Hostname: page-component-586b7cd67f-2brh9 Total loading time: 0 Render date: 2024-12-03T19:12:55.475Z Has data issue: false hasContentIssue false
  • English
  • Français

Lectin uptake and incorporation into the calcitic spicule of sea urchin embryos

Published online by Cambridge University Press:  15 April 2014

Nancy M. Mozingo
Nancy M. Mozingo*
Affiliation:
Biology Program, California State University, Channel Islands, Camarillo, California, USA
*
1 All correspondence to: Nancy M. Mozingo. Tel: +1 805 437 8989. Fax: +1 805 437 8895. e-mail: [email protected]
Get access Rights & Permissions [Opens in a new window]

Summary

Primary mesenchyme cells (PMCs) are skeletogenenic cells that produce a calcareous endoskeleton in developing sea urchin larvae. The PMCs fuse to form a cavity in which spicule matrix proteins and calcium are secreted forming the mineralized spicule. In this study, living sea urchin embryos were stained with fluorescently conjugated wheat germ agglutinin, a lectin that preferentially binds to PMCs, and the redistribution of this fluorescent tag was examined during sea urchin development. Initially, fluorescence was associated primarily with the surface of PMCs. Subsequently, the fluorescent label redistributed to intracellular vesicles in the PMCs. As the larval skeleton developed, intracellular granular staining diminished and fluorescence appeared in the spicules. Spicules that were cleaned to remove membranous material associated with the surface exhibited bright fluorescence, which indicated that fluorescently labelled lectin had been incorporated into the spicule matrix. The results provide evidence for a cellular pathway in which material is taken up at the cell surface, sequestered in intracellular vesicles and then incorporated into the developing spicule.

Keywords

BlastocoelCalciumPrimary mesenchyme cellsSkeletogenesisWheat germ agglutinin
Type
Short Communication
Information
Zygote , Volume 23 , Issue 3 , June 2015 , pp. 467 - 473
Copyright
Copyright © Cambridge University Press 2014 

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Ameye, L., Hermann, R., Killian, C., Wilt, F. & Dubois, P. (1999). Ultrastructural localization of proteins involved in sea urchin biomineralization. J. Histochem. Cytochem. 47, 1189–200.Google Scholar
Beniash, E., Addadi, L. & Weiner, S. (1999). Cellular control over spicule formation in sea urchin embryos: a structural approach. J. Struct. Biol. 125, 50–62.Google Scholar
Cho, J.W., Partin, J.S. & Lennarz, W.J. (1996). A technique for detecting matrix proteins in the crystalline spicule of the sea urchin embryo. Proc. Natl. Acad. Sci. U.S.A., 93, 1282–6.Google Scholar
Decker, G.L. & Lennarz, W.J. (1988). Skeletogenesis in the sea urchin embryo. Development 103, 231–47.CrossRefGoogle ScholarPubMed
Decker, G.L., Morrill, J.B. & Lennarz, W.J. (1987). Characterization of sea urchin primary mesenchyme cells and spicules during biomineralization in vitro. Development 101, 297–312.Google Scholar
DeSimone, D.W. & Spiegel, M. (1986a). Concanavalin A and wheat germ agglutinin binding to sea urchin embryo basal laminae. Rouxs Arch. Dev. Biol. 195, 433–44.Google Scholar
DeSimone, D.W. & Spiegel, M. (1986b). Wheat germ agglutinin binding to the micromeres and primary mesenchyme cells of sea urchin embryos. Dev. Biol. 114, 336–46.Google Scholar
Ettensohn, C.A. & Malinda, K.M. (1993). Size regulation and morphogenesis: a cellular analysis of skeletogenesis in the sea urchin embryo. Development 119, 155–67.Google Scholar
Ettensohn, C.A. & Ingersoll, E.P. (1992). Morphogenesis of the sea urchin embryo. In Morphogenesis: An Analysis of the Development of Biological Form (eds Rossomando, E.F. & Alexander, S.), pp. 189–262. Boca Raton, Florida: CRC Press.Google Scholar
Harkey, M.A., Klueg, K., Sheppard, P. & Raff, R.A. (1995). Structure, expression, and extracellular targeting of PM27, a skeletal protein associated specifically with growth of the sea urchin larval spicule. Dev. Biol. 168, 549–66.Google Scholar
Itza, E.M. & Mozingo, N.M. (2005). Septate junctions mediate the barrier to paracellular permeability in sea urchin embryos. Zygote 13, 255–64.Google Scholar
Killian, C.E. & Wilt, F.H. (1996). Characterization of the proteins comprising the integral matrix of Strongylocentrotus purpuratus embryonic spicules. J. Biol. Chem. 271, 9150–9.Google Scholar
Latham, V.H., Martinez, A.L., Cazares, L., Hamburger, H., Tully, M.J. & Oppenheimer, S.B. (1998). Accessing the embryo interior without microinjection. Acta Histochem. 100, 193–200.Google Scholar
Livingston, B.T., Killian, C.E., Wilt, F., Cameron, A., Landrum, M.J., Ermolaeva, O., Sapojnikov, V., Maglott, D.R., Buchanan, A.M. & Ettensohn, C.A. (2006). A genome-wide analysis of biomineralization-related proteins in the sea urchin Strongylocentrotus purpuratus . Dev. Biol. 300, 335–48.Google Scholar
Mann, K., Poustka, A.J. & Mann, M. (2008). The sea urchin (Strongylocentrotus purpuratus) test and spine proteomes. Proteome Sci. 6:22.Google Scholar
Mann, K., Wilt, F.H. & Poustka, A.J. (2010).Proteomic analysis of sea urchin (Strongylocentrotus purpuratus) spicule matrix. Proteome Sci. 8, 33.Google Scholar
Wilt, F.H. (1999). Matrix and mineral in the sea urchin larval skeleton. J. Struct. Biol. 126, 216–26.Google Scholar
Wilt, F.H. (2002). Biomineralization of the spicules of sea urchin embryos. Zool. Sci. 19, 253–61.CrossRefGoogle ScholarPubMed
Wilt, F.H., Killian, C.E. & Livingston, B.T. (2003). Development of calcareous skeletal elements in invertebrates. Differentiation 71, 237–50.Google Scholar
Wilt, F. H., Killian, C. E., Hamilton, P., & Croker, L. (2008). The dynamics of secretion during sea urchin embryonic skeleton formation. Exp. Cell Res. 314, 1744–52.Google Scholar