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- W2898023743 abstract "Extracellular matrix of bone and dentin is highly complex and involves a dynamic process of deposition and removal. Cells are the main architect that build this designer matrix that is highly specialized to calcified tissues. Osteoblasts or odontoblasts secrete both collagen and noncollagenous proteins in a temporal and spatial manner. Type I collagen self-assembles and forms a fabric-like template onto which noncollagenous proteins and mineral bind in a well-regulated manner. Dentin matrix protein 1 (DMP1) is one such noncollagenous protein that contains several acidic groups that can bind calcium ions which in turn binds phosphate and initiates the calcification process. In this study, we demonstrate that DMP1 is localized at specific sites on the self-assembled collagen matrix of dentin. In vitro nucleation studies on demineralized and deproteinized dentin slice adsorbed with DMP1 show bundles of well-ordered needle-shaped nanohydroxyapatite deposited on the dentin matrix. The nucleated mineral structures had uniform length and width and their long axis was oriented parallel to the collagen fibril axis. Overall, the physiologically self-assembled collagen and DMP1 mediated ordered deposition of nanocrystalline HAP." @default.
- W2898023743 created "2018-10-26" @default.
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- W2898023743 date "2018-01-01" @default.
- W2898023743 modified "2023-10-16" @default.
- W2898023743 title "DMP1 Binds Specifically to Type I Collagen and Regulates Mineral Nucleation and Growth" @default.
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- W2898023743 doi "https://doi.org/10.1007/978-981-13-1002-7_15" @default.
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