Fate Specification Along the Sea Urchin Embryo Animal-Vegetal Axis

1997 ◽  
Vol 192 (1) ◽  
pp. 175-177 ◽  
Author(s):  
R. C. Angerer ◽  
L. M. Angerer
Keyword(s):  
Sea Urchin ◽  
Fate Specification ◽  
Sea Urchin Embryo

scholarly journals Functional Gap Junctions in the Early Sea Urchin Embryo Are Localized to the Vegetal Pole

1999 ◽  
Vol 212 (2) ◽  
pp. 503-510 ◽  
Author(s):  
Ikuko Yazaki ◽  
Brian Dale ◽  
Elisabetta Tosti
Keyword(s):  
Gap Junctions ◽  
Sea Urchin ◽  
Sea Urchin Embryo ◽  
Vegetal Pole

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

Zygote ◽  
2008 ◽  
Vol 16 (1) ◽  
pp. 73-78 ◽  
Author(s):  
M. Alvarez ◽  
J. Nnoli ◽  
E.J. Carroll ◽  
V. Hutchins-Carroll ◽  
Z. Razinia ◽  
...  
Keyword(s):  
Sea Urchin ◽  
Cell Adhesion Molecule ◽  
Cellular Interaction ◽  
Adhesive Interaction ◽  
Lytechinus Pictus ◽  
Developmental Effects ◽  
Sea Urchin Embryo ◽  
Repeat Domain ◽  
Precise Quantification ◽  
Main Component

SummaryThe 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.

Sign in / Sign up

Export Citation Format

Share Document