Expression of MHC Class II, CD70, CD80, CD86 and pro-inflammatory cytokines is differentially regulated in oral epithelial cells following bacterial challenge

2003 ◽  
Vol 18 (6) ◽  
pp. 350-358 ◽  
Author(s):  
D. C. Han ◽  
G. T-J. Huang ◽  
L. M. Lin ◽  
N. A. Warner ◽  
J. S. Gim ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Mhc Class Ii ◽  
Inflammatory Cytokines ◽  
Class Ii ◽  
Bacterial Challenge ◽  
Oral Epithelial Cells ◽  
Oral Epithelial ◽  
Pro Inflammatory Cytokines

Synergism between TLRs and NOD1/2 in Oral Epithelial Cells

2008 ◽  
Vol 87 (7) ◽  
pp. 682-686 ◽  
Author(s):  
A. Uehara ◽  
H. Takada
Keyword(s):  
Epithelial Cells ◽  
Immune Responses ◽  
Inflammatory Cytokines ◽  
Oral Bacteria ◽  
Innate Immune ◽  
Oral Epithelium ◽  
Innate Immune Responses ◽  
Oral Epithelial Cells ◽  
Oral Epithelial ◽  
Pro Inflammatory Cytokines

Oral epithelium is the first barrier against oral bacteria in periodontal tissue. Oral epithelial cells constitutively express Toll-like receptors (TLRs) and NOD1/2, functional receptors which induce the production of antibacterial factors such as peptidoglycan recognition proteins (PGRPs) and β-defensin 2, but not pro-inflammatory cytokines such as interleukin (IL)-8. In this study, we hypothesized that innate immune responses in the oral epithelium are enhanced in inflamed tissue. We found that NOD1 and NOD2 agonists, in combination with TLR agonists, synergistically induced production of PGRPs and of β-defensin 2 in human oral epithelial cells via NF-κB. In contrast, co-stimulation with NOD1/2 and TLR ligands had no effect on the production of pro-inflammatory cytokines (IL-6, IL-8, and monocyte chemoattractant protein-1). These findings indicate that, in innate immune responses to invading microbes, a combination of signaling through TLRs and NODs leads to the synergistic activation of antibacterial responses in the oral epithelium.

Statin decreases IL-1 and LPS-induced inflammatory cytokines production in oral epithelial cells

2009 ◽  
pp. 125-131 ◽  
Author(s):  
Michihiko Usui ◽  
Reiko Suda ◽  
Yasushi Miyazawa ◽  
Makoto Kobayashi ◽  
Yoshimasa Okamatsu ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Inflammatory Cytokines ◽  
Oral Epithelial Cells ◽  
Oral Epithelial

scholarly journals Dual regulation of interleukin-8 production in human oral epithelial cells upon stimulation with gingipains from Porphyromonas gingivalis

2008 ◽  
Vol 57 (4) ◽  
pp. 500-507 ◽  
Author(s):  
Akiko Uehara ◽  
Mariko Naito ◽  
Takahisa Imamura ◽  
Jan Potempa ◽  
James Travis ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Porphyromonas Gingivalis ◽  
Nuclear Factor Kappa B ◽  
Periodontal Diseases ◽  
Nuclear Factor ◽  
Cysteine Proteinases ◽  
Oral Epithelial Cells ◽  
Cellular Recognition ◽  
Oral Epithelial ◽  
Pro Inflammatory Cytokines

Cysteine proteinases from Porphyromonas gingivalis, or gingipains, are considered to be key virulence factors of the bacterium in relation to periodontal diseases. Incubation of human oral epithelial cells with lysine-specific gingipain (Kgp) and high-molecular-mass arginine-specific gingipain (HRgpA) resulted in a decrease in the production of interleukin (IL)-8, but not in the production of other pro-inflammatory cytokines. In contrast, arginine-specific gingipain 2 (RgpB) increased IL-8 production. RNA interference assays demonstrated that Kgp- and HRgpA-mediated downregulation and RgpB-mediated upregulation occurred through protease-activated receptor (PAR)-1 and PAR-2 signalling. Although the RgpB-mediated upregulation of IL-8 production occurred through nuclear factor-kappa B (NF-κB), the Kgp- and HRgpA-mediated downregulation was not negated in NF-κB-silenced cells. Both the haemagglutinin and the enzymic domains are required for Kgp and HRgpA to downregulate the production of IL-8 in human oral epithelial cells, and the two domains are thought to co-exist. These results suggest that gingipains preferentially suppress IL-8, resulting in attenuation of the cellular recognition of bacteria, and as a consequence, sustain chronic inflammation.

scholarly journals Novel Aggregation Properties of Candida albicans Secreted Aspartyl Proteinase Sap6 Mediate Virulence in Oral Candidiasis

2015 ◽  
Vol 83 (7) ◽  
pp. 2614-2626 ◽  
Author(s):  
Rohitashw Kumar ◽  
Darpan Saraswat ◽  
Swetha Tati ◽  
Mira Edgerton
Keyword(s):  
Candida Albicans ◽  
Epithelial Cells ◽  
Oral Candidiasis ◽  
Oral Microbiome ◽  
Proteinase Activity ◽  
Adhesion Properties ◽  
Content Type ◽  
Oral Epithelial Cells ◽  
Oral Epithelial ◽  
Cell Cell

Candida albicans, a commensal fungus of the oral microbiome, causes oral candidiasis in humans with localized or systemic immune deficiencies. Secreted aspartic proteinases (Saps) are a family of 10 related proteases and are virulence factors due to their proteolytic activity, as well as their roles in adherence and colonization of host tissues. We found that mice infected sublingually withC. albicanscells overexpressing Sap6 (SAP6OE and a Δsap8strain) had thicker fungal plaques and more severe oral infection, while infection with the Δsap6strain was attenuated. These hypervirulent strains had highly aggregative colony structurein vitroand higher secreted proteinase activity; however, the levels of proteinase activity ofC. albicansSaps did not uniformly match their abilities to damage cultured oral epithelial cells (SCC-15 cells). Hyphal induction in cells overexpressing Sap6 (SAP6OE and Δsap8cells) resulted in formation of large cell-cell aggregates. These aggregates could be produced in germinated wild-type cells by addition of native or heat-inactivated Sap6. Sap6 bound only to germinated cells and increasedC. albicansadhesion to oral epithelial cells. The adhesion properties of Sap6 were lost upon deletion of its integrin-binding motif (RGD) and could be inhibited by addition of RGD peptide or anti-integrin antibodies. Thus, Sap6 (but not Sap5) has an alternative novel function in cell-cell aggregation, independent of its proteinase activity, to promote infection and virulence in oral candidiasis.

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