Recent advances in amelogenin biochemistry

This paper reviews advances in amelogenin biochemistry in three areas; (i) amelogenin expression; (ii) amelogenin posttranslational and post-secretory processing, and (iii) amelogenin structure and function. Recent studies of amelogenin expression(1,2) have demonstrated that alternative-splicing of mouse amelogenin RNA generates seven distinct mRNAs, coding for amelogenin proteins from 194 to 44 amino acid residues in length. A polyclonal antibody to a sequence of the 194-residue murine amelogenin identified this protein in vivo. While several studies have reported that amelogenins are post translationally phosphorylated, it has proved difficult to confirm this view-h?ass spectrometry studies of bovine and porcine TRAP and LRAP amelogenins have established a phosphoserine residue at position-16 as originally reported by Takagi et al.(3) for a 180-residue bovine amelogenin. Also, we discovered that the detailed mechanism(s) of carboxy terminal amelogenin proteolytic processing appear different than previously reported.(4) In terms of amelogenin structure, it is well known that amelogenins form aggregated structures. Studies employing a recombinant amelogenin and dynamic light-scattering instrumentation demonstrated aggregate structures of 15-20 nm in radius, corresponding to a mass of 2-3 million daltons. Imaging these aggregates by transmission electron and atomic force microscopy Suggested that these structures are equivalent to the ''stippled'' or ''granular'' material seen in electron photomicrographs of developing enamel. Collectively, these advances in amelogenin biochemistry lead to a new view of amelogenin structure, processing and functions in enamel biomineralization.