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J. Biol. Chem., Vol. 281, Issue 30, 21173-21182, July 28, 2006

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Altering Biomineralization by Protein Design^*

From the University of Southern California, Center for Craniofacial Molecular Biology, Los Angeles, California 90033

To create a bioceramic with unique materials properties, biomineralization exploits cells to create a tissue-specific protein matrix to control the crystal habit, timing, and position of the mineral phase. The biomineralized covering of vertebrate teeth is enamel, a distinctive tissue of ectodermal origin that is collagen-free. In forming enamel, amelogenin is the abundant protein that undergoes self-assembly to contribute to a matrix that guides its own replacement by mineral. Conserved domains in amelogenin suggest their importance to biomineralization. We used gene targeting in mice to replace native amelogenin with one of two engineered amelogenins. Replacement changed enamel organization by altering protein-to-crystallite interactions and crystallite stacking while diminishing the ability of the ameloblast to interact with the matrix. These data demonstrate that ameloblasts must continuously interact with the developing matrix to provide amelogenin-specific protein to protein, protein to mineral, and protein to membrane interactions critical to biomineralization and enamel architecture while suggesting that mutations within conserved amelogenin domains could account for enamel variations preserved in the fossil record.

Received for publication, October 3, 2005 , and in revised form, May 15, 2006.

^* The work was supported by United States Public Health Service, NIDCR, National Institutes of Health Grants DE 13045 (to M. L. S.) and DE13404 (to M. L. P.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Figs. 1-4 and Table 1.

¹ To whom correspondence should be addressed: University of Southern California, Center for Craniofacial Molecular Biology, 2250 Alcazar St., CSA 142, Los Angeles CA 90033. Tel.: 323-442-3178; Fax: 323-442-2981; E-mail: mlsnead{at}usc.edu.

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