Abstract

Dental implant therapy is a highly effective treatment for recovering occlusion after tooth loss. An important factor in the success of dental implants is establishing strong osseointegration. If more epithelial cells migrate to the implant-bone interface than mesenchymal stem cells, effective osseointegration may fail. Therefore, controlling epithelial cell adhesion and motility would be an effective strategy to increase the success rate of osseointegration. Laminin-332 is a major component of the basement membrane and is composed of three chains (α3, β3 and γ2). It is well-known that laminin-332 regulates cellular functions such as adhesion, proliferation, apoptosis and differentiation. These biological functions depend on changes in the structural arrangement of laminin-332 by proteolytic cleavage. It is well-known that cleavage of the α3 chain between its LG domains gives laminin-332 its biological function. In this study, we focused on LG domain cleavage and developed antibodies that target the LG domain cleavage site. We attempted to change the biological function of laminin-332 to control cell adhesion for the purpose of regulating dental implant therapy.

Highlights

  • Dental implant therapy is a key option for the recovery of occlusion following tooth loss [1] [2]

  • We focused on LG domain cleavage and developed antibodies that target the LG domain cleavage site

  • We focused on the structural change in the α3 chain of laminin332 by cleavage of LG domains

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Summary

Introduction

Dental implant therapy is a key option for the recovery of occlusion following tooth loss [1] [2]. The success of dental implants is related to effective osseointegration [3] [4]. Strong osseointegration may be lost when epithelial cells invade the target sites earlier than mesenchymal stem cells [5] [6]. The regulation of epithelial cells and mesenchymal stem cells could facilitate successful osseointegration in dental implant therapy.

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