Molecular diversity and interaction of the enamel protein in the odontogenesis.

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Enamel proteins, such as amelogenins and sheath proteins, have several isoforms produced by alternative splicing of mRNAs. In order to clarify the role of molecular diversities and their interactions in the development of the tooth germ, we have developed region specific antibodies which recognize specific molecular forms. Enamel organ and immature enamel matrix from the tooth germs of the mouse and incisors of the rat were analyzed by means of immunochemistry and immunohistochemistry. The results are summarized as follows.1.Differentiating ameloblasts of the developing murine tooth germ expressed low molecular weight sheath protein (near 35kDa) in the early stage, while those in the late differentiation stage and the secretory ameloblast expressed 55kDa and 65kDa sheath proteins.2.Growing end or the rat incisor expressed 33 kDa and 36 kDa sheath protein besides 55 kDa and 65 kDa ones, all of which except for 65 kDa protein increased after the treatment of the rat with Brefeldin A.3.Differentiating odontoblast facing inner enamel epithelium, early stage of differentiating ameloblast, and fibroblast like cells near the young odontoblast were stained with C-terminal specific sheath protein antibody but not with N terminal specific one, suggesting that these cell might express 33kDa and 36kDa sheath protein.4.Differentiating ameloblasts with intact basal lamina expressed sheath protein.