PubMed1996
In order to examine our hypothesis that maturation ameloblasts could degrade the enamel matrix in a manner analogous to bone resorption mediated by osteoclasts, we have assessed the distribution of lysosomal enzymes in the enamel organ by immunolocalizing the cation-in-independent mannose 6-phosphate receptor (MPR) and the lysosomal enzyme cathepsin B at all stages of amelogenesis. Secretory ameloblasts showed strong immunoreactivity for MPR in the supranuclear Golgi region and in the cytoplasm between the Golgi region and the distal junctional complexes. However, cathepsin B immunoreactivity was mainly seen in the distal portion of Tomes' process, which was unreactive for MPR immunogenicity. In maturation ameloblasts, the MPR was observed on the ruffled border of the ruffle-ended ameloblast (RA) but not on the distal cell membrane of the smooth-ended ameloblast (SA), although both cell types demonstrated strong immunoreactivity for MPR in the Golgi region. Immunoreactive cathepsin B was seen at the distal ends of both RA and SA. It is postulated that the nascent lysosomal enzymes bind to the mannose 6-phosphate receptors which target them not only to intracellular lysosomes, but also to the ruffled border of maturation ameloblasts where these enzymes are secreted into the enamel. Since MPR and lysosomal enzymes were also detected on the ruffled border of osteoclasts (Ocl) adjacent to alveolar bone, our immunocytochemical approach provides strong evidence for a similarity between the maturation process in enamel, as mediated by the ruffle-ended maturation ameloblasts, and bone resorption mediated by osteoclasts. This study has established that a common mechanism, based on MPR-targeted lysosomal secretion and matrix degradation, is basic to the maturation process involved in calcified tissues as different as bone and enamel.