Different forms of DMP1 play distinct roles in mineralization. Academic Article uri icon

abstract

  • Dentin matrix protein-1 (DMP1) is a major synthetic product of hypertrophic chondrocytes and osteocytes. Previous in vitro studies showed full-length DMP1 inhibits hydroxyapatite (HA) formation and growth, while its N-terminal fragment (37K) promotes HA formation. Since there are 3 fragments within the mineralized tissues [N-terminal, C-terminal (57K), and a chondroitin-sulfate-linked N-terminal fragment (DMP1-PG)], we predicted that each would have a distinct effect on mineralization related to its interaction with HA. In a gelatin-gel system, 37K and 57K fragments were both promoters of HA formation and growth; DMP1-PG was an inhibitor. The secondary structures of the 3 fragments and the full-length protein in the presence and absence of Ca2+ and HA determined by FTIR showed that the full-length protein undergoes slight conformational changes on binding to HA, while 37K, 57K, and DMP1-PG do not change conformation. These findings indicate that distinct forms of DMP1 may work collectively in controlling the mineralization process.

published proceedings

  • J Dent Res

author list (cited authors)

  • Gericke, A., Qin, C., Sun, Y., Redfern, R., Redfern, D., Fujimoto, Y., ... Boskey, A. L.

citation count

  • 70

complete list of authors

  • Gericke, A||Qin, C||Sun, Y||Redfern, R||Redfern, D||Fujimoto, Y||Taleb, H||Butler, WT||Boskey, AL

publication date

  • April 2010