Expression of Matrix Metalloproteinases (MMPs) and Tissue Inhibitors of Metalloproteinases (TIMPs) in Healthy and Diseased Human Gingiva

Abstract

The present study showed that metalloproteinases, particularly MMP-2, MMP-9, MMP-1, and MMP-13, are involved in the gingival extracellular matrix degradation during periodontitis.

MMP-2, MMP-8 Expression in gingival tissue of Chronic Periodontitis associated to Type 2 Diabetes Mellitus

“…And expression of MMP-2 in periodontium is localized mainly in fibroblast and granulation tissue of periodontal connective tissue(CT). In human periodontium, MMP-2 affects integrity of basement membrane and attachment of junctional epithelium and elevated MMP-2 expression level in chronic periodontitis is already reported in several investigations [15][16][17][18][19][20] . These results suggest the involvement of MMP-2 in periodontal destruction.…”

“…MMPs, produced by both infiltrating and resident cells of the periodontium, play a role in physiologic and pathologic events. It is recognized that an imbalance between activated MMPs and their endogenous tissue inhibitors of metalloproteinases(TIMPs) leads to pathologic breakdown of the extracellular matrix during chronic periodontitis [14][15][16][17] .…”

“…8,13) MMP-8 is mainly a polymorphonuclear leukocyte-(PMN-) specific matrix metalloproteinase stored in specific granules of PMNs. 13,17) When neutrophils are recruited to a site of inflammation, they release large quantities of MMP-8 stored in specific granules, and the inflammatory response is sustained by recruitment of new cells rather than by the local synthesis of MMP-8. MMP -8 activity and release are regulated by factors such as cytokines(TNF-α or IL-1β) and various bacterial virulence factors that affect MMP-8 release by PMN degraulation following PMN infiltration to the site of inflammation.…”

Role of Signal-Regulated Changes in Microtubule Stability Dynamics through <i>α</i>-Tubulin Phosphorylation on Ser/Tyr in Modulation of Salivary Gland Matrix Metalloproteinase-9 (MMP-9) Secretion in Response to <i>Porphyromonas gingivalis</i> and Ghrelin

“…Since the elevated levels of MMP-9 are routinely detected in gingival tissue of patients with periodontitis, a chronic inflammatory disease that leads to progressive destruction of teeth-supporting tissue [1] [3] [6], the results of our findings point to factors affecting MT dynamics as a tempting target for therapeutic intervention in the secretory processes of MMP-9.…”

“…The oral mucosal responses to P. gingivalis and its key endotoxin, cell-wall lipopolysaccharide (LPS), are characterized by the disturbances in nitric oxide synthase and cyclooxygenase systems, up-regulation in EGFR and MAPK activation, and induction in the secretion of highly glycosylated endopeptidase, metalloproteinase-9 (MMP-9) [4] [5] [6] [7] [8]. Similarly, to other regulated secretory proteins, the processing of MMP-9 along the endoplasmic reticulum (ER), Golgi, and trans-Golgi network (TGN) remains under a strict control of factors that affect the membrane recruitment and activation of various coat and cargo proteins, including ADPribosylation factors (Arfs) and protein kinase D (PKD), [9] [10] [11] [12].…”