{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,30]],"date-time":"2026-10-30T16:09:04Z","timestamp":1793376544715,"version":"4.5.0"},"reference-count":51,"publisher":"Wiley","issue":"6","license":[{"start":{"date-parts":[[2014,10,21]],"date-time":"2014-10-21T00:00:00Z","timestamp":1413849600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/501100001870","name":"Foundation for Polish Science","doi-asserted-by":"crossref","award":["TEAM, DPS\/424-329\/10"],"award-info":[{"award-number":["TEAM, DPS\/424-329\/10"]}],"id":[{"id":"10.13039\/501100001870","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"crossref","award":["NIDCR, DE 022597"],"award-info":[{"award-number":["NIDCR, DE 022597"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"crossref"}]},{"name":"National Science Centre, Poland","award":["2012\/07\/B\/NZ6\/03524"],"award-info":[{"award-number":["2012\/07\/B\/NZ6\/03524"]}]},{"name":"National Science Centre, Poland","award":["2011\/01\/B\/NZ6\/00268"],"award-info":[{"award-number":["2011\/01\/B\/NZ6\/00268"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecular Oral Microbiology"],"published-print":{"date-parts":[[2014,12]]},"abstract":"<jats:title>Summary<\/jats:title>\n                  <jats:p>\n                    <jats:italic>Porphyromonas gingivalis<\/jats:italic>\n                    (\n                    <jats:italic>P. gingivalis<\/jats:italic>\n                    ) expres\u2010ses the enzyme peptidylarginine deiminase (\n                    <jats:styled-content style=\"fixed-case\">PPAD<\/jats:styled-content>\n                    ), which has a strong preference for C\u2010terminal arginines. Due to the combined activity of\n                    <jats:styled-content style=\"fixed-case\">PPAD<\/jats:styled-content>\n                    and Arg\u2010specific gingipains,\n                    <jats:italic>P.\u00a0gingivalis<\/jats:italic>\n                    on the cell surface is highly citrullinated. To investigate the contribution of\n                    <jats:styled-content style=\"fixed-case\">PPAD<\/jats:styled-content>\n                    to the interaction of\n                    <jats:italic>P.\u00a0gingivalis<\/jats:italic>\n                    with primary human gingival fibroblasts (\n                    <jats:styled-content style=\"fixed-case\">PHGF<\/jats:styled-content>\n                    ) and\n                    <jats:italic>P.\u00a0gingivalis<\/jats:italic>\n                    \u2010induced synthesis of prostaglandin E\n                    <jats:sub>2<\/jats:sub>\n                    (PGE\n                    <jats:sub>2<\/jats:sub>\n                    ),\n                    <jats:styled-content style=\"fixed-case\">PHGF<\/jats:styled-content>\n                    were infected with wild\u2010type\n                    <jats:italic>P.\u00a0gingivalis<\/jats:italic>\n                    ATCC 33277, an isogenic\n                    <jats:styled-content style=\"fixed-case\">PPAD<\/jats:styled-content>\n                    \u2010knockout strain (\u2206\n                    <jats:italic>ppad<\/jats:italic>\n                    ) or a mutated strain (C351A) expressing an inactive enzyme in which the catalytic cysteine has been mutated to alanine (PPAD\n                    <jats:sup>C351A<\/jats:sup>\n                    ). Cells were infected in medium containing the mutants alone or in medium supplemented with purified, active PPAD. PHGF infection was assessed by colony\u2010forming assay, microscopic analysis and flow cytometry. Expression of cyclo\u2010oxygenase 2 (COX\u20102) and microsomal PGE synthase\u20101 (\n                    <jats:styled-content style=\"fixed-case\">mPGES<\/jats:styled-content>\n                    \u20101), key factors in the prostaglandin synthesis pathway, was examined by quantitative reverse transcription polymerase chain reaction (qRT\u2010PCR), while PGE\n                    <jats:sub>2<\/jats:sub>\n                    synthesis was evaluated by enzyme immunoassay. PHGF were infected more efficiently by wild\u2010type\n                    <jats:italic>P.\u00a0gingivalis<\/jats:italic>\n                    than by the \u2206\n                    <jats:italic>ppad<\/jats:italic>\n                    strain, which correlated with strong induction of COX\u20102 and\n                    <jats:styled-content style=\"fixed-case\">mPGES<\/jats:styled-content>\n                    \u20101 expression by wild\u2010type\n                    <jats:italic>P.\u00a0gingivalis<\/jats:italic>\n                    , but not by the PPAD activity\u2010null mutant strains (\u0394\n                    <jats:italic>ppad<\/jats:italic>\n                    and C351A). The impaired ability of the \u0394\n                    <jats:italic>ppad<\/jats:italic>\n                    strain to adhere to and\/or invade PHGF and both \u0394\n                    <jats:italic>ppad<\/jats:italic>\n                    and C351A to stimulate the PGE\n                    <jats:sub>2<\/jats:sub>\n                    \u2010synthesis pathway was fully restored by the addition of purified PPAD. The latter effect was strongly inhibited by aspirin. Collectively, our results implicate PPAD activity, but not PPAD itself, as an important factor for gingival fibroblast infection and activation of PGE\n                    <jats:sub>2<\/jats:sub>\n                    synthesis, the latter of which may strongly contribute to bone resorption and eventual tooth loss.\n                  <\/jats:p>","DOI":"10.1111\/omi.12081","type":"journal-article","created":{"date-parts":[[2014,8,30]],"date-time":"2014-08-30T04:24:46Z","timestamp":1409372686000},"page":"321-332","source":"Crossref","is-referenced-by-count":43,"title":["Peptidylarginine deiminase from\n                    <i>Porphyromonas gingivalis<\/i>\n                    contributes to infection of gingival fibroblasts and induction of prostaglandin E\n                    <sub>2<\/sub>\n                    \u2010signaling pathway"],"prefix":"10.1111","volume":"29","author":[{"given":"K.","family":"Gawron","sequence":"first","affiliation":[{"name":"Microbiology Department Faculty of Biochemistry, Biophysics and Biotechnology Jagiellonian University Krak\u00f3w Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"G.","family":"Bereta","sequence":"additional","affiliation":[{"name":"Microbiology Department Faculty of Biochemistry, Biophysics and Biotechnology Jagiellonian University Krak\u00f3w Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Z.","family":"Nowakowska","sequence":"additional","affiliation":[{"name":"Microbiology Department Faculty of Biochemistry, Biophysics and Biotechnology Jagiellonian University Krak\u00f3w Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"K.","family":"\u0141azarz\u2013Bartyzel","sequence":"additional","affiliation":[{"name":"Department of Periodontology and Oral Medicine Medical College Institute of Dentistry Jagiellonian University Krak\u00f3w 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