Different Forms of DMP1 Play Distinct Roles in Mineralization

• DOI: 10.1177/0022034510363250
• Publication Date: 2010-03-04T03:55:07Z
• Authors: A. Gericke; C. Qin; Y. Sun; R. Redfern; D. Redfern; Y. Fujimoto; H. Taleb; W.T. Butler; A.L. Boskey
• Keywords: DMP1

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 growth, while its N-terminal fragment (37K) promotes HA formation. Since there are 3 fragments within the mineralized tissues [N-terminal, C-terminal (57K), chondroitin-sulfate-linked (DMP1-PG)], we predicted that each would have distinct effect on mineralization related to interaction with HA. In gelatin-gel system, 37K 57K were both promoters growth; DMP1-PG was an inhibitor. The secondary structures protein presence absence Ca 2+ determined by FTIR undergoes slight conformational changes binding HA, 37K, 57K, do not change conformation. These findings indicate forms may work collectively controlling process.