EVIDENCE FOR AMELOGENIN NANOSPHERES AS FUNCTIONAL COMPONENTS OF SECRETORY-STAGE ENAMEL MATRIX

EVIDENCE FOR AMELOGENIN NANOSPHERES AS FUNCTIONAL COMPONENTS OF SECRETORY-STAGE ENAMEL MATRIX
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DOI:
10.1006/jsbi.1995.1029
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发表时间:
1995-07-01
影响因子:
3
通讯作者:
SLAVKIN, HC
SLAVKIN, HC
中科院分区:
生物学3区
文献类型:
--
作者:
FINCHAM, AG;MORADIANOLDAK, J;SLAVKIN, HC

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Amelogenins are the principal proteins of the extracellular matrix of developing dental enamel and are postulated to function in the processes of biomineralization of the developing tooth although the molecular mechanisms concerned are poorly understood. Recent imaging studies, employing dynamic light scattering, atomic force, and transmission electron microscopy (TEM) have shown that a recombinant amelogenin (M(r) similar to 20 000 Da) spontaneously forms supramolecular quasi-spherical aggregates (''nanospheres'') of 15-20 nm in diameter. By comparison with in vitro experiments employing the recombinant amelogenin we show that the nanospheres appear as electron-lucent structures when treated with conventional electron microscopy contrast reagents (phosphotungstate or uranyl acetate) and we speculate that this property derives from the hydrophobic nature of the amelogenin protein. Employing TEM preparations, developing enamel from mouse, bovine, and hamster we demonstrate that the amelogenin nanospheres occur as beaded rows of electron-lucent structures aligned with, and separating, the enamel mineral crystallites. We postulate that the amelogenin monomers self-assemble to form nanospheres which function to space the initial crystallites, control crystal habit, inhibit intercrystalline fusions, and, through the apposition of their surfaces, create anionic channels which facilitate ion transport within the mineralizing matrix. (C) 1995 Academic Press, Inc.