Dentin matrix protein 1 initiates hydroxyapatite formation in vitro

Gen He, Thomas Dahl, Arthur Veis, Anne George*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

89 Scopus citations


Bone and dentin formation are interesting examples of matrix-mediated mineralization. However, factors and mechanisms regulating this process are poorly understood. Dentin matrix protein 1 (DMP1) is an acidic extracellular matrix protein found in dentin and bone, and based on its amino acid composition it could be postulated to play an important role in mineralization. Our present study examines the ability of recombinant DMP1 to initiate apatite formation in vitro. A 45Ca-binding assay demonstrated that recombinant DMP1 (rDMP1) possesses calcium-binding ability under physiological conditions. The in vitro nucleation experiments when conducted with rDMP1-coated glass plates demonstrated hydroxyapatite nucleation, while amorphous mineral was deposited on blank or BSA-coated surface. This mineral deposition was found to be 10-fold higher on rDMP1-coated glass surface when compared with the control glass plates. These findings suggest that DMP1 could be considered as a nucleator for apatite deposition in vitro.

Original languageEnglish (US)
Pages (from-to)240-245
Number of pages6
JournalConnective tissue research
Issue numberSUPPL. 1
StatePublished - 2003


  • Apatite nucleation
  • Biomineralization
  • Dentin matrix protein 1

ASJC Scopus subject areas

  • Rheumatology
  • Biochemistry
  • Orthopedics and Sports Medicine
  • Molecular Biology
  • Cell Biology

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