Mapping of magnesium and of different protein fragments in sea urchin teeth via secondary ion mass spectroscopy

J. S. Robach, S. R. Stock*, A. Veis

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

57 Scopus citations

Abstract

Mature portions of sea urchin are comprised of a complex array of reinforcing elements yet are single crystals of high and very high Mg calcite. How a relatively poor structural material (calcite) can produce mechanically competent structures is of great interest. In teeth of the sea urchin Lytechinus variegatus, we recorded high-resolution secondary ion mass spectrometry (SIMS) maps of Mg, Ca,and specific amino acid fragments of mineral-related proteins including aspartic acid (Asp). SIMS revealed strong colocalization of Asp residues with very high Mg. Demineralized specimens showed serine localization on membranes between crystal elements and reduced Mg and aspartic acid signals, further emphasizing colocalization of very high Mg with ready soluble Asp-rich protein(s). The association of Asp with nonequilibrium, very high magnesium calcite provides insight to the makeup of the macromolecules involved in the growth of two different composition calcites and the fundamental process of biomineralization.

Original languageEnglish (US)
Pages (from-to)87-95
Number of pages9
JournalJournal of Structural Biology
Volume155
Issue number1
DOIs
StatePublished - Jul 2006

Keywords

  • Biomineralization
  • Calcite
  • Magnesium
  • Proteins
  • SIMS
  • Sea urchin
  • Tooth

ASJC Scopus subject areas

  • Structural Biology

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