Human Cementum Protein 1 induces expression of bone and cementum proteins by human gingival fibroblasts

Biochem Biophys Res Commun. 2007 Jul 6;358(3):763-9. doi: 10.1016/j.bbrc.2007.04.204. Epub 2007 May 11.

Abstract

We recently presented evidence showing that a human cementoblastoma-derived protein, named Cementum Protein 1 (CEMP1) may play a role as a local regulator of cementoblast differentiation and cementum-matrix mineralization. This protein was shown to be expressed by cementoblasts and progenitor cells localized in the periodontal ligament. In this study we demonstrate that transfection of CEMP1 into human gingival fibroblasts (HGF) induces mineralization and expression of bone and cementum-matrix proteins. The transfected HGF cells had higher alkaline phosphatase activity and proliferation rate and they expressed genes for alkaline phosphatase, bone sialoprotein, osteocalcin, osteopontin, the transcription factor Runx2/Cbfa1, and cementum attachment protein (CAP). They also produced biological-type hydroxyapatite. These findings indicate that the CEMP1 might participate in differentiation and mineralization of nonosteogenic cells, and that it might have a potential function in cementum and bone formation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alkaline Phosphatase / metabolism
  • Blotting, Northern
  • Bone and Bones / metabolism*
  • Cell Adhesion Molecules / biosynthesis*
  • Cell Differentiation
  • Cell Proliferation
  • Cells, Cultured
  • Fibroblasts / metabolism*
  • Gene Expression Regulation*
  • Gingiva / cytology*
  • Hepatocyte Growth Factor / metabolism
  • Humans
  • Phenotype
  • Time Factors
  • Transfection

Substances

  • Cell Adhesion Molecules
  • cementum attachment protein, 55-kDa
  • Hepatocyte Growth Factor
  • Alkaline Phosphatase