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The aim of this study is to reveal if the crosstalk between matriptase activators and intestinal epithelial monolayers can lead to perturbations in physiological redox regulation <jats:italic>in vitro<\/jats:italic>. <jats:italic>Methods.<\/jats:italic> The effects of suramin and sphingosine\u20101\u2010phosphate (S1P) were tested on viability of intestinal porcine epithelial IPEC\u2010J2 cells using MTS assay. Measurements of transepithelial electrical resistance (TER) were performed to determine changes in barrier integrity of cell monolayers. Amplex Red assay was used to monitor extracellular hydrogen peroxide production. Occludin distribution pattern was detected prior to and after matriptase activation using immunofluorescent staining technique. <jats:italic>Results.<\/jats:italic> TER reduction was observed in suramin\u2010treated IPEC\u2010J2 cell monolayers, which could be attributed to cell cytotoxic properties of 48\u2009hr 50\u2009<jats:italic>\u03bc<\/jats:italic>M suramin administration. In contrast, S1P treatment increased TER significantly and elevated occludin accumulation in tight junctions. It was also found that extracellular hydrogen peroxide levels were maintained in IPEC\u2010J2 cells exposed to matriptase activators. <jats:italic>Discussion.<\/jats:italic> S1P administration not accompanied by redox imbalance might be one of the key strategies in the improvement of barrier function and consequently in the therapy of intestinal inflammations.<\/jats:p>","DOI":"10.1155\/2016\/9674272","type":"journal-article","created":{"date-parts":[[2015,12,28]],"date-time":"2015-12-28T21:05:03Z","timestamp":1451336703000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":7,"title":["Reinforced Epithelial Barrier Integrity via Matriptase Induction with Sphingosine\u20101\u2010Phosphate Did Not Result in Disturbances in Physiological Redox Status"],"prefix":"10.1155","volume":"2016","author":[{"given":"E.","family":"P\u00e1szti-Gere","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"\u00c1.","family":"Jerzsele","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"P.","family":"Balla","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"G.","family":"Ujhelyi","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"A.","family":"Sz\u00e9k\u00e1cs","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2015,12,28]]},"reference":[{"key":"e_1_2_9_1_2","doi-asserted-by":"publisher","DOI":"10.1007\/s10616-011-9362-9"},{"key":"e_1_2_9_2_2","doi-asserted-by":"publisher","DOI":"10.1007\/s00418-005-0067-z"},{"key":"e_1_2_9_3_2","doi-asserted-by":"publisher","DOI":"10.1007\/s10753-011-9403-8"},{"key":"e_1_2_9_4_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.vetmic.2011.10.017"},{"key":"e_1_2_9_5_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.vetimm.2006.01.002"},{"key":"e_1_2_9_6_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.vetmic.2006.11.001"},{"key":"e_1_2_9_7_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.vetmic.2007.12.018"},{"key":"e_1_2_9_8_2","doi-asserted-by":"publisher","DOI":"10.1186\/1746-6148-8-245"},{"key":"e_1_2_9_9_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.ijfoodmicro.2010.03.026"},{"key":"e_1_2_9_10_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.0903923107"},{"key":"e_1_2_9_11_2","doi-asserted-by":"publisher","DOI":"10.3109\/14756366.2015.1060483"},{"key":"e_1_2_9_12_2","doi-asserted-by":"publisher","DOI":"10.1007\/s10753-014-9988-9"},{"key":"e_1_2_9_13_2","first-page":"183","article-title":"Matrix-degrading type II transmembrane serine protease matriptase: its role in cancer development and malignancy","volume":"2","author":"Lee M. 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