title: A post-classical theory of enamel biomineralization… and why we need one.
abstract: Enamel crystals are unique in shape, orientation and organization. They are hundreds of thousands times longer than they are wide, run parallel to each other, are oriented with respect to the ameloblast membrane at the mineralization front and are organized into rod or interrod enamel. The classical theory of amelogenesis postulates that extracellular matrix proteins shape crystallites by specifically inhibiting ion deposition on the crystal sides, orient them by binding multiple crystallites and establish higher levels of crystal organization. Elements of the classical theory are supported in principle by in vitro studies; however, the classical theory does not explain how enamel forms in vivo. In this review, we describe how amelogenesis is highly integrated with ameloblast cell activities and how the shape, orientation and organization of enamel mineral ribbons are established by a mineralization front apparatus along the secretory surface of the ameloblast cell membrane.
authors.affiliation: Department of Biologic and Materials Sciences, University of Michigan School of Dentistry, Ann Arbor, MD, USA. jsimmer@umich.edu
authors.forename: James P
authors.initials: JP
authors.lastname: Simmer
authors.forename: Amelia S
authors.initials: AS
authors.lastname: Richardson
authors.forename: Yuan-Yuan
authors.initials: YY
authors.lastname: Hu
authors.forename: Charles E
authors.initials: CE
authors.lastname: Smith
authors.forename: Jan
authors.initials: J
authors.lastname: Ching-Chun Hu
mesh_terms: D000565:Ameloblasts / Q000737:chemistry / Q000166:cytology; D000566:Amelogenesis / Q000502:physiology*; D001485:Basement Membrane / Q000737:chemistry; D003460:Crystallization; D003743:Dental Enamel / Q000737:chemistry*; D003746:Dental Enamel Proteins / Q000378:metabolism; D006801:Humans; D014074:Tooth Calcification
chemical_list: D003746:Dental Enamel Proteins