title: Protein-to-protein interactions: criteria defining the assembly of the enamel organic matrix.
abstract: 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.
authors.affiliation: University of Southern California, School of Dentistry, Center for Craniofacial Molecular Biology, Los Angeles 90033, USA.
authors.forename: M L
authors.initials: ML
authors.lastname: Paine
authors.forename: P H
authors.initials: PH
authors.lastname: Krebsbach
authors.forename: L S
authors.initials: LS
authors.lastname: Chen
authors.forename: C T
authors.initials: CT
authors.lastname: Paine
authors.forename: Y
authors.initials: Y
authors.lastname: Yamada
authors.forename: D
authors.initials: D
authors.lastname: Deutsch
authors.forename: M L
authors.initials: ML
authors.lastname: Snead
mesh_terms: D000566:Amelogenesis; D053523:Amelogenin; D015153:Blotting, Western; D002113:Calcification, Physiologic; D003460:Crystallization; D003746:Dental Enamel Proteins / Q000096:biosynthesis* / Q000737:chemistry; D005109:Extracellular Matrix / Q000378:metabolism; D016326:Extracellular Matrix Proteins / Q000096:biosynthesis* / Q000737:chemistry; D006801:Humans; D011485:Protein Binding; D011487:Protein Conformation; D011499:Protein Processing, Post-Translational; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis; D001616:beta-Galactosidase / Q000378:metabolism
chemical_list: C490889:AMBN protein, human; D053523:Amelogenin; D003746:Dental Enamel Proteins; D016326:Extracellular Matrix Proteins; D011993:Recombinant Fusion Proteins; C038456:tuftelin; D001616:beta-Galactosidase