Activation of human gingival epithelial cells by cell-surface components of black-pigmented bacteria: augmentation of production of interleukin-8, granulocyte colony-stimulating factor and granulocyte-macrophage colony-stimulating factor and expression of intercellular adhesion molecule 1

Sugiyama, Akira; Uehara, Akiko; Iki, K; Matsushita, Kakushi; Nakamura, Ryô; Ogawa, Taro; Sugawara, Shunji; Takada, Haruhiko

doi:10.1099/0022-1317-51-1-27

Cited by 50 publications

(41 citation statements)

References 18 publications

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“…In addition to acting as a physical barrier against the invasion of pathogenic organisms, oral (gingival) epithelial cells in inflamed regions appear to express several proinflammatory cytokines such as IL-1␤, IL-6, IL-8, TNF-␣, and TGF-␤1 (22), implying that the cells actively participate in the initiation and development of chronic oral inflammation such as periodontitis. However, only a few studies have demonstrated cytokine production by human gingival epithelial cells and related cell lines derived from the oral cavity in response to oral bacteria (23)(24)(25). In contrast to human colonic epithelial cells, human oral epithelial cells are shown to be basically unresponsive to many bacterial cell surface components, even in the presence of the soluble form of CD14, a bacterial pattern recognition receptor (26).…”

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confidence: 99%

Activation of Human Oral Epithelial Cells by Neutrophil Proteinase 3 Through Protease-Activated Receptor-2

Uehara¹,

Sugawara²,

Muramoto

et al. 2002

The Journal of Immunology

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Proteinase 3 (PR3), a 29-kDa serine proteinase secreted from activated neutrophils, also exists in a membrane-bound form, and is suggested to actively contribute to inflammatory processes. The present study focused on the mechanism by which PR3 activates human oral epithelial cells. PR3 activated the epithelial cells in culture to produce IL-8 and monocyte chemoattractant protein-1 and to express ICAM-1 in a dose- and time-dependent manner. Incubation of the epithelial cells for 24 h with PR3 resulted in a significant increase in the adhesion to neutrophils, which was reduced to baseline levels in the presence of anti-ICAM-1 mAb. Activation of the epithelial cells by PR3 was inhibited by serine proteinase inhibitors and serum. The epithelial cells strongly express protease-activated receptor (PAR)-1 and PAR-2 mRNA and weakly express PAR-3 mRNA. The expression of PAR-2 on the cell surface was promoted by PR3, and inhibited by cytochalasin B, but not by cycloheximide. PR3 cleaved the peptide corresponding to the N terminus of PAR-2 with exposure of its tethered ligand. Treatment with trypsin, an agonist for PAR-2, and a synthetic PAR-2 agonist peptide induced intracellular Ca2+ mobilization, and rendered cells refractory to subsequent stimulation with PR3 and vice versa. The production of cytokine induced by PR3 and the PAR-2 agonist peptide was completely abolished by a phospholipase C inhibitor. These findings suggest that neutrophil PR3 activates oral epithelial cells through G protein-coupled PAR-2 and actively participates in the process of inflammation such as periodontitis.

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confidence: 99%

Activation of Human Oral Epithelial Cells by Neutrophil Proteinase 3 Through Protease-Activated Receptor-2

Uehara¹,

Sugawara²,

Muramoto

et al. 2002

The Journal of Immunology

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“…In addition, the level of IL-8 was significantly elevated in the GCF of periodontitis patients compared to the GCF of healthy subjects (16). The surface molecules that showed enhanced IL-8 secretion were P. gingivalis gingipain-R (40), a glycoprotein fraction in the cell surface from P. intermedia (48), and a capsular polysaccharide from Actinobacillus actinomycetemcomitans (39). Several oral treponemes have been reported to stimulate proinflammatory cytokines in various cell types, such as gingival fibroblasts and gingival epithelial cells (2,25,37,43).…”

Section: Vol 73 2005 Induction Of Icam-1 and Cytokines By Spirochetmentioning

confidence: 99%

“…It is believed to play an important role in initiating the inflammatory reactions in gingival tissues, and its level of expression is related to the severity of periodontitis. Stimulated IL-8 production in the inflamed gingiva has been reported in the epithelium (45,48), gingival fibroblasts (52), and monocytes (47). In addition, the level of IL-8 was significantly elevated in the GCF of periodontitis patients compared to the GCF of healthy subjects (16).…”

Section: Vol 73 2005 Induction Of Icam-1 and Cytokines By Spirochetmentioning

confidence: 99%

“…It has been suggested that ICAM-1 is a therapeutic target in the inflamed gingiva based on local topical application of ICAM-1-directed antisense oligonucleotides (36). Among the periodontopathogens, LPS and purified fimbriae of Porphyromonas gingivalis and the glycoprotein fraction of Prevotella intermedia have been reported to induce ICAM-1 expression in human gingival fibroblasts (28,48). In Eikenella corrodens, an N-acetyl-D-galactosamine-specific lectin-like substance, an adhesin, was reported to be involved in induction of ICAM-1 expression in human oral epithelial cells (56).…”

Section: Vol 73 2005 Induction Of Icam-1 and Cytokines By Spirochetmentioning

confidence: 99%

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Upregulation of Intercellular Adhesion Molecule 1 and Proinflammatory Cytokines by the Major Surface Proteins of Treponema maltophilum and Treponema lecithinolyticum , the Phylogenetic Group IV Oral Spirochetes Associated with Periodontitis and Endodontic Infections

Lee¹,

Kim

Choi

2005

Infect Immun

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Treponema maltophilum and Treponema lecithinolyticum belong to the group IV oral spirochetes and are associated with endodontic infections, as well as periodontitis. Recently, the genes encoding the major surface proteins (Msps) of these bacteria (MspA and MspTL, respectively) were cloned and sequenced. The amino acid sequences of these proteins showed significant similarity. In this study we analyzed the functional role of these homologous proteins in human monocytic THP-1 cells and primary cultured periodontal ligament (

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“…Upon stimulation with the soluble mediators of inflammation, such as TNF-α as well as pathogen-associated molecular patterns (PAMPs), they secrete proinflammatory cytokines, including IL-8 (Li et al, 1996;Sugiyama et al, 2002). We know that ghrelin can reduce the LPS-induced pro-inflammatory response in murine macrophages (Waseem et al, 2008).…”

Section: Introduction Gmentioning

confidence: 99%

Expression and Possible Immune-regulatory Function of Ghrelin in Oral Epithelium

et al. 2011

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Originally found in stomach mucosa, ghrelin is a peptide appetite hormone that has been implicated as an immuno-modulatory factor. Ghrelin has also been found in salivary glands and saliva; however, its expression patterns and biological properties in the oral cavity remain unclear. Therefore, we investigated the expression patterns of ghrelin in saliva, gingival crevicular fluid (GCF), and gingival tissue, as well as its in vitro effects on IL-8 production by TNF-α or LPS-stimulated oral epithelial cells. In the clinical samples obtained from 12 healthy volunteers, the concentration of ghrelin in GCF remarkably exceeded that detected in saliva. The expression of ghrelin mRNAs and growth hormone secretagogue (GHS) receptors could be detected in human oral epithelial cells. Immunohistochemical analysis revealed the expression of ghrelin in gingival epithelium, as well as in fibroblasts in the lamina propria. Ghrelin increased intracellular calcium mobilization and cAMP levels in oral epithelial cells, suggesting that ghrelin acts on epithelial cells to induce cell signaling. Furthermore, synthetic ghrelin inhibited the production of IL-8 from TNF-α or LPS-stimulated oral epithelial cells. These results indicate that ghrelin produced in the oral cavity appears to play a regulatory role in innate immune responses to inflammatory infection.

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Activation of human gingival epithelial cells by cell-surface components of black-pigmented bacteria: augmentation of production of interleukin-8, granulocyte colony-stimulating factor and granulocyte-macrophage colony-stimulating factor and expression of intercellular adhesion molecule 1

Cited by 50 publications

References 18 publications

Activation of Human Oral Epithelial Cells by Neutrophil Proteinase 3 Through Protease-Activated Receptor-2

Activation of Human Oral Epithelial Cells by Neutrophil Proteinase 3 Through Protease-Activated Receptor-2

Upregulation of Intercellular Adhesion Molecule 1 and Proinflammatory Cytokines by the Major Surface Proteins of Treponema maltophilum and Treponema lecithinolyticum , the Phylogenetic Group IV Oral Spirochetes Associated with Periodontitis and Endodontic Infections

Expression and Possible Immune-regulatory Function of Ghrelin in Oral Epithelium

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