Induction of MMP-2 at the interface between epithelial cells and fibroblasts from human periodontal ligament

Shimonishi, Mitsuru; Takahashi, Ichiro; Terao, Fumie; Komatsu, Masashi; Kikuchi, Masahiko

doi:10.1111/j.1600-0765.2009.01237.x

Cited by 5 publications

(6 citation statements)

References 37 publications

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“…MMPs are a class of proteolytic enzymes that function to cleave and degrade collagens and other ECM proteins. PDL fibroblasts express several members of this protease family, including MMP1, MMP2, MMP3, MMP8, and MMP9 40‐43 . Several MMPs are upregulated during the inflammation‐driven tissue destruction of periodontal disease, including MMP1, MMP2, MMP8, and MMP9 44,45 .…”

Section: Discussionmentioning

confidence: 99%

“…PDL fibroblasts express several members of this protease family, including MMP1, MMP2, MMP3, MMP8, and MMP9. [40][41][42][43] Several MMPs are upregulated during the inflammation-driven tissue destruction of periodontal disease, including MMP1, MMP2, MMP8, and MMP9. 44,45 Smoking increases the activity of MMP8 and MMP9 in patients with chronic periodontitis.…”

Section: Discussionmentioning

confidence: 99%

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Cigarette Smoke Extract Induces Select Matrix Metalloproteinases and Integrin Expression in Periodontal Ligament Fibroblasts

Bulmanski

Brady

Stoute

et al. 2012

Journal of Periodontology

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Cigarette Smoke Extract Induces Select Matrix Metalloproteinases and Integrin Expression in Periodontal Ligament Fibroblasts

Bulmanski

Brady

Stoute

et al. 2012

Journal of Periodontology

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“…The cells were also incubated overnight at 4°C with primary antibodies to polyclonal rabbit anti‐porcine amelogenin (117‐81‐2b) (0.1 μg ml −1 ), polyclonal rabbit anti‐porcine ameloblastin (214) (0.1 μg ml −1 ) (courtesy of Dr Takashi Uchida, Department of Oral Biology, Division of Molecular Medical Science, Hiroshima University Graduate School of Biomedical Science, Hiroshima, Japan), monoclonal mouse anti‐human MMP‐20 (5 μg ml −1 ) (Daiichi Fine Chemical, Toyama, Japan), and monoclonal mouse anti‐human KLK‐4 (25 μg ml −1 ) (R&D Systems, Minneapolis, MN, USA). The sequence specificity of amelogenin and ameloblastin antibodies used in this study was conserved between mouse and human . The samples were subsequently incubated with secondary antibody to biotinylated immunoglobulin at room temperature for 30 min and visualized by the avidin‐biotinylated peroxidase complex (ABC) procedure using an ExtrAvidin peroxidase staining kit (Sigma‐Aldrich) and an AEC (3‐amino‐9‐ethylcarbazole) chromogen kit (Sigma‐Aldrich), according to the manufacturer's instructions.…”

Section: Methodsmentioning

confidence: 99%

“…We have reported that epithelial–mesenchymal interactions modulate the expression of alkaline phosphatase, osteocalcin, and bone sialoprotein at the interface between the epithelial cells and fibroblasts from human periodontal ligament . Furthermore, we showed that their interactions modulate the basement membrane for maintaining homeostasis of the periodontium at the interface space . On the other hand, their interactions do not mediate the basement membrane of cementum formation, because the basement membrane of Hertwig's epithelial root sheath is disrupted when cementoblasts start to form acellular cementum.…”

mentioning

confidence: 86%

Epithelial–mesenchymal interactions induce enamel matrix proteins and proteases in the epithelial cells of the rests of Malassez in vitro

Takahashi

Shimonishi

Wang

et al. 2012

European J Oral Sciences

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Epithelial-mesenchymal interactions influence morphogenesis and cell differentiation in periodontal tissue regeneration. The current study examined the expression of amelogenin, ameloblastin, matrix metallopeptidase-20 (MMP-20), and kallikrein-4 (KLK-4) and their effects on the interactions between the epithelial cells of Malassez and periodontal ligament fibroblasts. Explants of human periodontal ligament tissues produced outgrowths containing both the epithelial cells of Malassez and periodontal ligament fibroblasts after incubation in a modified serum-free medium. Both the epithelial cells and fibroblasts were co-cultured in the same dish. The distribution and expression of all four factors were evaluated using immunohistochemistry, in-situ hybridization and RT-PCR analysis. The epithelial cells of Malassez were cultured separately and were used as the control. Immunohistochemical analysis revealed weak expression of amelogenin, ameloblastin, MMP-20 and KLK-4 in epithelial cells of Malassez co-cultured with periodontal ligament fibroblasts. in-situ hybridization and RT-PCR confirmed significant mRNA expression of these factors in co-cultured cells compared with control cells. MMP20 mRNA was not expressed in control cells. These results suggest that the epithelial-mesenchymal interactions promote differentiation of human epithelial cells of Malassez and that the induction of enamel matrix proteases facilitates the degradation of enamel matrix proteins.

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“…Matrix metalloproteinases 2 and 9 were also shown to be induced during the development of inflammatory periapical lesions (34). Using in situ hybridization analysis it was demonstrated that human periodontal ligament fibroblasts expressed matrix metalloproteinase-2 mRNA, whereas putative epithelial cell rests of Malassez expressed matrix metalloproteinase-14 mRNA at the interface between epithelial cells and fibroblasts (194). In the inflammatory response of oral epithelial cells to F. nucleatum, Mahtout et al (127) detected up-regulated gene expression and protein secretion of interleukin-6, interleukin-8 and matrix metalloproteinase-9.…”

Section: Matrix Metalloproteinases 2 Andmentioning

confidence: 99%

Epithelial barrier and oral bacterial infection

Groeger¹,

Meyle²

2015

Periodontology 2000

166

140

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The oral epithelial barrier separates the host from the environment and provides the first line of defense against pathogens, exogenous substances and mechanical stress. It consists of underlying connective tissue and a stratified keratinized epithelium with a basement membrane, whose cells undergo terminal differentiation resulting in the formation of a mechanically resistant surface. Gingival keratinocytes are connected by various transmembrane proteins, such as tight junctions, adherens junctions and gap junctions, each of which has a specialized structure and specific functions. Periodontal pathogens are able to induce inflammatory responses that lead to attachment loss and periodontal destruction. A number of studies have demonstrated that the characteristics of pathogenic oral bacteria influence the expression and structural integrity of different cell-cell junctions. Tissue destruction can be mediated by host cells following stimulation with cytokines and bacterial products. Keratinocytes, the main cell type in gingival epithelial tissues, express a variety of proinflammatory cytokines and chemokines, including interleukin-1alpha, interleukin-1beta, interleukin-6, interleukin-8 and tumor necrosis factor-alpha. Furthermore, the inflammatory mediators that may be secreted by oral keratinocytes are vascular endothelial growth factor, prostaglandin E2 , interleukin-1 receptor antagonist and chemokine (C-C motif) ligand 2. The protein family of matrix metalloproteinases is able to degrade all types of extracellular matrix protein, and can process a number of bioactive molecules. Matrix metalloproteinase activities under inflammatory conditions are mostly deregulated and often increased, and those mainly relevant in periodontal disease are matrix metalloproteinases 1, 2, 3, 8, 9, 13 and 24. Viral infection may also influence the epithelial barrier. Studies show that the expression of HIV proteins in the mucosal epithelium is correlated with the disruption of epithelial tight junctions, suggesting a possible enhancement of human papilloma virus infection by HIV-associated disruption of tight junctions. Altered expression of matrix metalloproteinases was demonstrated in keratinocytes transformed with human papilloma virus-16 or papilloma virus-18,. To summarize, the oral epithelium is able to react to a variety of exogenous, possibly noxious influences.

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Induction of MMP-2 at the interface between epithelial cells and fibroblasts from human periodontal ligament

Cited by 5 publications

References 37 publications

Cigarette Smoke Extract Induces Select Matrix Metalloproteinases and Integrin Expression in Periodontal Ligament Fibroblasts

Cigarette Smoke Extract Induces Select Matrix Metalloproteinases and Integrin Expression in Periodontal Ligament Fibroblasts

Epithelial–mesenchymal interactions induce enamel matrix proteins and proteases in the epithelial cells of the rests of Malassez in vitro

Epithelial barrier and oral bacterial infection

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