano, O., Matsuzaki, J., Hibi, T., Reactive oxygen species-induced autophagic degradation of Helicobacter pylori CagA is specifically suppressed in cancer stem-like cells. Cell Host Microbe 12 (2012), 764–777.
    • (2012) Cell Host Microbe , vol.12 , pp. 764-777
    • Tsugawa, H.1    Suzuki, H.2    Saya, H.3    Hatakeyama, M.4    Hirayama, T.5    Hirata, K.6    Nagano, O.7    Matsuzaki, J.8    Hibi, T.9
  • 111
    • 84994884777 scopus 로고    scopus 로고
    • Helicobacter pylori induces Snail expression through ROS-mediated activation of Erk and inactivation of GSK-3beta in human gastric cancer cells, Mol. Carcinog.,
    • [111] H.K. Ngo, H.G. Lee, J.Y. Piao, X. Zhong, H.N. Lee, H.J. Han, W. Kim, D.H. Kim, Y.N. Cha, H.K. Na, Y.J. Surh, Helicobacter pylori induces Snail expression through ROS-mediated activation of Erk and inactivation of GSK-3beta in human gastric cancer cells, Mol. Carcinog., 2016.
    • (2016)
    • Ngo, H.K.1    Lee, H.G.2    Piao, J.Y.3    Zhong, X.4    Lee, H.N.5    Han, H.J.6    Kim, W.7    Kim, D.H.8    Cha, Y.N.9    Na, H.K.10    Surh, Y.J.11
  • 112
  • 113
    • 84907236500 scopus 로고    scopus 로고
    • alpha-Lipoic acid inhibits Helicobacter pylori-induced oncogene expression and hyperproliferation by suppressing the activation of NADPH oxidase in gastric epithelial cells
    • [113] Byun, E., Lim, J.W., Kim, J.M., Kim, H., alpha-Lipoic acid inhibits Helicobacter pylori-induced oncogene expression and hyperproliferation by suppressing the activation of NADPH oxidase in gastric epithelial cells. Mediat. Inflamm., 2014, 2014, 380830.
    • (2014) Mediat. Inflamm. , vol.2014 , pp. 380830
    • Byun, E.1    Lim, J.W.2    Kim, J.M.3    Kim, H.4
  • 114
    • 85027956600 scopus 로고    scopus 로고
    • Helicobacter pylori induces vascular endothelial growth factor production in gastric epithelial cells through hypoxia-inducible factor-1alpha-dependent pathway
    • [114] Kang, M.J., Song, E.J., Kim, B.Y., Kim, D.J., Park, J.H., Helicobacter pylori induces vascular endothelial growth factor production in gastric epithelial cells through hypoxia-inducible factor-1alpha-dependent pathway. Helicobacter 19 (2014), 476–483.
    • (2014) Helicobacter , vol.19 , pp. 476-483
    • Kang, M.J.1    Song, E.J.2    Kim, B.Y.3    Kim, D.J.4    Park, J.H.5
  • 116
    • 84930529440 scopus 로고    scopus 로고
    • Helicobacter pylori induces IL-1beta and IL-18 production in human monocytic cell line through activation of NLRP3 inflammasome via ROS signaling pathway
    • [116] Li, X., Liu, S., Luo, J., Liu, A., Tang, S., Liu, S., Yu, M., Zhang, Y., Helicobacter pylori induces IL-1beta and IL-18 production in human monocytic cell line through activation of NLRP3 inflammasome via ROS signaling pathway. Pathog. Dis., 73, 2015.
    • (2015) Pathog. Dis. , vol.73
    • Li, X.1    Liu, S.2    Luo, J.3    Liu, A.4    Tang, S.5    Liu, S.6    Yu, M.7    Zhang, Y.8
  • 117
    • 15944367779 scopus 로고    scopus 로고
    • NADPH oxidase involvement in the pathology of Helicobacter pylori infection
    • [117] Keenan, J.I., Peterson, R.A. 2nd, Hampton, M.B., NADPH oxidase involvement in the pathology of Helicobacter pylori infection. Free Radic. Biol. Med. 38 (2005), 1188–1196.
    • (2005) Free Radic. Biol. Med. , vol.38 , pp. 1188-1196
    • Keenan, J.I.1    Peterson, R.A.2    Hampton, M.B.3
  • 118
    • 0038583518 scopus 로고    scopus 로고
    • Severe inflammation and reduced bacteria load in murine Helicobacter infection caused by lack of phagocyte oxidase activity
    • [118] Blanchard, T.G., Yu, F., Hsieh, C.L., Redline, R.W., Severe inflammation and reduced bacteria load in murine Helicobacter infection caused by lack of phagocyte oxidase activity. J. Infect. Dis. 187 (2003), 1609–1615.
    • (2003) J. Infect. Dis. , vol.187 , pp. 1609-1615
    • Blanchard, T.G.1    Yu, F.2    Hsieh, C.L.3    Redline, R.W.4
  • 124
    • 51749087250 scopus 로고    scopus 로고
    • Oxidative stress by Helicobacter pylori causes apoptosis through mitochondrial pathway in gastric epithelial cells
    • [124] Calvino-Fernandez, M., Benito-Martinez, S., Parra-Cid, T., Oxidative stress by Helicobacter pylori causes apoptosis through mitochondrial pathway in gastric epithelial cells. Apoptosis 13 (2008), 1267–1280.
    • (2008) Apoptosis , vol.13 , pp. 1267-1280
    • Calvino-Fernandez, M.1    Benito-Martinez, S.2    Parra-Cid, T.3
  • 127
    • 22044443715 scopus 로고    scopus 로고
    • 2-induced phosphorylation of ERK1/2 and PKB requires tyrosine kinase activity of insulin receptor and c-Src
    • 2-induced phosphorylation of ERK1/2 and PKB requires tyrosine kinase activity of insulin receptor and c-Src. Antioxid. Redox Signal. 7 (2005), 1014–1020.
    • (2005) Antioxid. Redox Signal. , vol.7 , pp. 1014-1020
    • Mehdi, M.Z.1    Pandey, N.R.2    Pandey, S.K.3    Srivastava, A.K.4
  • 128
    • 84907525430 scopus 로고    scopus 로고
    • Helicobacter pylori infection activates Src homology-2 domain-containing phosphatase 2 to suppress IFN-gamma signaling
    • [128] Wang, Y.C., Chen, C.L., Sheu, B.S., Yang, Y.J., Tseng, P.C., Hsieh, C.Y., Lin, C.F., Helicobacter pylori infection activates Src homology-2 domain-containing phosphatase 2 to suppress IFN-gamma signaling. J. Immunol. 193 (2014), 4149–4158.
    • (2014) J. Immunol. , vol.193 , pp. 4149-4158
    • Wang, Y.C.1    Chen, C.L.2    Sheu, B.S.3    Yang, Y.J.4    Tseng, P.C.5    Hsieh, C.Y.6    Lin, C.F.7
  • 130
    • 0036184190 scopus 로고    scopus 로고
    • Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo
    • [130] Meng, T.C., Fukada, T., Tonks, N.K., Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo. Mol. Cell. 9 (2002), 387–399.
    • (2002) Mol. Cell. , vol.9 , pp. 387-399
    • Meng, T.C.1    Fukada, T.2    Tonks, N.K.3


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