Effect of apatite crystals on the activity of amelogenin degrading enzymes in vitro.

The objective of the present study was to determine the effect of apatite crystals on the activity of amelogenin degrading enzymes in vitro. Current experimental data, together with previous reports support the view that among the different proteinases present in the enamel extracellular matrix, serine proteinase(s) are responsible for the massive degradation of amelogenins during the maturation stage. For our in-vitro experiments we used the recombinant amelogenin M179 as substrate and a "65%-satd. (NH4)2SO4" fraction of enamel proteins as well as chymotrypsin as sources for serine-proteinase activity. We report preliminary experiments of amelogenin proteolysis in the presence of apatite crystals resulting in a different proteolysis pattern when compared to amelogenin proteolysis without apatite crystals. Quantitative analysis of the HPLC peaks corresponding to the proteolysis products indicates that the presence of apatite crystals in the proteolysis solution inhibits the ability of the serine-proteinases to degrade amelogenin. The present observations support the hypothesis that amelogenin degradation correlates with apatite crystal growth during enamel maturation.