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Micelle Structure of Amelogenin in Porcine Secretory Enamel

Department of Biochemistry and Anatomy,
¹ School of Dental Medicine, Tsurumi University, 2-1-3 Tsurumi, Tsurumi-ku, Yokohama 230-8501, Japan

^* corresponding author, fukae-m{at}tsurumi-u.ac.jp

Even during the secretory stage of amelogenesis, enamel crystals thicken as amelogenins (the major protein component) decrease. To explain this phenomenon, we propose a model for amelogenin structure and function based upon the hypothesis that amelogenin forms micelles. Solubility and hydrophobicity analyses suggest that all but the hydrophilic amelogenin C-terminal regions aggregate via hydrophobic bonds to form a micelle core. Amelogenin micelles may form super-assemblies via their C-termini (KTKREEVD), which contain complementary positive (KTKR) and negative (EEVD) elements. Disassembly of the micelles through controlled proteolysis provides space for crystal growth. Initial cleavage (by enamelysin) removes the surface-accessible amelogenin C-terminus, exposing the middle portion to cleavage (by EMSP1). As a result, the 13-kDa amelogenin, a rod-shaped domain based upon ultrafiltration and transmission electron microscopy studies, is released. This model explains how amelogenin is able to ‘space’ and support the ribbon-like crystals and continuously yield space as the crystals thicken, until they are sufficiently mature to support themselves. Abbreviations: dentino-enamel junction (DEJ), sodium dodecyl sulfate (SDS), polyacrylamide gel electro phoresis (PAGE), transmission electron microscope (TEM).

KEY WORDS: amelogenin • rod-like structure • hydrophobicity • micelle structure • aggregation