摘要
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.
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.
