Abstract

The aim of this study was to investigate the relationship between proteoglycans (PGs) and collagen fibrils at the early mineralization process of mantle dentin. Ten first molar dental germs of rats were removed and fixed in glutaraldehyde/formaldehyde in cacodylate buffer and post-fixed in osmium tetroxide. The samples were dehydrated and embedded in epoxy resin. Ultrathin sections were contrasted and analyzed in TEM before and after treatment with EDTA, chondroitinases AC and ABC. After EDTA treatment, a electrondense substance associated with collagen fibril was removed, and did not stain again. A high magnification of these areas showed globular structures with 15 nm diameter surrounding collagen fibrils. In advanced mineralization areas, collagen fibrils showed a banded pattern and at high magnification the fibrils presented a light 10 nm ring inside and a dark 10 nm ring outside. After chondroitinase treatment, the electrondense substance associated with collagen fibrils was removed, showing a banded pattern of clear and dark areas along them. From morphological data, the authors proposed a model of interaction between PGs and collagen fibrils, where glicosaminoglycans chains are inside the fibrils, while the protein core remains outside. That stereochemical arrangement would start the crystal nucleation.

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