Characterization of two distinctly different mineral-related proteins from the teeth of the Camarodont sea urchin Lytechinus variegatus: Specificity of function with relation to mineralization.
The majority of the mineral phase of the Lytechinus variegatus tooth is comprised of magnesium containing calcite crystal elements, collectively arranged so that they appear as a single crystal under polarized light, as well as under X-ray or electron irradiation. However, the crystal elements are small, and in spite of the common alignment of their crystal axes, are not the same size or shape in different parts of the tooth. The toughness of the tooth structure arises from the fact that it is a composite in which the crystals are coated with surface layers of organic matter that probably act to inhibit crack formation and elongation. In the growth region the organic components represent a greater part of the tooth structure. In the most heavily mineralized adoral region the primary plates fuse with inter-plate pillars. Using Scanning Electron Microscopy; TOF-SIMS mapping of the characteristic amino acids of the mineral related proteins; and isolation and characterization of the mineral-protected protein we report that the late-forming inter-plate pillars had more than a three-fold greater Mg content than the primary plates. Furthermore, the aspartic acid content of the mineral-related protein was highest in the high Mg pillars whereas the mineral-protected protein of the primary plates was richer in glutamic acid content.These results suggest that the Asp-rich protein(s) is important for formation of the late developing inter-plate pillars that fuse the primary plates and increase the stiffness of the most mature tooth segment. Supported by NIDCR Grant DE R01-01374 to AV.
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Department of Cell and Molecular Biology, Feinberg School of Medicine, Northwestern University, Chicago, IL 60611, USA.
Alvares
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Dixit
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Robach
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Stock
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