{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,14]],"date-time":"2026-07-14T18:19:50Z","timestamp":1784053190309,"version":"3.55.0"},"reference-count":34,"publisher":"Wiley","issue":"3","license":[{"start":{"date-parts":[[2018,1,5]],"date-time":"2018-01-05T00:00:00Z","timestamp":1515110400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["81371146"],"award-info":[{"award-number":["81371146"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["81670995"],"award-info":[{"award-number":["81670995"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["J of Periodontal Research"],"published-print":{"date-parts":[[2018,6]]},"abstract":"<jats:sec><jats:title>Background and Objective<\/jats:title><jats:p>Extracellular matrix metalloproteinase inducer (EMMPRIN) is a transmembrane glycoprotein that may induce activation of matrix metalloproteinases (MMPs) and lead to the destruction of periodontal tissue. The level of EMMPRIN glycosylation might be involved in this process. This study aims to investigate the role of EMMPRIN glycosylation in regulating MMP\u20102 and MMP\u20109 during the progression of periodontitis.<\/jats:p><\/jats:sec><jats:sec><jats:title>Material and Methods<\/jats:title><jats:p>Gingival tissues were collected from patients with chronic periodontitis and from patients undergoing crown\u2010lengthening procedures (healthy gingival tissue). Tissues were used for immunohistochemistry and double immunofluorescence. A human immortalized oral epithelial cell (HIOEC) line was stably transfected by an <jats:italic>N<\/jats:italic>\u2010acetylglucosaminyltransferase\u2010V (GnT\u2010V) RNA interference (RNAi) lentivirus to suppress EMMPRIN glycosylation. Gene silence efficiency was detected by western blot, quantitative real\u2010time PCR and immunofluorescence (IF) staining. An HIOEC\/human gingival fibroblast (HGF) co\u2010culture model and an individual culture model were used in this study. After exposure of cells to <jats:italic>Porphyromonas gingivalis<\/jats:italic> lipopolysaccharide (<jats:italic>Pg<\/jats:italic>. LPS), the expression of EMMPRIN, MMP\u20102 and MMP\u20109 were assessed by western blot, quantitative real\u2010time PCR and IF, and the secretion of MMP\u20102 and MMP\u20109 were detected by gelatin\u2010degradation assays.<\/jats:p><\/jats:sec><jats:sec><jats:title>Results<\/jats:title><jats:p>Compared with the periodontally healthy group, patients with periodontitis showed increased expression of EMMPRIN on the gingival epithelial cell membrane. GnT\u2010V, a key regulator of EMMPRIN glycosylation, was co\u2010expressed with EMMPRIN in gingival epithelial cells in patients with periodontitis. Knockdown of GnT\u2010V reduced the level of EMMPRIN glycosylation in HIOECs. Furthermore, in the HIOEC\/HGF co\u2010culture model, stimulation with <jats:italic>Pg<\/jats:italic>. LPS (10\u00a0\u03bcg\/mL, 4\u00a0hours) promoted EMMPRIN glycosylation and increased the activities of MMP\u20102 and MMP\u20109, while suppression of EMMPRIN glycosylation by GnT\u2010V knockdown reduced the synthesis and activities of MMP\u20102 and MMP\u20109 under <jats:italic>Pg<\/jats:italic>. LPS stimulation. Moreover, the gelatin\u2010degradation assay showed that inhibition of EMMPRIN glycosylation suppressed the <jats:italic>Pg<\/jats:italic>. LPS\u2010induced degradation of gelatin in the co\u2010culture model.<\/jats:p><\/jats:sec><jats:sec><jats:title>Conclusion<\/jats:title><jats:p>We conclude that EMMPRIN glycosylation participates in the regulation of MMP\u20102 and MMP\u20109 production through mediating the interaction of HIOECs and HGFs. Inhibiting EMMPRIN glycosylation can reduce the activation of MMP\u20102 and MMP\u20109 and suppress the degradation of extracellular matrix (ECM) in the HIOEC\/HGF co\u2010culture model. Therefore, this study suggests that EMMPRIN glycosylation may affect the host immune\u2010inflammatory response by regulating MMPs in periodontitis.<\/jats:p><\/jats:sec>","DOI":"10.1111\/jre.12524","type":"journal-article","created":{"date-parts":[[2018,1,10]],"date-time":"2018-01-10T02:45:22Z","timestamp":1515552322000},"page":"391-402","source":"Crossref","is-referenced-by-count":24,"title":["The role of extracellular matrix metalloproteinase inducer glycosylation in regulating matrix metalloproteinases in periodontitis"],"prefix":"10.1111","volume":"53","author":[{"given":"Z.","family":"Zhang","sequence":"first","affiliation":[{"name":"The State Key Laboratory Breeding Base of Basic Science of Stomatology (Hubei\u2010MOST) &amp; Key Laboratory of Oral Biomedicine Ministry of Education, School and Hospital of Stomatology Wuhan University  Wuhan Hubei 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