{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T21:11:18Z","timestamp":1790889078566,"version":"4.1.0"},"reference-count":43,"publisher":"Portland Press Ltd.","issue":"4","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2011,8,1]]},"abstract":"<jats:p>There is increasing interest in oxidative stress being a potential aetiological factor and\/or a triggering factor in Crohn's disease, rather than a concomitant occurrence during the pathogenesis of the disease. Recent research has shown that the immune mononuclear cells of Crohn's disease patients are induced to produce hydrogen peroxide (H2O2). Similarly, the regulation of antioxidant enzymes during disease in these cells has been unravelled, showing that SOD (superoxide dismutase) activity and GPx (glutathione peroxidase) activity is increased during active disease and returns to normal in remission phases. However, catalase remains constantly inhibited which supports the idea that catalase is not a redox-sensitive enzyme, but a regulator of cellular processes. ROS (reactive oxygen species) can be produced under the stimulus of different cytokines such as TNF\u03b1 (tumour necrosis factor \u03b1). It has been shown in different experimental models that they are also able to regulate apoptosis and other cellular processes. The status of oxidative stress elements in Crohn's disease and their possible implications in regulating cellular processes are reviewed in the present paper.<\/jats:p>","DOI":"10.1042\/bst0391102","type":"journal-article","created":{"date-parts":[[2011,7,26]],"date-time":"2011-07-26T12:05:03Z","timestamp":1311681903000},"page":"1102-1106","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":107,"title":["Role of oxidative stress and antioxidant enzymes in Crohn's disease"],"prefix":"10.1042","volume":"39","author":[{"given":"Marisa","family":"Iborra","sequence":"first","affiliation":[{"name":"Gastroenterology Department, Hospital Universitari I Polit\u00e8cnic La Fe, Boulevard Sud, 46026 Valencia, Spain"},{"name":"CIBER de Enfermedades Hep\u00e1ticas y Digestivas (CIBEREHD), Hospital Universitari I Polit\u00e8cnic La Fe, Boulevard Sud, 46026 Valencia, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"In\u00e9s","family":"Moret","sequence":"additional","affiliation":[{"name":"Gastroenterology Department, Hospital Universitari I Polit\u00e8cnic La Fe, Boulevard Sud, 46026 Valencia, Spain"},{"name":"CIBER de Enfermedades Hep\u00e1ticas y Digestivas (CIBEREHD), Hospital Universitari I Polit\u00e8cnic La Fe, Boulevard Sud, 46026 Valencia, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Francisco","family":"Rausell","sequence":"additional","affiliation":[{"name":"Gastroenterology Department, Hospital Universitari I Polit\u00e8cnic La Fe, Boulevard Sud, 46026 Valencia, Spain"},{"name":"CIBER de Enfermedades Hep\u00e1ticas y Digestivas (CIBEREHD), Hospital Universitari I Polit\u00e8cnic La Fe, Boulevard Sud, 46026 Valencia, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Guillermo","family":"Bastida","sequence":"additional","affiliation":[{"name":"Gastroenterology Department, Hospital Universitari I Polit\u00e8cnic La Fe, Boulevard Sud, 46026 Valencia, Spain"},{"name":"CIBER de Enfermedades Hep\u00e1ticas y Digestivas (CIBEREHD), Hospital Universitari I Polit\u00e8cnic La Fe, Boulevard Sud, 46026 Valencia, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mariam","family":"Aguas","sequence":"additional","affiliation":[{"name":"Gastroenterology Department, Hospital Universitari I Polit\u00e8cnic La Fe, Boulevard Sud, 46026 Valencia, Spain"},{"name":"CIBER de Enfermedades Hep\u00e1ticas y Digestivas (CIBEREHD), Hospital Universitari I Polit\u00e8cnic La Fe, Boulevard Sud, 46026 Valencia, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Elena","family":"Cerrillo","sequence":"additional","affiliation":[{"name":"Gastroenterology Department, Hospital Universitari I Polit\u00e8cnic La Fe, Boulevard Sud, 46026 Valencia, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pilar","family":"Nos","sequence":"additional","affiliation":[{"name":"Gastroenterology Department, Hospital Universitari I Polit\u00e8cnic La Fe, Boulevard Sud, 46026 Valencia, Spain"},{"name":"CIBER de Enfermedades Hep\u00e1ticas y Digestivas (CIBEREHD), Hospital Universitari I Polit\u00e8cnic La Fe, Boulevard Sud, 46026 Valencia, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bel\u00e9n","family":"Beltr\u00e1n","sequence":"additional","affiliation":[{"name":"Gastroenterology Department, Hospital Universitari I Polit\u00e8cnic La Fe, Boulevard Sud, 46026 Valencia, Spain"},{"name":"CIBER de Enfermedades Hep\u00e1ticas y Digestivas (CIBEREHD), Hospital Universitari I Polit\u00e8cnic La Fe, Boulevard Sud, 46026 Valencia, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","published-online":{"date-parts":[[2011,7,20]]},"reference":[{"key":"2021111719405945900_B1","first-page":"527","article-title":"New insights into the pathogenesis of IBD: are they relevant for therapeutic options?","volume":"139","author":"Vavricka","year":"2009","journal-title":"Swiss Med. Wkly."},{"key":"2021111719405945900_B2","first-page":"1997","article-title":"Oxidative stress as a pathogenic factor in inflammatory bowel disease: radicals or ridiculous? Aliment. Pharmacol. Ther","volume":"16","author":"Kruidenier","year":"2002"},{"key":"2021111719405945900_B3","doi-asserted-by":"crossref","first-page":"859","DOI":"10.1016\/S0140-6736(94)92831-2","article-title":"Oxidants and free radicals in inflammatory bowel disease","volume":"344","author":"Grisham","year":"1994","journal-title":"Lancet"},{"key":"2021111719405945900_B4","volume-title":"Free Radicals in Biology and Medicine","author":"Halliwell","year":"1999","edition":"3rd edn"},{"key":"2021111719405945900_B5","doi-asserted-by":"crossref","first-page":"6104","DOI":"10.1038\/sj.onc.1203128","article-title":"Role of redox potential and reactive oxygen species in stress signalling","volume":"18","author":"Adler","year":"1999","journal-title":"Oncogene"},{"key":"2021111719405945900_B6","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1016\/S0006-2952(99)00298-1","article-title":"Redox regulation of signal transduction in mammalian cells","volume":"59","author":"Herrlich","year":"2000","journal-title":"Biochem. Pharmacol."},{"key":"2021111719405945900_B7","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1002\/path.1408","article-title":"Imbalanced secondary mucosal antioxidant response in inflammatory bowel disease","volume":"201","author":"Kruidenier","year":"2003","journal-title":"J. Pathol."},{"key":"2021111719405945900_B8","doi-asserted-by":"crossref","first-page":"1289","DOI":"10.1080\/003655201317097146","article-title":"Reduced plasma antioxidant concentrations and increased oxidative DNA damage in inflammatory bowel disease","volume":"36","author":"D\u00f3dorico","year":"2001","journal-title":"Scand. J. Gastroenterol."},{"key":"2021111719405945900_B9","doi-asserted-by":"crossref","first-page":"1433","DOI":"10.1023\/B:DDAS.0000042242.22898.d9","article-title":"Decreased total and corrected antioxidant capacity in patients with inflammatory bowel disease","volume":"49","author":"Koutroubakis","year":"2004","journal-title":"Dig. Dis. Sci."},{"key":"2021111719405945900_B10","doi-asserted-by":"crossref","first-page":"76","DOI":"10.1002\/ibd.21027","article-title":"Mitochondrial dysfunction, persistent oxidative damage and catalase inhibition in na\u00efve and treated Crohn's disease","volume":"16","author":"Beltr\u00e1n","year":"2010","journal-title":"Inflamm. Bowel Dis."},{"key":"2021111719405945900_B11","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1046\/j.1365-2249.1998.00528.x","article-title":"Catalase and \u03b1-enoase: two novel granulocyte autoantigens in inflammatory bowel disease (IBD)","volume":"112","author":"Roozendaal","year":"1998","journal-title":"Clin. Exp. Immunol."},{"key":"2021111719405945900_B12","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1111\/j.1365-2036.2006.03134.x","article-title":"Altering the natural history of Crohn's disease: evidence for and against current therapies","volume":"25","author":"Vermeire","year":"2006","journal-title":"Aliment. Pharmacol. Ther."},{"key":"2021111719405945900_B13","doi-asserted-by":"crossref","first-page":"557","DOI":"10.1016\/S0016-5085(99)70177-0","article-title":"Lamina propria T cells in Crohn's disease and other gastrointestinal inflammation show defective CD2 pathway-induced apoptosis","volume":"116","author":"Boirivant","year":"1999","journal-title":"Gastroenterology"},{"key":"2021111719405945900_B14","doi-asserted-by":"crossref","first-page":"913","DOI":"10.1136\/gut.32.8.913","article-title":"Serum concentrations of tumor necrosis factor \u03b1 in childhood chronic inflammatory bowel disease","volume":"32","author":"Murch","year":"1991","journal-title":"Gut"},{"key":"2021111719405945900_B15","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1016\/0140-6736(92)90999-J","article-title":"Tumor necrosis factor \u03b1 in stool as a marker of intestinal inflammation","volume":"339","author":"Braegger","year":"1992","journal-title":"Lancet"},{"key":"2021111719405945900_B16","doi-asserted-by":"crossref","first-page":"206","DOI":"10.1136\/gut.50.2.206","article-title":"Infliximab treatment induces apoptosis of lamina propria T lymphocytes in Crohn's disease","volume":"50","author":"Ten\u00a0Hove","year":"2002","journal-title":"Gut"},{"key":"2021111719405945900_B17","doi-asserted-by":"crossref","first-page":"1145","DOI":"10.1053\/gast.2001.28702","article-title":"Infliximab induces apoptosis in monocytes in patients with chronic active inflammatory bowel disease by using a caspase-dependent pathway","volume":"121","author":"Lugering","year":"2001","journal-title":"Gastroenterology"},{"key":"2021111719405945900_B18","doi-asserted-by":"crossref","first-page":"1423","DOI":"10.1083\/jcb.141.6.1423","article-title":"The regulation of reactive oxygen species production during programmed cell death","volume":"141","author":"Tan","year":"1998","journal-title":"J. Cell Biol."},{"key":"2021111719405945900_B19","doi-asserted-by":"crossref","first-page":"735","DOI":"10.1016\/S1074-7613(00)80072-2","article-title":"Reactive oxygen species regulate activation-induced T cell apoptosis","volume":"10","author":"Hildeman","year":"1999","journal-title":"Immunity"},{"key":"2021111719405945900_B20","first-page":"2656","article-title":"Antiproliferative and antiapoptotic effects of cRel may occur within the same cells via the up-regulation of manganese superoxide dismutase","volume":"61","author":"Bernard","year":"2001","journal-title":"Cancer Res."},{"key":"2021111719405945900_B21","doi-asserted-by":"crossref","first-page":"747","DOI":"10.1081\/DMR-200033488","article-title":"Antioxidants enzymes and apoptosis","volume":"36","author":"Kahl","year":"2004","journal-title":"Drug Metab. Rev."},{"key":"2021111719405945900_B22","doi-asserted-by":"crossref","first-page":"687","DOI":"10.1523\/JNEUROSCI.18-02-00687.1998","article-title":"Mitochondrial manganese superoxide dismutase prevents neural apoptosis and reduces ischemic brain injury: suppression of peroxynitrite production, lipid peroxidation, and mitochondrial dysfunction","volume":"18","author":"Keller","year":"1998","journal-title":"J. Neurosci."},{"key":"2021111719405945900_B23","doi-asserted-by":"crossref","first-page":"29626","DOI":"10.1074\/jbc.M208665200","article-title":"Resistance to tumor necrosis factor-\u03b1 (TNF-\u03b1)-induced apoptosis in rat hepatoma cells expressing TNF-\u03b1 is linked to low antioxidant enzyme expression","volume":"278","author":"Chovolou","year":"2003","journal-title":"J. Biol. Chem."},{"key":"2021111719405945900_B24","first-page":"5885","article-title":"Regulation of the catalase gene promoter by Sp1, CCAAT-recognizing factors, and a WT1\/Egr-related factor in hydrogen peroxide-resistant HP100 cells","volume":"61","author":"Nenoi","year":"2001","journal-title":"Cancer Res."},{"key":"2021111719405945900_B25","doi-asserted-by":"crossref","first-page":"297","DOI":"10.1172\/JCI116959","article-title":"Vulnerability of the human airway epithelium to hyperoxia: constitutive expression of the catalase gene in human bronchial epithelial cells despite oxidant stress","volume":"93","author":"Yoo","year":"1994","journal-title":"J. Clin. Invest."},{"key":"2021111719405945900_B26","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1016\/j.yjmcc.2003.10.011","article-title":"Adenovirus-mediated overexpression of catalase attenuates oxLDL-induced apoptosis in human aortic endothelial cells via AP-1 and c-Jun N-terminal kinase\/extracellular signal-regulated kinase mitogen-activated protein kinase pathways","volume":"36","author":"Lin","year":"2004","journal-title":"J. Mol. Cell. Cardiol."},{"key":"2021111719405945900_B27","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1054\/plef.2001.0332","article-title":"Signaling and proapoptotic functions of transformed cell-derived reactive oxygen species. Prostaglandins Leukotrienes Essent","volume":"66","author":"Bauer","year":"2002","journal-title":"Fatty Acids"},{"key":"2021111719405945900_B28","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1016\/S0014-5793(00)01669-0","article-title":"Redox-dependent signal transduction","volume":"476","author":"Finkel","year":"2000","journal-title":"FEBS Lett."},{"key":"2021111719405945900_B29","doi-asserted-by":"crossref","first-page":"114","DOI":"10.1016\/S0014-5793(01)02593-5","article-title":"Caspases are reversibly inactivated by hydrogen peroxide","volume":"500","author":"Borutaite","year":"2001","journal-title":"FEBS Lett."},{"key":"2021111719405945900_B30","doi-asserted-by":"crossref","first-page":"111S","DOI":"10.1111\/acer.1998.22.s3_part1.111s","article-title":"Oxidative stress and mitochondrial damage precedes gastric mucosal cell death induced by ethanol administration","volume":"22","author":"Hirokawa","year":"1998","journal-title":"Alcohol. Clin. Exp. Res."},{"key":"2021111719405945900_B31","doi-asserted-by":"crossref","first-page":"943","DOI":"10.1016\/S0891-5849(01)00668-2","article-title":"cRel induces mitochondrial alterations in correlation with proliferation arrest","volume":"31","author":"Bernard","year":"2001","journal-title":"Free Radical Biol. Med."},{"key":"2021111719405945900_B32","first-page":"3990","article-title":"Tumor necrosis factor\/cachectin decreases catalase activity of rat liver","volume":"51","author":"Yasmineh","year":"1991","journal-title":"Cancer Res."},{"key":"2021111719405945900_B33","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1016\/S0014-5793(97)00805-3","article-title":"TNF-\u03b1 downregulates the peroxisome proliferator activated receptor-\u03b1 and the mRNAs encoding peroxisomal proteins in rat liver","volume":"412","author":"Beier","year":"1997","journal-title":"FEBS Lett."},{"key":"2021111719405945900_B34","doi-asserted-by":"crossref","first-page":"2853","DOI":"10.1016\/S0021-9258(19)50660-3","article-title":"Oxidation\u2013reduction-sensitive binding of lung protein to rat catalase mRNA","volume":"267","author":"Clerch","year":"1992","journal-title":"J. Biol. Chem."},{"key":"2021111719405945900_B35","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1023\/A:1020680131754","article-title":"Regulation of catalase enzyme activity by cell signaling molecules","volume":"240","author":"Yano","year":"2002","journal-title":"Mol. Cell. Biochem."},{"key":"2021111719405945900_B36","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1007\/BF03260057","article-title":"Catalase enzyme mutations and their association with diseases","volume":"8","author":"Goth","year":"2004","journal-title":"Mol. Diagn."},{"key":"2021111719405945900_B37","first-page":"863","article-title":"Nucleotide substitution C1167T in the catalase gene and position of nearby polymorphic markers DS11S907 and D11S2008 are connected with development of diabetes mellitus type 2","volume":"34","author":"Chistiakov","year":"2000","journal-title":"Mol. Biol. (Moscow)"},{"key":"2021111719405945900_B38","doi-asserted-by":"crossref","first-page":"62","DOI":"10.1034\/j.1600-0749.2002.00057.x","article-title":"Genetic association of the catalase gene (CAT) with vitiligo susceptibility","volume":"15","author":"Casp","year":"2002","journal-title":"Pigment Cell Res."},{"key":"2021111719405945900_B39","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1007\/s004390100553","article-title":"A polymorphism in the promoter region of catalase is associated with blood pressure levels","volume":"109","author":"Jiang","year":"2001","journal-title":"Hum. Genet."},{"key":"2021111719405945900_B40","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1093\/clinchem\/42.2.341","article-title":"Hypocatalasemia in hospital patients","volume":"42","author":"Goth","year":"1996","journal-title":"Clin. Chem."},{"key":"2021111719405945900_B41","doi-asserted-by":"crossref","first-page":"1243","DOI":"10.1016\/j.freeradbiomed.2008.07.017","article-title":"Telomerase deficiency promotes oxidative stress by reducing catalase activity","volume":"45","author":"P\u00e9rez-Rivero","year":"2008","journal-title":"Free Radical Biol. Med."},{"key":"2021111719405945900_B42","doi-asserted-by":"crossref","first-page":"1187","DOI":"10.1203\/00006450-198511000-00015","article-title":"Congenital acatalasemia: a study of neutrophil functions after provocation with hydrogen peroxide","volume":"19","author":"Matsunaga","year":"1985","journal-title":"Pediatr. Res."},{"key":"2021111719405945900_B43","first-page":"345","article-title":"Mammalian acatalasemia: the perspectives of bioinformatics and genetic toxicology","volume":"62","author":"Ogata","year":"2008","journal-title":"Acta Med. Okayama"}],"container-title":["Biochemical Society Transactions"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemsoctrans\/article-pdf\/39\/4\/1102\/548342\/bst0391102.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemsoctrans\/article-pdf\/39\/4\/1102\/548342\/bst0391102.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,4,9]],"date-time":"2024-04-09T03:06:56Z","timestamp":1712632016000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemsoctrans\/article\/39\/4\/1102\/65161\/Role-of-oxidative-stress-and-antioxidant-enzymes"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2011,7,20]]},"references-count":43,"journal-issue":{"issue":"4","published-online":{"date-parts":[[2011,7,20]]},"published-print":{"date-parts":[[2011,8,1]]}},"URL":"https:\/\/doi.org\/10.1042\/bst0391102","relation":{},"ISSN":["0300-5127","1470-8752"],"issn-type":[{"value":"0300-5127","type":"print"},{"value":"1470-8752","type":"electronic"}],"subject":[],"published":{"date-parts":[[2011,7,20]]}}}