Elucidation of the mechanism of biomineralization with acidic phosphoprotein from molecular evolution studies

点击翻译按钮获取中文摘要

Dentin matrix protein 1(DMP1), which is a one of the acidic phosphoproteins composed of the bone. Molecular evolution study of DMP1 indicated that phosphorylation by casein kinase(CK) might be related to the DMP1 function. Highly phosphorylated DMP1 by CK has a large number of acidic domains. Because of its highly acidic nature, it is supposed that negative-charged DMP1 can bind to calcium, thereby regulating matrix mineralization. In this study, we found that Ser residues of DMP1 were phosphorylated in the bone and cultured osteoblast and that osteoblast-derived CK might phosphorylate DMP1. Culture experiment with CK inhibitor indicated that mineralization was controlled by inhibition of the CK activity. Therefore, it was supposed when DMP1 was phosphorylated by CK, and did negative-charged DMP1 promoted mineralization.