scholarly journals Characterization of aSpANPromoter Sufficient to Mediate Correct Spatial Regulation along the Animal–Vegetal Axis of the Sea Urchin Embryo

1996 ◽  
Vol 176 (1) ◽  
pp. 95-107 ◽  
Author(s):  
David J. Kozlowski ◽  
Michael L. Gagnon ◽  
Jeffrey K. Marchant ◽  
Susan D. Reynolds ◽  
Lynne M. Angerer ◽  
...  
Keyword(s):  
Sea Urchin ◽  
Spatial Regulation ◽  
Sea Urchin Embryo

Ontogeny and characterization of mesenchyme antigens of the sea urchin embryo

1989 ◽  
Vol 136 (1) ◽  
pp. 75-86 ◽  
Author(s):  
Colin R. Tamboline ◽  
Robert D. Burke
Keyword(s):  
Sea Urchin ◽  
Sea Urchin Embryo

scholarly journals Characterization of the SpHE Promoter That Is Spatially Regulated along the Animal-Vegetal Axis of the Sea Urchin Embryo

1995 ◽  
Vol 171 (1) ◽  
pp. 195-211 ◽  
Author(s):  
Zheng Wei ◽  
Lynne M. Angerer ◽  
Michael L. Gagnon ◽  
Robert C. Angerer
Keyword(s):  
Sea Urchin ◽  
Sea Urchin Embryo

Identification and characterization of gelatin-cleavage activities in the apically located extracellular matrix of the sea urchin embryo

2000 ◽  
Vol 78 (4) ◽  
pp. 455-462 ◽  
Author(s):  
Justin Flood ◽  
Janice Mayne ◽  
John J Robinson
Keyword(s):  
Extracellular Matrix ◽  
Sea Urchin ◽  
Inhibitory Effect ◽  
Divalent Metal Ions ◽  
Gelatinase Activity ◽  
Sea Urchin Embryo ◽  
Phenylmethyl Sulfonyl Fluoride ◽  
Sulfonyl Fluoride ◽  
Identification And Characterization

We have identified and partially characterized several gelatinase activities associated with the sea urchin extraembryonic matrix, the hyaline layer. A previously identified 41-kDa collagenase/gelatinase activity was generally not found to be associated with isolated hyaline layers but was dissociated from the surface of 1-h-old embryos in the absence of Ca2+ and Mg2+. While hyaline layers, freshly prepared from 1-h-old embryos, were devoid of any associated gelatinase activities, upon storage at 4°C for 4 days, a number of gelatin-cleavage activities appeared. Comparative analysis of these activities with the 41-kDa collagenase/gelatinase revealed that all species were inhibited by ethylenediamine tetraacetic acid but were refractory to inhibition with the serine protease inhibitors, phenylmethyl sulfonyl fluoride and benzamidine. In contrast, the largely Zn2+ specific chelator 1,10-phenanthroline had markedly different effects on the gelatinase activities. While several of the storage-induced, hyaline-layer-associated gelatinase activities were inhibited, the 41-kDa collagenase/gelatinase was refractory to inhibition as was a second gelatinase species with an apparent molecular mass of 45 kDa. We also examined the effects of a series of divalent metal ions on the gelatin-cleavage activities. In both qualitative and quantitative assays, Ca2+ was the most effective activator while Mn2+, Cu2+, Cd2+, and Zn2+ were all inhibitory. In contrast, Mg2+ had a minimal inhibitory effect on storage-induced gelatinase activities but significantly inhibited the 41-kDa collagenase/gelatinase. These results identify several distinct gelatin-cleavage activities associated with the sea urchin extraembryonic hyaline layer and point to diversity in the biochemical nature of these species.Key words: gelatinase, sea urchin, extracellular matrix.

Purification and characterization of a 32-kDa protein that localizes to the sea urchin extraembryonic matrix, the hyaline layer

1992 ◽  
Vol 70 (8) ◽  
pp. 623-628 ◽  
Author(s):  
John J. Robinson
Keyword(s):  
Embryonic Development ◽  
Quantitative Determination ◽  
Sea Urchin ◽  
Polyclonal Antiserum ◽  
Purification And Characterization ◽  
Blastula Stage ◽  
Stage Of Development ◽  
Sea Urchin Egg ◽  
Sea Urchin Embryo

We have purified a 32 kilodalton (kDa) protein that localized with isolated, intact hyaline layers prepared from 1-h-old embryos. The protein appeared not to bind calcium and was not quantitatively released from 1-h-old embryos in the absence of Ca2+ and Mg2+. Using polyclonal antiserum prepared against the 32-kDa protein, the antigen was detected throughout embryonic development. By the hatched blastula stage of development, the 32-kDa protein was replaced by a species of slightly smaller molecular mass. Quantitative determination indicated that the 32-kDa protein accounted for approximately 6% of the total protein present in the sea urchin egg. This result is suggestive of a structural role for the 32-kDa protein that is required throughout embryonic development, although perhaps in a modified form from the hatched blastula stage on.Key words: sea urchin, embryo, hyaline layer, component.

Sign in / Sign up

Export Citation Format

Share Document