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Exogenous hyalin and sea urchin gastrulation, Part II: hyalin, an interspecies cell adhesion molecule

Published online by Cambridge University Press:  01 February 2008

M. Alvarez ,
J. Nnoli ,
E.J. Carroll Jr ,
V. Hutchins-Carroll ,
Z. Razinia  and
S.B. Oppenheimer
M. Alvarez
Affiliation:
Department of Biology and Center for Cancer and Developmental Biology, California State University, Northridge, CA 91330-8303, USA.
J. Nnoli*
Affiliation:
Department of Chemistry and Biochemistry, California State University, Northridge, 18111 Nordhoff Street, Northridge, CA 91330-8262, USA
E.J. Carroll Jr*
Affiliation:
Department of Chemistry and Biochemistry, California State University, Northridge, 18111 Nordhoff Street, Northridge, CA 91330-8262, USA
V. Hutchins-Carroll
Affiliation:
Department of Biology and Center for Cancer and Developmental Biology, California State University, Northridge, CA 91330-8303, USA.
Z. Razinia
Affiliation:
Department of Biology and Center for Cancer and Developmental Biology, California State University, Northridge, CA 91330-8303, USA.
S.B. Oppenheimer*
Affiliation:
Department of Biology and Center for Cancer and Developmental Biology, California State University, Northridge, CA 91330-8303, USA.
*
Department of Chemistry and Biochemistry, California State University, Northridge, 18111 Nordhoff Street, Northridge, CA 91330-8262, USA; [email protected]; [email protected]
Department of Chemistry and Biochemistry, California State University, Northridge, 18111 Nordhoff Street, Northridge, CA 91330-8262, USA; [email protected]; [email protected]
All correspondence to: S.B. Oppenheimer. Department of Biology and Center for Cancer and Developmental Biology, California State University, Northridge, CA 91330-8303, USA. Tel: +1 818 677 3336. Fax: +1 818 677 2034. e-mail: [email protected]
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Summary

The 330 kDa fibrillar glycoprotein hyalin is a well known component of the sea urchin embryo extracellular hyaline layer. Only recently, the main component of hyalin, the hyalin repeat domain, has been identified in organisms as widely divergent as bacteria and humans using the GenBank database and therefore its possible function has garnered a great deal of interest. In the sea urchin, hyalin serves as an adhesive substrate in the developing embryo and we have recently shown that exogenously added purified hyalin from Strongylocentrotus purpuratus embryos blocks a model cellular interaction in these embryos, archenteron elongation/attachment to the blastocoel roof. It is important to demonstrate the generality of this result by observing if hyalin from one species of sea urchin blocks archenteron elongation/attachment in another species. Here we show in three repeated experiments, with 30 replicate samples for each condition, that the same concentration of S. purpuratus hyalin (57 μg/ml) that blocked the interaction in living S. purpuratus embryos blocked the same interaction in living Lytechinus pictus embryos. These results correspond with the known crossreactivity of antibody against S. purpuratus hyalin with L. pictus hyalin. We propose that hyalin–hyalin receptor binding may mediate this adhesive interaction. The use of a microplate assay that allows precise quantification of developmental effects should help facilitate identification of the function of hyalin in organisms as divergent as bacteria and humans.

Keywords

Archenteron attachmentCell adhesionHyalinInterspeciesSea urchins
Type
Research Article
Information
Zygote , Volume 16 , Issue 1 , February 2008 , pp. 73 - 78
Copyright
Copyright © Cambridge University Press 2008

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References

B Tidwell, J.P. & Spotte, S. (1985). Artificial Seawaters, Formulas and Methods, p. 256. Boston: Jones and Bartlett Publishers, Inc.Google Scholar
Callebout, I., Gilges, D., Vignon, I. & Mornon, J.P. (2000). HYR, an extracellular module involved in cellular adhesion and related to the immunoglobulin-like fold. Protein Sci. 9, 1382–90.CrossRefGoogle Scholar
Citkowitz, E. (1971). The hyaline layer: its isolation and role in echinoderm development. Dev. Biol. 24, 348–62.CrossRefGoogle ScholarPubMed
Coyle-Thompson, C. & Oppenheimer, S.B. (2005). A novel approach to study adhesion mechanisms by isolation of the interacting system. Acta Histochem. 107, 243–51.CrossRefGoogle ScholarPubMed
Davidson, E.H. (2006). The sea urchin genome: where will it lead us? Science 314, 939–40.CrossRefGoogle ScholarPubMed
Davidson, E.H. & Cameron, R.A. (2002). Arguments for sequencing the genome of the sea urchin Strongylocentrotus purpuratus www.genome.gov/pages/research/sequencing/SegProposals/Sea>Urchin_Genome.prob.2002Urchin_Genome.prob.2002>Google Scholar
Edelman, G.M. (1987). CAMs and Igs: cell adhesion and the evolutionary origins of immunity. Immunol. Rev. 100, 9–43.Google ScholarPubMed
Fink, R.D. & McClay, D.R. (1985). Three cell recognition changes accompany the ingression of sea urchin primary mesenchyme cells. Dev. Biol. 107, 66–74.CrossRefGoogle ScholarPubMed
Gray, J., Justice, R., Nagel, G.M. & Carroll, E.J. Jr (1985). Resolution and characterization of a major protein of the sea urchin hyaline layer. J. Biol. Chem. 26, 9282–88.Google Scholar
Herbst, C. (1900). Über das auseinandergenhen von furchungs-und gewebezellen in kalkfreiem medium. Arch. F. Entwick 9, 424–63.CrossRefGoogle Scholar
Khurrum, M., Hernandez, A., Eskalaei, M., Badali, O., Coyle-Thompson, C. & Oppenheimer, S.B. (2004). Carbohydrate involvement in cellular interactions in sea urchin gastrulation. Acta Histochem. 106, 97–106.CrossRefGoogle ScholarPubMed
Latham, V., Martinez, A., Cazares, L., Hamburger, H., Tully, M.J. & Oppenheimer, S.B. (1998). Accessing the embryo int-erior without microinjection. Acta Histochem. 100, 193–200.CrossRefGoogle ScholarPubMed
Latham, V., Tully, M. & Oppenheimer, S.B. (1999). A putative role for carbohydrates in sea urchin gastrulation. Acta Histochem. 101, 293–303.CrossRefGoogle ScholarPubMed
McClay, D.R. (1986). Embryo dissociation, cell isolation and cell reassociation. In: Methods in Cell Biology (ed. Schroeder, T.E.), pp. 309–23. San Diego: Academic Press.Google Scholar
Razinia, Z., Carroll, E.J. Jr & Oppenheimer, S.B. (2007). Microplate assay for quantifying developmental morphologies: effects of exogenous hyalin on sea urchin gastrulation. Zygote 15, 1–6.CrossRefGoogle ScholarPubMed
Sajadi, S., Rojas, P. & Oppenheimer, S.B. (2007). Cyclodextrin, a probe for studying adhesive interactions. Acta Histochem. 109, 338–42.Google ScholarPubMed
Stephens, R.E. & Kane, R.E. (1970). Some properties of hyalin: the calcium-insoluble protein of the hyaline layer of the sea urchin egg. J. Cell Biol. 44, 611–17.CrossRefGoogle ScholarPubMed
Vater, C.A. & Jackson, R.C. (1990). Immunolocalization of hyalin in sea urchin egg and embryo using an antihyalin-specific monoclonal antibody. Mol. Reprod. Develop. 25, 215–26.CrossRefGoogle ScholarPubMed
Warburg, O. & Christian, W. (1941). Isolierung und kristal-lisation des garnugsferments enolase. Biochem Z. 310, 384–421.Google Scholar
Wessel, G.M., Berg, L., Adelson, D.L., Cannon, G. & McClay, D.R. (1998). A molecular analysis of hyalin, a substrate for cell adhesion in the hyaline layer of the sea urchin embryo. Dev. Biol. 193, 115–26.CrossRefGoogle ScholarPubMed