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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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