Epithelial cell adhesion efficacy of a novel peptide identified by panning on a smooth titanium surface

Hidemichi Kihara; David M. Kim; Masazumi Nagai; Toshiki Nojiri; Shigemi Nagai; Chia-Yu Chen; Cliff Lee; Wataru Hatakeyama; Hisatomo Kondo; John Da Silva

doi:10.1038/s41368-018-0022-1

International Journal of Oral Science ›› 2018, Vol. 10 ›› Issue (3) : 21 DOI: 10.1038/s41368-018-0022-1

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Epithelial cell adhesion efficacy of a novel peptide identified by panning on a smooth titanium surface

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Abstract

Epithelial attachment via the basal lamina on the tooth surface provides an important structural defence mechanism against bacterial invasion in combating periodontal disease. However, when considering dental implants, strong epithelial attachment does not exist throughout the titanium-soft tissue interface, making soft tissues more susceptible to peri-implant disease. This study introduced a novel synthetic peptide (A10) to enhance epithelial attachment. A10 was identified from a bacterial peptide display library and synthesized. A10 and protease-activated receptor 4-activating peptide (PAR4-AP, positive control) were immobilized on commercially pure titanium. The peptide-treated titanium showed high epithelial cell migration ability during incubation in platelet-rich plasma. We confirmed the development of dense and expanded BL (stained by Ln5) with pericellular junctions (stained by ZO1) on the peptide-treated titanium surface. In an adhesion assay of epithelial cells on A10-treated titanium, PAR4-AP-treated titanium, bovine root and non-treated titanium, A10-treated titanium and PAR4-AP-treated titanium showed significantly stronger adhesion than non-treated titanium. PAR4-AP-treated titanium showed significantly higher inflammatory cytokine release than non-treated titanium. There was no significant difference in inflammatory cytokine release between A10-treated and non-treated titanium. These results indicated that A10 could induce the adhesion and migration of epithelial cells with low inflammatory cytokine release. This novel peptide has a potentially useful application that could improve clinical outcomes with titanium implants and abutments by reducing or preventing peri-implant disease.

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Hidemichi Kihara, David M. Kim, Masazumi Nagai, Toshiki Nojiri, Shigemi Nagai, Chia-Yu Chen, Cliff Lee, Wataru Hatakeyama, Hisatomo Kondo, John Da Silva. Epithelial cell adhesion efficacy of a novel peptide identified by panning on a smooth titanium surface. International Journal of Oral Science, 2018, 10(3): 21 DOI:10.1038/s41368-018-0022-1

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References

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[1]	Larjava H, Koivisto L, Hakkinen L, Heino J. Epithelial integrins with special reference to oral epithelia. J. Dent. Res., 2011, 90: 1367-1376.

[2]	Atsuta I, . Evaluations of epithelial sealing and peri-implant epithelial down-growth around "step-type" implants. Clin. Oral. Implants Res., 2012, 23: 459-466.

[3]	Ikeda H, . Difference in penetration of horseradish peroxidase tracer as a foreign substance into the peri-implant or junctional epithelium of rat gingivae. Clin. Oral. Implants Res., 2002, 13: 243-251.

[4]	Linkevicius T, Apse P. Biologic width around implants. Evid.-Based Rev. Stomatol. / Issued Public Inst. "Odontol. Stud." [Et al], 2008, 10: 27-35.

[5]	Iglhaut G, . Epithelial attachment and downgrowth on dental implant abutments--a comprehensive review. J. Esthet. Restor. Dent., 2014, 26: 324-331.

[6]	Deporter DA, Kermalli J, Todescan R, Atenafu E. Performance of sintered, porous-surfaced, press-fit implants after 10 years of function in the partially edentulous posterior mandible. Int J. Periodontics Restor. Dent., 2012, 32: 563-570.

[7]	Deporter D, Pharoah M, Yeh S, Todescan R, Atenafu EG. Performance of titanium alloy sintered porous-surfaced (SPS) implants supporting mandibular overdentures during a 20-year prospective study. Clin. Oral. Implants Res., 2014, 25: e189-e195.

[8]	Lops D, . Short implants in partially edentuolous maxillae and mandibles: a 10 to 20 years retrospective evaluation. Int. J. Dent., 2012, 2012: 351793.

[9]	Mangano FG, . Short (8-mm) locking-taper implants supporting single crowns in posterior region: a prospective clinical study with 1-to 10-years of follow-up. Clin. Oral. Implants Res., 2014, 25: 933-940.

[10]	Simonis P, Dufour T, Tenenbaum H. Long-term implant survival and success: a 10-16-year follow-up of non-submerged dental implants. Clin. Oral. Implants Res., 2010, 21: 772-777.

[11]	Lang NP, Berglundh T Periodontology WGoSEWo. Periimplant diseases: where are we now?--Consensus of the Seventh European Workshop on Periodontology. J. Clin. Periodontol., 2011, 38(Suppl 11): 178-181.

[12]	Mombelli A, Müller N, Cionca N. The epidemiology of peri-implantitis. Clin. Oral. Implants Res, 2012, 23(Suppl 6): 67-76.

[13]	Hormia M, Könönen M, Kivilahti J, Virtanen I. Immunolocalization of proteins specific for adhaerens junctions in human gingival epithelial cells grown on differently processed titanium surfaces. J. Periodontal Res, 1991, 26: 491-497.

[14]	Werner S, . The effect of microstructured surfaces and laminin-derived peptide coatings on soft tissue interactions with titanium dental implants. Biomaterials, 2009, 30: 2291-2301.

[15]	Rich A, Harris AK. Anomalous preferences of cultured macrophages for hydrophobic and roughened substrata. J. Cell Sci., 1981, 50: 1-7.

[16]	Sugawara S, . Establishment of epithelial attachment on titanium surface coated with platelet activating peptide. PLoS ONE, 2016, 11: e0164693.

[17]	Maeno M, . Function of platelet-induced epithelial attachment at titanium surfaces inhibits microbial colonization. J. Dent. Res., 2017, 96: 633-639.

[18]	Atsuta I, . Promotive effect of insulin-like growth factor-1 for epithelial sealing to titanium implants. J. Biomed. Mater. Res. A, 2013, 101: 2896-2904.

[19]	Dorkhan M, Yucel-Lindberg T, Hall J, Svensater G, Davies JR. Adherence of human oral keratinocytes and gingival fibroblasts to nano-structured titanium surfaces. BMC Oral Health, 2014, 14

[20]	Vergnolle N, Derian CK, D'Andrea MR, Steinhoff M, Andrade-Gordon P. Characterization of thrombin-induced leukocyte rolling and adherence: a potential proinflammatory role for proteinase-activated receptor-4. J. Immunol., 2002, 169: 1467-1473.

[21]	Hollenberg MD, Saifeddine M, Sandhu S, Houle S, Vergnolle N. Proteinase-activated receptor-4: evaluation of tethered ligand-derived peptides as probes for receptor function and as inflammatory agonists in vivo. Br. J. Pharmacol., 2004, 143: 443-454.

[22]	Ehrlich GK, Berthold W, Bailon P. Phage display technology. Affinity selection by biopanning. Methods Mol. Biol., 2000, 147: 195-208.

[23]	Gerwert K. Molecular reaction mechanisms of proteins monitored by time-resolved FTIR-spectroscopy. Biol. Chem., 1999, 380: 931-935.

[24]	Burnouf T, . Blood-derived biomaterials and platelet growth factors in regenerative medicine. Blood Rev., 2013, 27: 77-89.

[25]	Kouzoukas DE, . Protease-activated receptor 4 induces bladder pain through high mobility group box-1. PLoS ONE, 2016, 11: e0152055.

[26]	Asokananthan N, . Activation of protease-activated receptor (PAR)-1, PAR-2, and PAR-4 stimulates IL-6, IL-8, and prostaglandin E2 release from human respiratory epithelial cells. J. Immunol., 2002, 168: 3577-3585.

[27]	Strande JL, Phillips SA. Thrombin increases inflammatory cytokine and angiogenic growth factor secretion in human adipose cells in vitro. J. Inflamm., 2009, 6: 4.

[28]	Steinhoff M, . Proteinase-activated receptors: transducers of proteinase-mediated signaling in inflammation and immune response. Endocr. Rev., 2005, 26: 1-43.

[29]	Cocks TM, Moffatt JD. Protease-activated receptors: sentries for inflammation?. Trends Pharmacol. Sci., 2000, 21: 103-108.

[30]	Shankar R, de la Motte CA, Poptic EJ, DiCorleto PE. Thrombin receptor-activating peptides differentially stimulate platelet-derived growth factor production, monocytic cell adhesion, and E-selectin expression in human umbilical vein endothelial cells. J. Biol. Chem., 1994, 269: 13936-13941.

[31]	Colotta F, . Expression of monocyte chemotactic protein-1 by monocytes and endothelial cells exposed to thrombin. Am. J. Pathol., 1994, 144: 975-985.

[32]	Jesmin S, Gando S, Zaedi S, Sakuraya F. Differential expression, time course and distribution of four PARs in rats with endotoxin-induced acute lung injury. Inflammation, 2007, 30: 14-27.

[33]	Yun LW, Decarlo AA, Hunter N. Blockade of protease-activated receptors on T cells correlates with altered proteolysis of CD27 by gingipains of Porphyromonas gingivalis. Clin. Exp. Immunol., 2007, 150: 217-229.

[34]	Nieuwenhuizen L, . Stimulation of naïve monocytes and PBMCs with coagulation proteases results in thrombin-mediated and PAR-1-dependent cytokine release and cell proliferation in PBMCs only. Scand. J. Immunol., 2013, 77: 339-349.

[35]	Wang H, He S. Induction of lactoferrin and IL-8 release from human neutrophils by tryptic enzymes via proteinase activated receptor-2. Cell Biol. Int, 2006, 30: 688-697.

[36]	Miike S, McWilliam AS, Kita H. Trypsin induces activation and inflammatory mediator release from human eosinophils through protease-activated receptor-2. J. Immunol., 2001, 167: 6615-6622.

[37]	He S, . Analysis of properties and proinflammatory functions of cockroach allergens Per a 1.01s. Scand. J. Immunol., 2011, 74: 288-295.

[38]	Han W, Wang Z, Lu X, Guo C. Protease activated receptor 4 status of mast cells in post infectious irritable bowel syndrome. Neurogastroenterol. Motil., 2012, 24: 113-9, e182.

[39]	Suo Z, Wu M, Citron BA, Gao C, Festoff BW. Persistent protease-activated receptor 4 signaling mediates thrombin-induced microglial activation. J. Biol. Chem., 2003, 278: 31177-31183.

[40]	Kornman KS, Page RC, Tonetti MS. The host response to the microbial challenge in periodontitis: assembling the players. Periodontol 2000, 1997, 14: 33-53.