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Exogenous hyalin and sea urchin gastrulation. Part III: Biological activity of hyalin isolated from Lytechinus pictus embryos

Published online by Cambridge University Press:  01 November 2008

Azalia Contreras ,
John Vitale ,
Virginia Hutchins-Carroll ,
Edward J. Carroll Jr  and
Steven B. Oppenheimer
Azalia Contreras
Affiliation:
Department of Biology and Center for Cancer and Developmental Biology, California State University, Northridge, 18111 Nordhoff Street, Northridge, CA 91330–8303, USA.
John Vitale
Affiliation:
Department of Biology and Center for Cancer and Developmental Biology, California State University, Northridge, 18111 Nordhoff Street, Northridge, CA 91330–8303, USA.
Virginia Hutchins-Carroll
Affiliation:
Department of Biology and Center for Cancer and Developmental Biology, California State University, Northridge, 18111 Nordhoff Street, Northridge, CA 91330–8303, USA.
Edward J. Carroll Jr
Affiliation:
Department of Chemistry and Biochemistry, California State University, Northridge, 18111 Nordhoff Street, Northridge, CA 91330–8262, USA.
Steven B. Oppenheimer*
Affiliation:
Department of Biology and Center for Cancer and Developmental Biology, California State University, Northridge, Northridge, CA 91330–8303, USA. Department of Biology and Center for Cancer and Developmental Biology, California State University, Northridge, 18111 Nordhoff Street, Northridge, CA 91330–8303, USA.
*
All correspondence to: Dr Steven B. Oppenheimer. Department of Biology and Center for Cancer and Developmental Biology, California State University, Northridge, Northridge, CA 91330–8303, USA. Tel: +1 818 677 3336. Fax: +1 818 677 2034. e-mail: [email protected]
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Summary

Hyalin is a large glycoprotein, consisting of the hyalin repeat domain and non-repeated regions, and is the major component of the hyaline layer in the early sea urchin embryo of Strongylocentrotus purpuratus. The hyalin repeat domain has been identified in proteins from organisms as diverse as bacteria, sea urchins, worms, flies, mice and humans. While the specific function of hyalin and the hyalin repeat domain is incompletely understood, many studies suggest that it has a functional role in adhesive interactions. In part I of this series, we showed that hyalin isolated from the sea urchin S. purpuratus blocked archenteron elongation and attachment to the blastocoel roof occurring during gastrulation in S. purpuratus embryos, (Razinia et al., 2007). The cellular interactions that occur in the sea urchin, recognized by the U.S. National Institutes of Health as a model system, may provide insights into adhesive interactions that occur in human health and disease. In part II of this series, we showed that S. purpuratus hyalin heterospecifically blocked archenteron–ectoderm interaction in Lytechinus pictus embryos (Alvarez et al., 2007). In the current study, we have isolated hyalin from the sea urchin L. pictus and demonstrated that L. pictus hyalin homospecifically blocks archenteron–ectoderm interaction, suggesting a general role for this glycoprotein in mediating a specific set of adhesive interactions. We also found one major difference in hyalin activity in the two sea urchin species involving hyalin influence on gastrulation invagination.

Keywords

Archenteron attachmentHyalinLytechinus pictus sea urchin embryo
Type
Research Article
Information
Zygote , Volume 16 , Issue 4 , November 2008 , pp. 355 - 361
Copyright
Copyright © Cambridge University Press 2008

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