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

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 bact...

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Bibliographic Details
Published in:	Zygote (Cambridge) Vol. 16; no. 4; p. 355
Main Authors:	Contreras, Azalia, Vitale, John, Hutchins-Carroll, Virginia, Carroll, Jr, Edward J, Oppenheimer, Steven B
Format:	Journal Article
Language:	English
Published:	England 01-11-2008
Subjects:	Animals Calcium-Binding Proteins - isolation & purification Calcium-Binding Proteins - pharmacology Calcium-Binding Proteins - physiology Electrophoresis, Polyacrylamide Gel Embryo, Nonmammalian - drug effects Embryo, Nonmammalian - physiology Extracellular Matrix Proteins - isolation & purification Extracellular Matrix Proteins - pharmacology Extracellular Matrix Proteins - physiology Female Gastrula - drug effects Gastrula - physiology Lytechinus - drug effects Lytechinus - embryology Lytechinus - physiology Male Sea Urchins - physiology Spermatozoa - physiology
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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.
ISSN:	0967-1994
DOI:	10.1017/S096719940800484X