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Protein-to-Protein Interactions: Criteria Defining the Assembly of the Enamel Organic Matrix

University of Southern California, School of Dentistry, Center for Craniofacial Molecular Biology, 2250 Alcazar Street, CSA Room 142, Los Angeles, California 90033

P.H. Krebsbach

The University of Michigan, School of Dentistry, Room 4207, Ann Arbor, Michigan 48109-1078

L.S. Chen

University of Southern California, School of Dentistry, Center for Craniofacial Molecular Biology, 2250 Alcazar Street, CSA Room 142, Los Angeles, California 90033

C.T. Paine

University of Southern California, School of Dentistry, Center for Craniofacial Molecular Biology, 2250 Alcazar Street, CSA Room 142, Los Angeles, California 90033

Y. Yamada

Laboratory of Craniofacial Developmental Biology and Regeneration, National Institute of Dental Research, National Institutes of Health, Bethesda, Maryland 20892

D. Deutsch

Dental Research Unit, Hebrew University, Hadassah Faculty of Dental Medicine, Jerusalem, Israel

M.L. Snead

University of Southern California, School of Dentistry, Center for Craniofacial Molecular Biology, 2250 Alcazar Street, CSA Room 142, Los Angeles, California 90033

Enamel crystallites form in a protein matrix located proximal to the ameloblast cell layer. This unique organic extracellular matrix is constructed from structural protein components biosynthesized and secreted by ameloblasts. To date, three distinct classes of enamel matrix proteins have been cloned. These are the amelogenins, tuftelin, and ameloblastin, with recent data implicating ameloblastin gene expression during cementogenesis. The organic enamel extracellular matrix undergoes assembly to provide a three-dimensional array of protein domains that carry out the physiologic function of guiding enamel hydroxyapatite crystallite formation. Using the yeast two-hybrid system, we have surveyed these three known enamel gene products for their ability to direct self-assembly. We measured the capacity of the enamel gene products to direct protein-to-protein interactions, a characteristic of enamel proteins predicated to be required for self-assembly. We provide additional evidence for the self-assembly nature of amelogenin and tuftelin. Ameloblastin self-assembly could not be demonstrated, nor were protein-to-protein interactions observed between ameloblastin and either amelogenin or tuftelin. Within the limits of the yeast two-hybrid assay, these findings constrain the emerging model of enamel matrix assembly by helping to define the limits of enamel matrix protein-protein interactions that are believed to guide enamel mineral crystallite formation.

Key Words: amelin • ameloblastin • amelogenin • biomineralization • enamel • enamelin • protein matrix assembly • sheathlin • tooth development • tuftelin • yeast two-hybrid system • protein interactions.

Journal of Dental Research, Vol. 77, No. 3, 496-502 (1998)
DOI: 10.1177/00220345980770030901


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