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Dentin proteins: chemistry, structure and biosynthesis.

W T Butler, E C Munksgaard, W S Richardson

    Journal of Dental Research
    |March 1, 1979
    PubMed
    Summary
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    Dentin phosphoprotein, abundant in aspartic acid, binds calcium and associates with collagen. This protein

    Area of Science:

    • Biochemistry
    • Biomineralization
    • Dental Research

    Background:

    • Dentin is a mineralized tissue comprising an organic matrix and hydroxyapatite crystals.
    • Noncollagenous proteins play crucial roles in dentin formation and mineralization.
    • Dentin phosphoprotein (DPP) is a major noncollagenous protein in dentin.

    Purpose of the Study:

    • To investigate the properties and localization of dentin phosphoprotein.
    • To elucidate the role of DPP in the dentin mineralization process.

    Main Methods:

    • Biochemical analysis of dentin phosphoprotein.
    • Radioautographic studies to track protein transport and binding.
    • Characterization of soluble and inextractable forms of DPP.

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    Main Results:

    • Dentin phosphoprotein is rich in aspartic acid and phosphoserine.
    • DPP exists in soluble and inextractable forms, with the latter bound to the collagen matrix.
    • DPP exhibits high calcium-binding capacity.
    • Biosynthetic and radioautographic data indicate DPP transport and binding to collagen at the predentin-dentin junction.

    Conclusions:

    • Dentin phosphoprotein is a key molecule in dentin mineralization.
    • The binding of DPP to collagen at the predentin-dentin junction is crucial for calcium binding and subsequent mineralization.
    • Other glycoproteins may also contribute to the dentin mineralization process.