Expression of Spicule Matrix Proteins in the Sea Urchin Embryo during Normal and Experimentally Altered Spiculogenesis

• Published in: Developmental biology Vol. 225; no. 1; pp. 201 - 213
• Main Authors: Urry, Lisa A., Hamilton, Patricia C., Killian, Christopher E., Wilt, Fred H.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.09.2000
• Subjects: Animals; biomineralization; Cytoskeletal Proteins - physiology; Embryo, Nonmammalian - physiology; Extracellular Matrix Proteins; Gene Expression Regulation, Developmental - physiology; sea urchin; Sea Urchins - embryology; Sea Urchins - physiology; Space life sciences; spicule; Strongylocentrotus purpuratus; biomineralization; spicule; sea urchin; Non-programmatic
• ISSN: 0012-1606; 1095-564X
• DOI: 10.1006/dbio.2000.9828

During its embryonic development, the sea urchin embryo forms an endoskeletal calcitic spicule. This instance of biomineralization is experimentally accessible and also offers the advantage of occurring within a developmental context. Here we investigate the time course of appearance and localization of two proteins among the four dozen that constitute the protein matrix of the skeletal spicule. SM50 and SM30 have been studied in some detail, and polyclonal antisera have been prepared against them (C. E. Killian and F. H. Wilt, 1996, J. Biol. Chem. 271, 9150–9159). Using these antibodies we describe here the localization and time course of accumulation of these two proteins in Strongylocentrotus purpuratus, both in the intact embryo and in micromere cultures. We also investigate the disposition of the matrix proteins, SM50, SM30, and PM27, in the three-dimensional spicule by studying changes in protein localization during experimental manipulation of isolated skeletal spicules. We conclude that SM50, PM27, and SM30 probably play different roles in biomineralization, based on their localization and patterns of expression. It is unlikely that these proteins are solely structural elements within the mineral. SM50 and PM27 may play a role in defining the extracellular space in which spicule deposition occurs, while SM30 may play a role in secretion of spicule components. Finally, we report on the effects of serum on expression of some primary mesenchyme-specific proteins in micromere cultures; withholding serum severely depresses accumulation of SM30 but has only modest effects on the accumulation of other proteins.