Mineral-matrix interactions in bone and dentin

Abstract

The bone, dentin, and cementum of the mature individual are comprised from a dense collagenous fiber network into which the carbonate-apatite mineral phase is deposited. It is hypothesized that a set of collagen-interactive acidic phosphoproteins are secreted by the osteoblasts, odontoblasts, and cementoblasts into the preformed collagenous matrix. These proteins then interact specifically with the collagen and nucleate apatite formation on and within the fibrils. These phosphoproteins may also regulate the morphology, rate of growth, and stability of the mineral phase crystals. The acidic matrix phosphoproteins may thus be considered as the crucial regulators of mineralization and tissue stability. In the dentin system, these regulatory proteins are synthesized, posttranslationally modified, and secreted in vesicles different from the collagen secretory vesicles. Mineralization occurs as the regulatory proteins are deposited on the preformed fibrils. This model requires testing in the bone system. In dentin, in the absence of tissue turnover, the resident phosphoproteins are degraded in situ over time, perhaps changing the properties of the tissue. Regulation of synthesis, secretory pathways and retention of integrity within the matrix are thus important areas for further investigation.