To determine the role of amelogenin in the mineralization of dental enamel,
the effects of the recombinant mouse amelogenin rM179 on in vitro hydroxya
patite formation have been studied. In a steady-state agarose gel assay for
hydroxyapatite nucleation, rM179 lacked significant activity at concentrat
ions up to 300 mu g/ml. In an autotitration assay for inhibition of de novo
hydroxyapatite formation, rM179 had no significant activity at concentrati
ons up to 30 mu g/ml. Using selected-area dark-field electron microscopy, i
t was shown that rM179, at concentrations up to 30 mu g/ml, did not signifi
cantly affect the length of hydroxyapatite crystals formed in steady-state
agarose gels. These findings suggest that amelogenins do not possess the sp
ecific crystal-modulating properties characteristic of certain acidic miner
alized tissue proteins proteins.