Amelotin-Mediated Crystals Assembly in Liquid-Phase and on Tooth Surface
- 1 School of Medicine, University of Electronic Science and Technology of China, Chengdu, China
- 2 School of Medicine, University of Electronic Science and Technology of China, Chengdu, China
- 3 School of Medicine, University of Electronic Science and Technology of China, Chengdu, China
- 4 School of Medicine, University of Electronic Science and Technology of China, Chengdu, China
Abstract
Objectives: To study the role of amelotin in enamel formation, purified recombinant human amelotin was used in a study of amelotin self assembly and its role in new HAP crstal structure formation in a laboratory setting. Methods: The full-length human amelotin gene was cloned from developing tooth buds and recombinant amelotin was expressed and purified. Morphological changes during amelotin self-assembly and the role of amelotin in promoting new minieralization structure is studied using Transmission electronic microscopy and Scanning electron microscopy. Results: The measured molecular weight of expressed human amelotin was 28 kDa that matches the predicted values. Amelotin self-assembles to form nano-spheres 10 - 30 nm in size. The amelotin self-assembly process further produces higher 3-D structure in the forms of chain-like fabric arranged in parallel and perpendicular direction. The neonatal pearl crystals were arranged side by side to form a string of small rods and small parallel rods extend from the demineralized glaze on the surface of teeth that were pre-treated with amelotin.
- Chun, K., Choi, H. and Lee, J. (2014) Comparison of Mechanical Property and Role between Enamel and Dentin in the Human Teeth. Journal of Dental Biomechanics, 5. https://doi.org/10.1177/1758736014520809
- Chen, H., Clarkson, B.H., Sun, K. and Mansfield, J.F. (2005) Self-Assembly of Synthetic Hydroxyapatite Nanorods into an Enamel Prism-Like Structure. Journal of Colloid and Interface Science, 288, 97-103. https://doi.org/10.1016/j.jcis.2005.02.064
- Koto, W., Shinohara, Y., Kitamura, K., Wachi, T., Makihira, S. and Koyano, K. (2017) Porcine Dental Epithelial Cells Differentiated in a Cell Sheet Constructed by Magnetic Nanotechnology. Nanomaterials (Basel, Switzerland), 7, 322. https://doi.org/10.3390/nano7100322
- Yamazaki, H., Beniash, E., Yamakoshi, Y., Simmer, J.P. and Margolis, H.C. (2017) Protein Phosphorylation and Mineral Binding Affect the Secondary Structure of the Leucine-Rich Amelogenin Peptide. Frontiers in Physiology, 8, 450. https://doi.org/10.3389/fphys.2017.00450
- Margolis, H.C., Kwak, S.Y. and Yamazaki, H. (2014) Role of Mineralization Inhibitors in the Regulation of Hard Tissue Biomineralization: Relevance to Initial Enamel Formation and Maturation. Frontiers in Physiology, 5, 339. https://doi.org/10.3389/fphys.2014.00339
- Gibson, C.W., Yuan, Z.A., Hall, B., Longenecker, G., Chen, E., Thyagarajan, T., Sreenath, T., Wright, J.T., Decker, S., Piddington, R., Harrison, G. and Kulkarni, A.B. (2001) Amelogenin-Deficient Mice Display an Amelogenesis Imperfecta Phenotype. The Journal of Biological Chemistry, 276, 31871–31875. https://doi.org/10.1074/jbc.M104624200
- Hu, J.C., Hu, Y., Smith, C.E., McKee, M.D., Wright, J.T., Yamakoshi, Y., Papagerakis, P., Hunter, G.K., Feng, J.Q., Yamakoshi, F. and Simmer, J.P. (2008) Enamel Defects and Ameloblast-Specific Expression in Enam Knock-Out/Lacz Knock-In Mice. The Journal of Biological Chemistry, 283, 10858-10871. https://doi.org/10.1074/jbc.M710565200
- Wazen, R.M., Moffatt, P., Zalzal, S.F., Yamada, Y. and Nanci, A. (2009) A Mouse Model Expressing a Truncated Form of Ameloblastin Exhibits Dental and Junctional Epithelium Defects. Matrix Bi-ology: Journal of the International Society for Matrix Biology, 28, 292-303. https://doi.org/10.1016/j.matbio.2009.04.004