Degradation of enamel matrix proteins in porcine secretory enamel.

To elucidate the progressive disappearance of 25 kDa amelogenin occurring in a narrow space near the surface of enamel, the alkaline soluble fraction which contained 80% of the total proteins was extracted from a newly formed porcine enamel. When this fraction was incubated with the addition of Ca ions in an in vitro system, the degradation of the coexisting amelogenin and enamelin occurred without activation during the incubation period. Although the fraction contained mainly two kinds of metalloproteinases, 56 kDa and 61 kDa gelatinolytic, and 41 kDa and 46 kDa caseinolytic activities, it was demonstrated on amelogenin enzymography that the caseinolytic one was concerned with the conversion of the 25 kDa amelogenin into the 20 kDa amelogenin. The protein distribution of the newly formed enamel indicated that the metalloproteinases degraded the coexisting enamelin and amelogenin imperfectly. Nevertheless, during the next developing stage they demonstrated their full activities. It is suspected that these activities are regulated by Ca ions, which may be increased by a cascade system.