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Phosphoprotein modulation of apatite crystallization

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Summary

Several phosphoprotein preparations (phosvitin, rat incisor and fetal calf molar dentin phosphoproteins) all inhibit apatite growth/replication from pre-existing crystal seeds in metastable solutions. Two stages of the crystal growth process were inhibited by these phosphoproteins. First, an initial lag period was induced, probably associated with seed surface phenomena. This period was prolonged indefinitely when a combination of phosphoprotein precoated seeds was used together with soluble phosphoproteins in the crystal growth reaction. Second, the phosphoproteins prolonged that stage of the reaction where octacalcium phosphate is the predominant mineral phase present prior to its conversion to the final apatite product. Pretreatment of the phosphoproteins with calcium diminished their inhibitory activity to seeded crystal growth as well as towards de novo apatite formation in synthetic extracellular fluids. The presence of collagen diminished the inhibitory activity of the phosphoproteins towards de novo precipitation but had no effect on phosphoprotein-modulated apatite crystal growth in the seeded systems. These results suggest a potential regulatory role for phosphoproteins in dentin mineralization.

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References

  1. Schour, I., Massler, M.: The teeth. In E.J. Farris, J.Q. Griffith (eds.): The Rat in Laboratory Investigation, pp. 104–165. J.B. Lippincott Co., Philadelphia, 1942

    Google Scholar 

  2. Veis, A., Perry, A.: The phosphoprotein of dentin matrix, Biochemistry6:2409–2416, 1967

    Article  PubMed  CAS  Google Scholar 

  3. Veis, A., Spector, A.R., Zamoscianyk, H.: The isolation of an EDTA soluble phosphoprotein from mineralizing dentin, Biochim. Biophys. Acta257:404–413, 1972

    PubMed  CAS  Google Scholar 

  4. Butler, W.T., Finch, J.E., Jr., DeSteno, C.V.: Chemical character of proteins in rat incisors, Biochim. Biophys. Acta257:161–171, 1972

    Google Scholar 

  5. Lee, S.L., Veis, A., Glonek, T.: Dentin phosphoprotein: an extracellular calcium binding protein, Biochemistry16:2971–2979, 1977

    Article  PubMed  CAS  Google Scholar 

  6. DeSteno, C.V., Feagin, F., Butler, W.T.: Mineralization of dentin, bone and tendonin vitro, Calcif. Tissue Res.17:161–163, 1975

    PubMed  CAS  Google Scholar 

  7. Nawrot, C.F., Campbell, D.J., Schroeder, J.K., Van Valkenbourg, M.: Dentin phosphoprotein-induced formation of hydroxylapatite duringin vitro synthesis of amorphous calcium phosphate, Biochemistry15:3445–3449, 1976

    Article  PubMed  CAS  Google Scholar 

  8. Termine, J.D., Conn, K.M.: Inhibition of apatite formation by phosphorylated metabolites and macromolecules, Calcif. Tissue Res.22:149–157, 1976

    Article  PubMed  CAS  Google Scholar 

  9. Bernardi, G.: Chromatography of proteins on hydroxyapatite, Methods Enzymol22:325–339, 1971

    Article  CAS  Google Scholar 

  10. Moreno, E.C., Varughese, K., Hay, D.I.: Effect of human salivary proteins on the precipitation kinetics of calcium phosphate, Calcif. Tissue Int.28:7–16, 1979

    PubMed  CAS  Google Scholar 

  11. Termine, J.D., Eanes, E.D.: Calcium phosphate deposition from balanced salt solutions, Calcif. Tissue Res.15:81–84, 1974

    Article  PubMed  CAS  Google Scholar 

  12. Eanes, E.D.: The influence of fluoride on the seeded growth of apatite from stable supersaturated solutions at pH 7.4, J. Dent. Res.59:144–150, 1980

    PubMed  CAS  Google Scholar 

  13. Williams, B.R., Gelman, R.A., Poppke, D.C., Piez, K.A.: Collagen fibril formation: optimalin vitro conditions and preliminary kinetic results, J. Biol. Chem.253:6578–6585, 1978

    PubMed  CAS  Google Scholar 

  14. Termine, J.D., Torchia, D.A., Conn, K.M.: Enamel matrix: structural proteins. In M.U. Nylen, J.D. Termine (eds.): Proceedings, Third International Symposium on Tooth Enamel, pp. 773–778. J. Dent. Res.58B (AADR), Washington, D.C., 1979

  15. Eanes, E.D.: The interaction of supersaturated calcium phosphate solutions with apatitic substrates, Calcif. Tissue Res.20:75–89, 1976

    PubMed  CAS  Google Scholar 

  16. Weinstock, M., Leblond, C.P.: Radioautographic visualization of the deposition of a phosphoprotein at the mineralization front in the dentin of the rat incisor, J. Cell Biol.56:838–845, 1973

    Article  PubMed  CAS  Google Scholar 

  17. Grizzuti, K., Perlmann, G.E.: Binding of magnesium and calcium ions to the phosphoglycoprotein phosvitin, Biochemistry12:4399–4403, 1973

    Article  PubMed  CAS  Google Scholar 

  18. Glimcher, M.J.: Phosphopeptides of enamel matrix. In M.U. Nylen, J.D. Termine (eds.): Proceedings, Third International Symposium on Tooth Enamel, pp. 790–806. J. Dent. Res.58B (AADR), Washington, D.C. 1979

  19. Schlueter, R.J., Veis, A.: The macromolecular organization of dentin matrix collagen. II. Periodate degradation and carbohydrate cross-linking, Biochemistry3:1657–1665, 1964

    Article  PubMed  CAS  Google Scholar 

  20. Carmichael, D.J., Veis, A., Wang, E.T.: Dentin matrix collagen: evidence for a covalently linked phosphoprotein attachment, Calcif. Tissue Res.7:331–334, 1971

    Article  PubMed  CAS  Google Scholar 

  21. Curley-Joseph, J., Veis, A.: The nature of the covalent complexes of phosphoproteins with collagen in the bovine dentin matrix, J. Dent. Res.58:1625–1633, 1979

    PubMed  CAS  Google Scholar 

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Termine, J.D., Eanes, E.D. & Conn, K.M. Phosphoprotein modulation of apatite crystallization. Calcif Tissue Int 31, 247–251 (1980). https://doi.org/10.1007/BF02407188

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  • DOI: https://doi.org/10.1007/BF02407188

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