• Title of article

    The effect of stromelysin-1 (MMP-3) on non-collagenous extracellular matrix proteins of demineralized dentin and the adhesive properties of restorative resins

  • Author/Authors

    T. Boukpessi، نويسنده , , S. Menashi، نويسنده , , L. Camoin، نويسنده , , J.M. TenCate، نويسنده , , M. Goldberg، نويسنده , , C. Chaussain-Miller، نويسنده ,

  • Issue Information
    روزنامه با شماره پیاپی سال 2008
  • Pages
    7
  • From page
    4367
  • To page
    4373
  • Abstract
    Dentin non-collagenous matrix components (NCPs) are structural proteins involved in the formation, the architecture and the mineralization of the extracellular matrix (ECM). We investigated here how recombinant metalloproteinase stromelysin-1, also termed MMP-3, initiates the release of ECM molecules from artificially demineralized human dentin. Analysis of the supernatants by Western blotting reveals that MMP-3 extracts PGs (decorin, biglycan), and also a series of phosphorylated proteins: dentin sialoprotein (DSP), osteopontin (OPN), bone sialoprotein (BSP) and MEPE, but neither dentin matrix protein-1 (DMP1), another member of the SIBLING family, nor osteocalcin (OC), a non-phosphorylated matrix molecule. After treatment of dentin surfaces by MMP-3, scanning electron microscope (SEM) examination of resin replica shows an increased penetration of the resin into the dentin tubules when compared to surfaces only treated by demineralizing solutions. This preclinical investigation suggests that MMP-3 may be used to improve the adhesive properties of restorative materials.
  • Keywords
    DentinStromelysin-1 (MMP-3)ProteoglycansExtracellular matrix proteins (ECM)Adhesion
  • Journal title
    Biomaterials
  • Serial Year
    2008
  • Journal title
    Biomaterials
  • Record number

    483262