Porphyromonas gingivalis and its lipopolysaccharide differently modulate epidermal growth factor–dependent signaling in human gingival epithelial cells

References

• Hajishengallis G. Periodontitis: from microbial immune subversion to systemic inflammation. Nat Rev Immunol. 2015;15:1–10.
   Web of Science ®Google Scholar
• Kurita-Ochiai T, Jia R, Cai Y, et al. Periodontal disease-induced atherosclerosis and oxidative stress. Antioxidants. 2015;4:577–590.
   Web of Science ®Google Scholar
• Maresz KJ, Hellvard A, Sroka A, et al. Porphyromonas gingivalis facilitates the development and progression of destructive arthritis through its unique bacterial peptidylarginine deiminase (PAD). PLoS Pathogens. 2013;9:1–10.
   Web of Science ®Google Scholar
• Schultz G, Rotatori DS, Clark W. EGF and TGF-alpha in wound healing and repair. J Cell Biochem. 1991;4:346–352.
   Google Scholar
• Brown GL, Curtsinger LJ, White M, et al. Acceleration of tensile strength of incisions treated with EGF and TGF-beta. Ann Surg. 1988;208:788–794.
   PubMed Web of Science ®Google Scholar
• Di Genio M, Barone A, Ramaglia L, et al. Periodontal regeneration: the use of polypeptide growth factors. Minerva Stomatol. 1994;43:437–443.
   Google Scholar
• Di Domenico M, Giordano A. Signal transduction growth factors: the effective governance of transcription and cellular adhesion in cancer invasion. Oncotarget. 2017;16:1–17.
   Google Scholar
• Moosavijazi M, Rasouli Ghahroudi AA, Yaghoobee S, et al. Comparison of salivary epidermal growth factor levels in patients with gingivitis and advanced periodontitis and healthy subjects. J Dent (Tehran). 2011;11:516–522.
   Google Scholar
• Pietruska MD, Pietruski JK, Stokowska W. Polypeptide growth factors in the course of surgical periodontal treatment. Rocz Akad Med Bialymst. 2000;45:199–210.
   Google Scholar
• Chang KM, Lehrhaupt N, Lin LM, et al. Epidermal growth factor in gingival crevicular fluid and its binding capacity in inflamed and non-inflamed human gingiva. Arch Oral Biol. 1996;41:719–724.
   PubMed Web of Science ®Google Scholar
• Suzuki A, Ji G, Numabe Y, et al. Single nucleotide polymorphisms associated with aggressive periodontitis and severe chronic periodontitis in Japanese. Biochem Biophys Res Commun. 2004;317:887–892.
   PubMed Web of Science ®Google Scholar
• Irwin CR, Schor SL, Ferguson MW. Expression of EGF-receptors on epithelial and stromal cells of normal and inflamed gingiva. J Periodontal Res. 1991;26:388–394.
   Web of Science ®Google Scholar
• Parkar MH, Kuru L, Giouzeli M, et al. Expression of growth-factor receptors in normal and regenerating human periodontal cells. Arch Oral Biol. 2001;46:275–284.
   PubMed Web of Science ®Google Scholar
• Soell M, Elkaim R, Tenenbaum H. Cathepsin C, matrix metalloproteinases, and their tissue inhibitors in gingiva and gingival crevicular fluid from periodontitis-affected patients. J Dent Res. 2002;81:174–178.
   Web of Science ®Google Scholar
• Schlessinger J. Ligand-induced, receptor-mediated dimerization and activation of EGF receptor. Cell. 2002;110:669–672.
   PubMed Web of Science ®Google Scholar
• Herbst RS, Sandler AB. Overview of the current status of human epidermal growth factor receptor inhibitors in lung cancer. Clin Lung Cancer. 2004;6:7–19.
   Google Scholar
• Quinchia-Rios BH, Guerrero M, Abozeid S, et al. Down-regulation of epidermal growth factor receptor-dependent signaling by Porphyromonas gingivalis lipopolysaccharide in life-expanded human gingival fibroblasts. J Periodontal Res. 2008;43:290–304.
   Web of Science ®Google Scholar
• Rodríguez SB, Stitt BL, Ash DE. Expression of peptidylarginine deiminase from Porphyromonas gingivalis in Escherichia coli: enzyme purification and characterization. Arch Biochem Biophys. 2009;488:14–22.
   Web of Science ®Google Scholar
• Mangat P, Wegner N, Venables PJ, et al. Bacterial and human peptidylarginine deiminases: targets for inhibiting the autoimmune response in rheumatoid arthritis? Arthritis Res Ther. 2010;12:209–217.
   PubMed Web of Science ®Google Scholar
• Pyrc K, Milewska A, Kantyka T, et al. Inactivation of epidermal growth factor by Porphyromonas gingivalis as a potential mechanism for periodontal tissue damage. Infect Immun. 2013;81:55–64.
   Web of Science ®Google Scholar
• McGraw WT, Potempa J, Farley D, et al. Purification, characterization, and sequence analysis of a potential virulence factor from Porphyromonas gingivalis, peptidylarginine deiminase. Infect Immun. 1999;67:3248–3256.
   PubMed Web of Science ®Google Scholar
• Carow B, Rottenberg ME. SOCS-3, a major regulator of infection and inflammation. Front Immunol. 2014;19(5):58.
   Google Scholar
• Li Y, de Haar C, Peppelenbosch MP, et al.. SOCS-3 in immune regulation of inflammatory bowel disease and inflammatory bowel disease-related cancer. Cytokine Growth Factor Rev. 2012;23:127–138.
   Web of Science ®Google Scholar
• Alexander WS, Starr R, Metcalf D, et al. Suppressors of cytokine signaling (SOCS): negative regulators of signal transduction. J Leukoc Biol. 1999;66:588–592.
   PubMed Web of Science ®Google Scholar
• Jauregui CE, Wang Q, Wright CJ, et al. Suppression of T-cell chemokines by Porphyromonas gingivalis. Infect Immun. 2013;81:2288–2295.
   PubMed Web of Science ®Google Scholar
• Elkaim R, Obrecht-Pflumio S, Tenenbaum H. Paxillin phosphorylation and integrin expression in osteoblasts infected by Porphyromonas gingivalis. Arch Oral Biol. 2006;51:761–768.
   Web of Science ®Google Scholar
• Mali SB. Review of STAT3 (Signal Transducers and Activators of Transcription) in head and neck cancer. Oral Oncol. 2015;51:565–569.
   Web of Science ®Google Scholar
• Cavalcante LB, Tanaka MH, Pires JR, et al. Expression of the interleukin-10 signaling pathway genes in individuals with Down syndrome and periodontitis. J Periodontol. 2012;83:926–935.
   Web of Science ®Google Scholar
• Moffatt CE, Lamont RJ. Porphyromonas gingivalis induction of microRNA-203 expression controls suppressor of cytokine signaling 3 in gingival epithelial cells. Infect Immun. 2011;79:2632–2637.
   PubMed Web of Science ®Google Scholar
• Zhou Q, Amar S. Identification of proteins differentially expressed in human monocytes exposed to Porphyromonas gingivalis and its purified components by high-throughput immunoblotting. Infect Immun. 2006;74:1204–1214.
   Web of Science ®Google Scholar
• Tanaka MH, Giro EM, Cavalcante LB, et al. Expression of interferon-γ, interferon-α and related genes in individuals with Down syndrome and periodontitis. Cytokin. 2012;60:875–881.
   Google Scholar
• Bode JG, Ehlting C, Häussinger D. The macrophage response towards LPS and its control through the p38(MAPK)-STAT3 axis. Cell Signal. 2012;24:1185–1194.
   PubMed Web of Science ®Google Scholar
• Cho YC, Kim HJ, Kim YJ, et al. Differential anti-inflammatory pathway by xanthohumol in IFN-gamma and LPS-activated macrophages. Int Immunopharmacol. 2008;8:567–573.
   PubMed Web of Science ®Google Scholar
• Marecki S, Riendeau CJ, Liang MD, et al. PU1 and multiple IFN regulatory factor proteins synergize to mediate transcriptional activation of the human IL-1 beta gene. J Immunol. 2001;166:6829–6838.
   PubMed Web of Science ®Google Scholar
• Jang SW, Lim SG, Suk K, et al. Activation of lymphotoxin-beta receptor enhances the LPS-induced expression of IL-8 through NF-κB and IRF-1. Immunol Lett. 2015;165:63–69.
   Web of Science ®Google Scholar
• Zhang L, Cardinal JS, Bahar R, et al. Interferon regulatory factor-1 regulates the autophagic response in LPS-stimulated macrophages through nitric oxide. Mol Med. 2012;18:201–208.
   PubMed Web of Science ®Google Scholar
• Zhou Q, Desta T, Fenton M, et al. Cytokine profiling of macrophages exposed to Porphyromonas gingivalis, its lipopolysaccharide or its FimA protein. Infect Immun. 2005;74:935–943.
   Web of Science ®Google Scholar
• Mao S, Park Y, Hasegawa Y, et al. Intrinsic apoptotic pathways of gingival epithelial cells modulated by Porphyromonas gingivalis. Cell Microbiol. 2007;9:1997–2007.
   PubMed Web of Science ®Google Scholar
• Babon JJ, Nicola NA. The biology and mechanism of action of suppressor of cytokine signaling 3. Growth Factors. 2012;30:207–219.
   PubMed Web of Science ®Google Scholar
• Soo Kim H, Young Park S, Kyoung Kim E, et al. Acanthopanax senticosus has a heme oxygenase-1 signaling-dependent effect on Porphyromonas gingivalis lipopolysaccharide-stimulated macrophages. J Ethnopharmacol. 2012;142:819–828.
   Web of Science ®Google Scholar