Abstract
Recent studies have highlighted the potential role of the metalloproteinase enamelysin (MMP-20) in controlling some of the most critical stages during enamel development. This study was aimed to assess the selectivity of enamelysin to the three most abundant cleavage sites on the amelogenin sequence, and to gain insight into the factors that control the pattern of amelogenin processing during enamel mineralization. Three deca-peptides with sequences based on pig amelogenin and including the proteolytic cleavage sites W/L, S/M, and P/A were synthesized as substrates. Statistical analysis revealed no significant differences in the rates of cleavage among the three peptides, indicating comparable selectivity of enamelysin for these peptide bonds. Considering the selective appearance of amelogenin proteolytic products, we suggest that amelogenin folding and assembly are the primary factors in controlling the pattern of its proteolysis during the secretory stage of enamel development.
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