Altering biomineralization by protein design

doi:10.1074/jbc.M510757200

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Papers In Press, published online ahead of print May 17, 2006
J. Biol. Chem, 10.1074/jbc.M510757200
Submitted on October 3, 2005
Revised on May 15, 2006
Accepted on May 17, 2006

Altering biomineralization by protein design

DanHong Zhu, Michael L. Paine, Wen Luo, Pablo Bringas . Jr, and Malcolm L. Snead

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

Corresponding Author: mlsnead{at}usc.edu

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.

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