Expression of extracellular matrix metalloproteinase inducer glycosylation and c aveolin‐1 in healthy and inflamed human gingiva

Background and Objective Glycosylated extracellular matrix metalloproteinase inducer ( EMMPRIN ) is specifically associated with c aveolin‐1 and influences its ability to induce matrix metalloproteinases ( MMP s) production. This study investigated EMMPRIN glycosylation and c aveolin‐1 expression in healthy and inflamed human gingival tissues, analyzed the relationship between EMMPRIN glycosylation and c aveolin‐1 expression, and assessed how this interaction influenced MMP ‐1 production. Material and Methods Gingival tissues were collected from 10 healthy subjects and 15 chronic periodontitis ( chronic periodontitis ) subjects. EMMPRIN , caveolin‐1 and MMP ‐1 expressions were analyzed by immunohistochemistry. EMMPRIN and c aveolin‐1 co‐localization was detected by immunofluorescence. EMMPRIN glycosylation, c aveolin‐1, active MMP ‐1 and pro MMP ‐1 expression was assessed by Western blot. Results EMMPRIN was expressed in gingival epithelial cells, inflammatory cells, endothelial and fibroblast‐like cells. Strong c aveolin‐1 immunoreactivity was detected in gingival epithelial and endothelial cells. Double immunofluorescence studies revealed EMMPRIN and c aveolin‐1 co‐localization in gingival epithelium, endothelial and fibroblast‐like cells. Compared with healthy subjects, the chronic periodontitis group had increased high‐glycoform EMMPRIN ( HG ‐ EMMPRIN ) and active MMP ‐1 expression ( p  < 0.05). Active MMP ‐1 and pro MMP ‐1 protein levels were positively correlated with HG ‐ EMMPRIN levels ( p  < 0.05). Conclusion EMMPRIN and c aveolin‐1 colocalize in periodontal tissues. The increased active MMP ‐1 and pro MMP ‐1 production may be associated with elevated HG ‐ EMMPRIN levels.