A western-blotting study of enamel glycoproteins in rat experimental fluorosis

Experimental fluorosis was induced in order to get information on enamel protein glycosylation, using Western-blotting methodology with peroxidase-labelled concanavalin A. Fluoride inhibited amelogenin degradation, especially the production of intermediate forms. Within the non-amelogenin family of proteins there were changes in both the conventionally stainable components and the glycoconjugates revealed by lectin only. Fluoride influenced the whole extracellular processing of enamel proteins including movement between the mineral and non-mineral compartments. A different degradation scheme of enamel proteins, which also affects the glycoconjugates, might be of importance in the properties of the fluorosed enamel surface and its interactions with the oral environment.