A putative role for carbohydrates in sea urchin gastrulation

Latham, Virginia H.; Tully, Monica J.; Oppenheimer, Steven B.

doi:10.1016/s0065-1281(99)80030-0

Cited by 15 publications

(34 citation statements)

References 43 publications

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“…This article showed that both Lens culinaris and Pisum sativum lectins that bind mannose/glucose caused exogastrulation due to D-mannose/glucose-like residues, perhaps playing a role in archenteron development (Latham et al, 1999) (See figure 2). The authors further suggest that wheat germ agglutinin (WGA)…”

Section: Carbohydratesmentioning

confidence: 98%

“…In efforts to understand the mechanisms of carbohydrate involvement in gastrulation (Latham et al, 1999) suggested the mechanism for how some carbohydrates may interfere with the binding of the archenteron tip to the blastocoel roof. This article showed that both Lens culinaris and Pisum sativum lectins that bind mannose/glucose caused exogastrulation due to D-mannose/glucose-like residues, perhaps playing a role in archenteron development (Latham et al, 1999) (See figure 2).…”

Section: Carbohydratesmentioning

confidence: 99%

“…bound to mesenchymal cells were involved in skeletogenesis of the embryo and caused defective skeletogenesis (Latham et al, 1999).…”

Section: Carbohydratesmentioning

confidence: 99%

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Involvement of l(–)-rhamnose in sea urchin gastrulation: a live embryo assay

Smith

Oppenheimer

2013

Zygote

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SummaryThe sea urchin embryo is a National Institutes of Health model system that has provided major developments, and is important in human health and disease. To obtain initial insights to identify glycans that mediate cellular interactions, Lytechinus pictus sea urchin embryos were incubated at 24 or 30 h post-fertilization with 0.0009–0.03 M alpha-cyclodextrin, melibiose, l(–)-rhamnose, trehalose, d(+)-xylose or l(–)-xylose in lower-calcium artificial sea water (pH 8.0, 15°C), which speeds the entry of molecules into the interior of the embryos. While α-cyclodextrin killed the embryos, and l(–)-xylose had small effects at one concentration tested, l(–)-rhamnose caused substantially increased numbers of unattached archenterons and exogastrulated embryos at low glycan concentrations after 18–24 h incubation with the sugar. The results were statistically significant compared with the control embryos in the absence of sugar (P < 0.05). The other sugars (melibiose, trehalose, d(+)-xylose) had no statistically significant effects whatsoever at any of the concentrations tested. In total, in the current study, 39,369 embryos were examined. This study is the first demonstration that uses a live embryo assay for a likely role for l(–)-rhamnose in sea urchin gastrula cellular interactions, which have interested investigators for over a century.

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Section: Carbohydratesmentioning

confidence: 98%

Section: Carbohydratesmentioning

confidence: 99%

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Involvement of l(–)-rhamnose in sea urchin gastrulation: a live embryo assay

Smith

Oppenheimer

2013

Zygote

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“…Large molecules can enter embryos if added exogenously (Latham et al, 1998) and exert their effects internally as well as externally (Latham et al, 1999).…”

Section: Discussionmentioning

confidence: 99%

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

Alvarez

Nnoli

Carroll

et al. 2008

Zygote

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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 hyalinhyalin 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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“…In the present report, we provide evidence that the sea urchin glycoprotein hyalin is a cell adhesion molecule that is involved in mediating a specific cellular interaction in the model sea urchin embryo system, attachment of the tip of the developing gut (archenteron) to the roof of the blastocoel. This is a classic cellular interaction that has interested investigators for a century, yet its molecular basis has not been elucidated (Herbst, 1900: Gustafson, 1963: Hardin and McClay, 1990Latham et al, 1999;Khurrum et al, 2004;Oppenheimer and Carroll, 2004).…”

Section: Introductionmentioning

confidence: 99%

Hyalin is a cell adhesion molecule involved in mediating archenteron–blastocoel roof attachment

et al. 2008

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SummaryThe U. S. National Institutes of Health has designated the sea urchin embryo as a model organism because about twenty-five discoveries in this system have led to insights into the physiology of higher organisms, including humans. Hyalin is a large glycoprotein in the hyaline layer of sea urchin embryos that functions to maintain general adhesive relationships in the developing embryo. It consists of the hyalin repeat domain that has been identified in organisms as diverse as bacteria, worms, flies, mice, sea urchins and humans. Here we show, using a polyclonal antibody raised against the 11.6 S species of hyalin, that it localizes at the tip of the archenteron and on the roof of the blastocoel exactly where these two structures bond in an adhesive interaction that has been of interest for over a century. In addition, the antibody blocks the interaction between the archenteron tip and blastocoel roof. These results, in addition to other recent findings from this laboratory that will be discussed, suggest that hyalin is involved in mediating this cellular interaction. This is the first demonstration that suggests that hyalin is a specific cell adhesion molecule that may function as such in many organisms, including humans.

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A putative role for carbohydrates in sea urchin gastrulation

Cited by 15 publications

References 43 publications

Involvement of l(–)-rhamnose in sea urchin gastrulation: a live embryo assay

Involvement of l(–)-rhamnose in sea urchin gastrulation: a live embryo assay

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

Hyalin is a cell adhesion molecule involved in mediating archenteron–blastocoel roof attachment

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