Expression of extracellular matrix metalloproteinase inducer glycosylation and caveolin-1 in healthy and inflamed human gingiva.

BACKGROUND AND

OBJECTIVE

Glycosylated extracellular matrix metalloproteinase inducer (EMMPRIN) is specifically associated with caveolin-1 and influences its ability to induce matrix metalloproteinases (MMPs) production. This study investigated EMMPRIN glycosylation and caveolin-1 expression in healthy and inflamed human gingival tissues, analyzed the relationship between EMMPRIN glycosylation and caveolin-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 caveolin-1 co-localization was detected by immunofluorescence. EMMPRIN glycosylation, caveolin-1, active MMP-1 and proMMP-1 expression was assessed by Western blot.

RESULTS

EMMPRIN was expressed in gingival epithelial cells, inflammatory cells, endothelial and fibroblast-like cells. Strong caveolin-1 immunoreactivity was detected in gingival epithelial and endothelial cells. Double immunofluorescence studies revealed EMMPRIN and caveolin-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 proMMP-1 protein levels were positively correlated with HG-EMMPRIN levels (p < 0.05).

CONCLUSION

EMMPRIN and caveolin-1 colocalize in periodontal tissues. The increased active MMP-1 and proMMP-1 production may be associated with elevated HG-EMMPRIN levels.