{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,26]],"date-time":"2026-09-26T13:01:57Z","timestamp":1790427717181,"version":"4.1.0"},"reference-count":44,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2015,11,26]],"date-time":"2015-11-26T00:00:00Z","timestamp":1448496000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"name":"Scientific Research Unit of Hacettepe University","award":["010 01 101 004"],"award-info":[{"award-number":["010 01 101 004"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Allergy"],"published-print":{"date-parts":[[2016,2]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:sec><jats:title>Background<\/jats:title><jats:p>Indoleamine 2,3\u2010dioxygenase (<jats:styled-content style=\"fixed-case\">IDO<\/jats:styled-content>), which degrades tryptophan (Trp) to kynurenine (Kyn), has been demonstrated to contribute to modulation of allergic responses. However, the role of <jats:styled-content style=\"fixed-case\">IDO<\/jats:styled-content> in food allergy has not yet been elucidated.<\/jats:p><\/jats:sec><jats:sec><jats:title>Methods<\/jats:title><jats:p>Serum Trp and Kyn concentrations were analyzed by high\u2010pressure liquid chromatography. Expression of <jats:styled-content style=\"fixed-case\">IDO<\/jats:styled-content> gene was measured by real\u2010time <jats:styled-content style=\"fixed-case\">PCR<\/jats:styled-content>. The levels of interleukin (<jats:styled-content style=\"fixed-case\">IL<\/jats:styled-content>)\u20104, <jats:styled-content style=\"fixed-case\">IL<\/jats:styled-content>\u201010, and interferon (<jats:styled-content style=\"fixed-case\">IFN<\/jats:styled-content>)\u2010\u03b3 in cell culture supernatants were measured by <jats:styled-content style=\"fixed-case\">ELISA<\/jats:styled-content>.<\/jats:p><\/jats:sec><jats:sec><jats:title>Results<\/jats:title><jats:p>Kyn\/Trp (<jats:styled-content style=\"fixed-case\">IDO<\/jats:styled-content> activity) was significantly lower in subjects with food allergy (<jats:italic>n<\/jats:italic> = 100) than in aged\u2010matched healthy controls (<jats:italic>n<\/jats:italic> = 112) (<jats:italic>P<\/jats:italic> = 0.004). Kyn\/Trp was decreased from healthy through completely tolerant, partially tolerant, and reactive ones [<jats:styled-content style=\"fixed-case\">LN<\/jats:styled-content> transformation (mean \u00b1 <jats:styled-content style=\"fixed-case\">SEM<\/jats:styled-content>) healthy: 3.9 \u00b1 0.02 \u03bcM\/<jats:styled-content style=\"fixed-case\">mM<\/jats:styled-content>; completely tolerant: 3.83 \u00b1 0.04; partially tolerant: 3.8 \u00b1 0.06; reactive: 3.7 \u00b1 0.04] (<jats:italic>P<\/jats:italic> = 0.008). The frequency of genetic polymorphisms of <jats:styled-content style=\"fixed-case\">IDO<\/jats:styled-content> did not reveal a significant association with Trp, Kyn, and Kyn\/Trp in healthy and food\u2010allergic cases. Culture of <jats:styled-content style=\"fixed-case\">PBMC<\/jats:styled-content> experiments yielded that <jats:styled-content style=\"fixed-case\">IDO mRNA<\/jats:styled-content> expression was not different between tolerant and reactive groups. <jats:styled-content style=\"fixed-case\">IL<\/jats:styled-content>\u20104 synthesis when stimulated with casein increased significantly in subjects who are reactive and tolerant to foods (<jats:italic>P<\/jats:italic> = 0.042, <jats:italic>P<\/jats:italic> = 0.006, respectively). Increase in <jats:styled-content style=\"fixed-case\">IL<\/jats:styled-content>\u201010 synthesis was observed only in children tolerant to milk, but not in reactive ones. <jats:styled-content style=\"fixed-case\">IFN<\/jats:styled-content>\u2010\u03b3 synthesis, when stimulated with <jats:styled-content style=\"fixed-case\">IL<\/jats:styled-content>\u20102 and \u03b2\u2010lactoglobulin in cell culture, was significantly higher in subjects tolerant to milk than in the reactive ones (<jats:italic>P<\/jats:italic> = 0.005 and <jats:italic>P<\/jats:italic> = 0.029, respectively).<\/jats:p><\/jats:sec><jats:sec><jats:title>Conclusion<\/jats:title><jats:p>Our results imply the probability of involvement of <jats:styled-content style=\"fixed-case\">IDO<\/jats:styled-content> in development of tolerance process, and we presume that high <jats:styled-content style=\"fixed-case\">IDO<\/jats:styled-content> activity is associated with nonresponsiveness to food allergens despite allergen sensitization.<\/jats:p><\/jats:sec>","DOI":"10.1111\/all.12785","type":"journal-article","created":{"date-parts":[[2015,10,9]],"date-time":"2015-10-09T11:52:53Z","timestamp":1444391573000},"page":"258-266","source":"Crossref","is-referenced-by-count":31,"title":["Low indoleamine 2,3\u2010dioxygenase activity in persistent food allergy in children"],"prefix":"10.1111","volume":"71","author":[{"given":"B.","family":"Buyuktiryaki","sequence":"first","affiliation":[{"name":"Division of Pediatric Allergy Hacettepe University School of Medicine Ankara Turkey"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"U. 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