期刊
MATRIX BIOLOGY
卷 20, 期 5-6, 页码 293-305出版社
ELSEVIER
DOI: 10.1016/S0945-053X(01)00154-8
关键词
enamel biomineralization; amelogenin assembly; enamel proteases; octacalcium phosphate; hydroxy apatite
资金
- NIDCR NIH HHS [DE02848, DE12350] Funding Source: Medline
The remarkable properties of enamel crystals and their arrangements in an extraordinary micro-architecture are clear indications that the processes of crystal nucleation and growth in the extracellular matrix are highly controlled. The major extracellular events involved in enamel formation are: (a) delineation of space by the secretory ameloblasts and the dentino-enamel junction; (b) self-assembly of amelogenin proteins to form the supramolecular structural framework; (c) transportation of calcium and phosphate ions by the ameloblasts resulting in a supersaturated solution; (d) nucleation of apatite crystallites; and (c) elongated growth of the crystallites. Finally, during the 'maturation' step, rapid growth and thickening of the crystallites take place, which is concomitant with progressive degradation and eventual removal of the enamel extracellular matrix components (mainly amelogenins). This latter stage during which physical hardening of enamel occurs is perhaps unique to dental enamel. We have focused our in vitro studies on three major extracellular events: matrix assembly, matrix processing and control of crystal growth. This paper summarizes current knowledge on the assembly, processing and effect on crystal morphology by amelogenin proteins. The correlation between these three events and putative functional roles for amelogenin protein are discussed. (C) 2001 Elsevier Science B.V./International Society of Matrix Biology. All rights reserved.
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