Degradation of enamelins by proteinases found in porcine secretory enamel in vitro

Arch Oral Biol. 1994 Apr;39(4):277-81. doi: 10.1016/0003-9969(94)90117-1.

Abstract

The action of proteinases obtained from porcine secretory enamel on the porcine 89-kDa enamelin was examined in vitro. The results of sodium dodecyl sulphate-acrylamide gel electrophoresis of the reaction products indicated the following. (1) The 76- and 78-kDa proteinases localized in the outermost layer of the secretory enamel not only convert the 25-kDa amelogenin to the 20-kDa amelogenin, but also split the 89-kDa enamelin, which is the major enamelin component in the enamel in the very early secretory stage, into large fragments such as 25-, 41- and 56-kDa enamelins. (2) The serine proteinases localized in the inner layer of secretory enamel further degrade not only amelogenins but also enamelins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amelogenesis
  • Animals
  • Dental Enamel / enzymology
  • Dental Enamel / metabolism*
  • Dental Enamel Proteins / metabolism*
  • Serine Endopeptidases / physiology*
  • Swine

Substances

  • Dental Enamel Proteins
  • tuftelin
  • Serine Endopeptidases