The micro1 gene is necessary and sufficient for micromere differentiation and mid/hindgut-inducing activity in the sea urchin embryo

2005 ◽  
Vol 215 (9) ◽  
pp. 450-459 ◽  
Author(s):  
Atsuko Yamazaki ◽  
Rika Kawabata ◽  
Kosuke Shiomi ◽  
Shonan Amemiya ◽  
Masaya Sawaguchi ◽  
...  
Keyword(s):  
Sea Urchin ◽  
Sea Urchin Embryo ◽  
Necessary And Sufficient

LvDelta is a mesoderm-inducing signal in the sea urchin embryo and can endow blastomeres with organizer-like properties

Development ◽  
2002 ◽  
Vol 129 (8) ◽  
pp. 1945-1955 ◽  
Author(s):  
Hyla C. Sweet ◽  
Michael Gehring ◽  
Charles A. Ettensohn
Keyword(s):  
Sea Urchin ◽  
Critical Role ◽  
Cell Types ◽  
Notch Signaling Pathway ◽  
Notch Receptor ◽  
Pigment Cells ◽  
Mesodermal Cell ◽  
Sea Urchin Embryo ◽  
Organizing Center ◽  
Necessary And Sufficient

Signals from micromere descendants play a critical role in patterning the early sea urchin embryo. Previous work demonstrated a link between the induction of mesoderm by micromere descendants and the Notch signaling pathway. In this study, we demonstrate that these micromere descendants express LvDelta, a ligand for the Notch receptor. LvDelta is expressed by micromere descendants during the blastula stage, a time when signaling has been shown to occur. By a combination of embryo microsurgery, mRNA injection and antisense morpholino experiments, we show that expression of LvDelta by micromere descendants is both necessary and sufficient for the development of two mesodermal cell types, pigment cells and blastocoelar cells. We also demonstrate that LvDelta is expressed by macromere descendants during mesenchyme blastula and early gastrula stages. Macromere-derived LvDelta is necessary for blastocoelar cell and muscle cell development. Finally, we find that expression of LvDelta is sufficient to endow blastomeres with the ability to function as a vegetal organizing center and to coordinate the development of a complete pluteus larva.

The Sea Urchin Embryo

1986 ◽  
Author(s):  
Giovanni Giudice
Keyword(s):  
Sea Urchin ◽  
Sea Urchin Embryo

scholarly journals An anterior signaling center patterns and sizes the anterior neuroectoderm of the sea urchin embryo

Development ◽  
2016 ◽  
Vol 143 (9) ◽  
pp. 1523-1533 ◽  
Author(s):  
Ryan C. Range ◽  
Zheng Wei
Keyword(s):  
Sea Urchin ◽  
Sea Urchin Embryo ◽  
Signaling Center

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.

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