Increased expression of extracellular matrix metalloproteinase inducer is associated with matrix metalloproteinase-1 and -2 in gingival tissues from patients with periodontitis.

Abstract

BACKGROUND AND OBJECTIVE:

Extracellular matrix metalloproteinase inducer (EMMPRIN), an immunoglobulin-like cell surface glycoprotein, could promote collagenolytic balance in favor of the expression and activation of matrix metalloproteinases (MMPs). This study was to investigate the expression of EMMPRIN in gingival tissues from different periodontal conditions and to correlate it with the production of MMP-1 and MMP-2.

MATERIAL AND METHODS:

Gingival biopsies were collected from 15 patients with untreated advanced chronic periodontitis and 15 patients with aggressive periodontitis (AgP). The control group consisted of 12 subjects diagnosed either as periodontally healthy individuals or as individuals with a gingival index of one (H/G1). The peptides and mRNA of EMMPRIN, MMP-1 and MMP-2 were detected by immunohistochemistry and semi-quantitative reverse transcriptase-polymerase chain reaction, respectively.

RESULTS:

The expression of EMMPRIN, MMP-1 and MMP-2 peptides in periodontally healthy tissues was mainly confined to the gingival epithelium. The EMMPRIN was strongly expressed in the cell membrane of the basal layer. Immunoreactivity for EMMPRIN was more intensive and more widespread in periodontitis, extended from the epithelial layers to the underlying connective tissues, and was essential in both inflammatory and fibroblast-like cells. In addition, MMP-1 and MMP-2 showed the same localized expression. The chronic periodontitis group had a significantly higher mRNA expression of EMMPRIN and MMP-2 compared with the H/G1 subjects (p < 0.05). Production of MMP-1 and MMP-2 by gingival tissues was correlated with the mRNA level of EMMPRIN (r = 0.463, p = 0.013 for MMP-1 and r = 0.404, p = 0.033 for MMP-2).

CONCLUSION:

The expression of EMMPRIN in human normal and diseased gingiva might contribute to periodontal physiological and pathological processes; moreover, its increased production might be associated with MMP-1 and MMP-2 expression.

• Authors: W Dong, J Xiang, C Li, Z Cao, Z Huang
• Journal: Journal of periodontal research (J Periodontal Res) Vol. 44 Issue 1 Pg. 125-32 (Feb 2009) ISSN: 1600-0765 [Electronic] United States
• PMID: 19515022 (Publication Type: Comparative Study, Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• BSG protein, human
• Basigin
• MMP2 protein, human
• Matrix Metalloproteinase 2
• MMP1 protein, human
• Matrix Metalloproteinase 1

Topics

• Adolescent
• Adult
• Aggressive Periodontitis (enzymology, pathology)
• Basigin (analysis)
• Biopsy
• Cell Membrane (enzymology, ultrastructure)
• Child
• Chronic Periodontitis (enzymology, pathology)
• Connective Tissue (enzymology, pathology)
• Dental Plaque Index
• Epithelial Cells (enzymology, ultrastructure)
• Epithelium (enzymology, pathology)
• Fibroblasts (enzymology, pathology)
• Gingiva (enzymology, pathology)
• Gingival Hemorrhage (enzymology, pathology)
• Humans
• Matrix Metalloproteinase 1 (analysis)
• Matrix Metalloproteinase 2 (analysis)
• Middle Aged
• Periodontal Index
• Periodontal Pocket (enzymology, pathology)
• Periodontitis (enzymology, pathology)
• Young Adult