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Enamel Matrix Proteins and Ameloblast Biology

1995; Taylor & Francis; Volume: 32; Issue: 1-4 Linguagem: Inglês

10.3109/03008209509013710

1607-8438

D. Deutsch, J. Catalano-Sherman, Leah Dafni, Sasson David, A. Palmon,

Periodontal Regeneration and Treatments

The paper reviews the changes in ameloblast ultrastructure, concomitant with the changes in its functions across the major stages of amelogenesis. It describes the mechanisms associated with the major events in biosynthesis and degradation of the major enamel proteins (amelogenins and tuftelin/enamelins) and with the presecretory and postsecretory mechanisms leading to the heterogeneity of these extracellular matrix proteins. The gene structure, chromosomal localization, protein primary structure and possible function, and the involvement of the different proteins in X-linked (amelogenin) and possibly in autosomally linked (tuftelin) amelogenesis imperfecta, the most common hereditary disease of enamel, are also discussed.