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

被引:74
|
作者
Boukpessi, T. [1 ]
Menashi, S. [2 ]
Camoin, L. [3 ]
TenCate, J. M.
Goldberg, M. [1 ]
Chaussain-Miller, C. [1 ]
机构
[1] Univ Paris 05, Fac Chirurg Dentaire, Grp Matrice Extracellulaire & Biomineralisat EA 2, F-92120 Montrouge, France
[2] Univ Paris 12, Lab CRRET, CNRS, UMR 7149, Creteil, France
[3] Univ Paris 05, Proteom Lab, Cochin Inst, Paris, France
关键词
Dentin; Stromelysin-1 (MMP-3); Proteoglycans; Extracellular matrix proteins (ECM); Adhesion;
D O I
10.1016/j.biomaterials.2008.07.035
中图分类号
R318 [生物医学工程];
学科分类号
0831 ;
摘要
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 PCs (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 (DMPI), 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. (C) 2008 Elsevier Ltd. All rights reserved.
引用
收藏
页码:4367 / 4373
页数:7
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