Localization of Integrin Beta-4 Subunit at Soft Tissue–Titanium or Zirconia Interface

Currently, along with titanium (Ti), zirconia is widely used as an abutment material for dental implants because it makes it possible to avoid gingival discoloration; however, the epithelial sealing capability of zirconia remains unknown. The purpose of the present study is to elucidate the localization of integrin β4 subunit (Inβ4), one of the main proteins in the attachment structure between gingival junctional epithelial (JE) cells and substrata. Maxillary first molars were extracted from rats, and implants were placed with Ti or zirconia transgingival parts; then, the localization of Inβ4 was observed. Morphological and functional changes in rat oral epithelial cells (OECs) cultured on a culture dish (Dish) and Ti and zirconia plates were also evaluated with Inβ4 immunofluorescence histochemistry and Western blotting. After four weeks of implant placement, the morphology of the peri-implant epithelium (PIE) and the localization of Inβ4 around the Ti and zirconia transgingival parts were similar. However, both exhibited markedly shorter Inβ4-positive bands in the PIE than in the JE around natural teeth. Decreased expression levels of Inβ4 were observed in OECs cultured on Ti and zirconia plates compared with those cultured on Dish. In conclusion, although inferior to natural teeth, zirconia implants are thought to have epithelial sealing properties comparable to those of titanium.

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Faculty Opinions recommendation of From attachment to damage: defined genes of Candida albicans mediate adhesion, invasion and damage during interaction with oral epithelial cells.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.11552956.12602054 ◽

2011 ◽

Author(s):

Judith Berman ◽

Anja Forche

Keyword(s):

Candida Albicans ◽

Epithelial Cells ◽

Oral Epithelial Cells ◽

Oral Epithelial

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Assessment of the Effect of Complete Denture Adhesives on Oral Epithelial Cells’ DNA in Elderly Patients with Controlled Diabetes

Egyptian Dental Journal ◽

10.21608/edj.2018.77272 ◽

2018 ◽

Vol 64 (3) ◽

pp. 2747-2756

Author(s):

Noha El-Shaheed ◽

Amira Gomaa ◽

Ashraf Zakaria

Keyword(s):

Epithelial Cells ◽

Elderly Patients ◽

Complete Denture ◽

Oral Epithelial Cells ◽

Denture Adhesives ◽

Oral Epithelial

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

Infection and Immunity ◽

10.1128/iai.00282-15 ◽

2015 ◽

Vol 83 (7) ◽

pp. 2614-2626 ◽

Cited By ~ 35

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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