Elucidation of onset mechanism of amelogenesis imperfecta (AI) using a biomineralization model

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The purpose of this study was to investigate the effects of mutation of amelgenin, an enamel matrix protein, on the enamel crystal formation, and to elucidate of onset mechanism of amelogenesis imperfecta (AI).Wild-type recombinant human full-length amelogenin and mutated recombinant human full-length ameogenin (P41T) were synthesized. There was a difference in the aggregation ability in solution at neutral pH (pH 7.4) between the wild-type and mutated full-length amelogenins. In addition, recombinant human MMP20 wa synthesized, and the digestion of recombinant human full-length amelogenin by the MMP20 was investigated. The digestion of mutated recombinant human full-length amelogenin was delayed as compared with that in wild-type amelogenin.From these results, it was strongly suggested that a mutation of amelogenin may induce the abnormality of enamel structure during tooth formation.