The use of autoradiography and cycloheximide to determine the origin of enamel proteins in the maturation ameloblasts of the rat incisor.

Morphological and cytochemical studies have suggested that maturation ameloblasts participate in protein loss by absorbing and degrading enamel proteins as the enamel matures. Several immunocytochemical and autoradiographic studies have suggested other possible explanations for the presence of enamel matrix proteins in maturation ameloblasts. The weakness of these autoradiographic studies is the uncontrolled distribution of systemically injected radioactive amino acids, making it impossible to trace the source of the visualized intracellular isotope. This study used a localized technique to control the targets of the applied isotope and to identify enamel matrix proteins in the maturation ameloblasts with more confidence about their origin. The amount of labelled enamel protein was higher in maturation ameloblasts than transitional ameloblasts. When cycloheximide, a protein-synthesis inhibitor, was applied, there was no effect on the amount of labelled protein in the maturation ameloblasts. These findings support the hypothesis that maturation ameloblasts actively resorb and degrade enamel matrix proteins during enamel formation in the mandibular incisor of the rat.