title: Enamel matrix proteins bind to wound matrix proteins and regulate their cell-adhesive properties.
abstract: Enamel matrix proteins (EMP) induce periodontal regeneration and accelerate dermal wound healing, but the cellular mechanisms of these processes are unclear. We investigated the binding of EMP to the wound matrix proteins fibronectin, laminin-1, collagen type I, and collagen type IV and analyzed the interaction of epithelial cells and periodontal ligament fibroblasts (PDLF) with EMP and composite matrices of EMP + fibronectin or EMP + collagen. The adhesion of PDLF to EMP was concentration- and integrin-dependent and did not require de novo protein synthesis. EMP supported PDLF migration. In contrast, keratinocytes did not adhere to EMP if their protein synthesis was blocked. EMP showed concentration-dependent binding of fibronectin, peaking at 100 microg ml(-1) (before the precipitation point) of EMP. Type I collagen binding to EMP peaked at a low (1 microg ml(-1)) and narrow concentration range. Neither laminin-1 nor type IV collagen bound to EMP. Collagen and fibronectin, bound to EMP, showed significantly reduced (> 50%) binding of both epithelial cells and PDLF compared with the equivalent concentration of these proteins alone. PDLF, but not epithelial cell, adhesion was rescued by increasing the EMP concentration. These findings show that EMP binds to wound extracellular matrix proteins and regulates their adhesive properties. Such interactions may favor fibroblast adhesion over epithelial cells, potentially promoting connective tissue regeneration.
authors: Faculty of Dentistry, Department of Oral, Biological and Medical Sciences, Laboratory of Periodontal Biology, University of British Columbia, Vancouver, BC, Canada.
authors: Nazanin
authors: N
authors: Narani
authors: Gethin Rhys
authors: GR
authors: Owen
authors: Lari
authors: L
authors: Häkkinen
authors: Edward
authors: E
authors: Putnins
authors: Hannu
authors: H
authors: Larjava
mesh_terms: D000704:Analysis of Variance; D000818:Animals; D002417:Cattle; D002448:Cell Adhesion / Q000502:physiology*; D018929:Cell Culture Techniques / Q000379:methods; D002465:Cell Movement; D024042:Collagen Type I / Q000737:chemistry / Q000378:metabolism; D024141:Collagen Type IV / Q000737:chemistry / Q000378:metabolism; D003746:Dental Enamel Proteins / Q000737:chemistry / Q000378:metabolism*; D004847:Epithelial Cells / Q000737:chemistry / Q000378:metabolism; D005347:Fibroblasts / Q000378:metabolism*; D005353:Fibronectins / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D007797:Laminin / Q000737:chemistry / Q000378:metabolism; D010513:Periodontal Ligament / Q000166:cytology; D014945:Wound Healing / Q000502:physiology*
chemical_list: D024042:Collagen Type I; D024141:Collagen Type IV; D003746:Dental Enamel Proteins; D005353:Fibronectins; D007797:Laminin; C109069:enamel matrix proteins; C121346:laminin 1