scholarly journals Biochemical analysis of the interaction of calcium with toposome: A major protein component of the sea urchin egg and embryo

2008 ◽  
Vol 103 (5) ◽  
pp. 1464-1471 ◽  
Author(s):  
Michael Hayley ◽  
Ming Sun ◽  
Erika F. Merschrod S ◽  
Philip J. Davis ◽  
John J. Robinson
Keyword(s):  
Sea Urchin ◽  
Biochemical Analysis ◽  
Protein Component ◽  
Major Protein ◽  
Sea Urchin Egg

scholarly journals Roles for Ca2+, Mg2+ and NaCl in modulating the self-association reaction of hyalin, a major protein component of the sea-urchin extraembryonic hyaline layer

1988 ◽  
Vol 256 (1) ◽  
pp. 225-228 ◽  
Author(s):  
J J Robinson
Keyword(s):  
Sea Urchin ◽  
Sea Water ◽  
Protein Component ◽  
The Self ◽  
Major Protein ◽  
Aggregate Formation ◽  
Protein Protein Interaction ◽  
Sea Urchin Embryo ◽  
Association Reaction ◽  
Self Association

The self-association reaction of hyalin, a major protein component of the sea-urchin extraembryonic hyaline layer, was examined. Concentrations of Ca2+ below 1 mM had little effect on the hyalin gelation reaction, but higher concentrations of the cation induced protein aggregation. Quantitative aggregate formation required a Ca2+ concentration in excess of 10 mM. This reaction was modulated by both NaCl and Mg2+. The effectiveness of Ca2+ in inducing hyalin gelation was markedly enhanced in the presence of 500 mM-NaCl, the concentration found in sea water. Similarly, 20 mM-Mg2+ also enhanced Ca2+-induced hyalin gelation. Neither NaCl nor Mg2+ alone induced hyalin gelation. Concentrations of Ca2+ as low as 1 mM effectively protected hyalin from tryptic digestion both in the presence and in the absence of 500 mM-NaCl. The latter result suggested that, although higher concentrations of Ca2+ were required to induce the hyalin gelation reaction, lower concentrations of the cation could mediate a protein-protein interaction in an NaCl-independent fashion. These results identify the parameters that modulate hyalin self-association, a reaction that is essential for hyaline-layer assembly around the developing sea-urchin embryo.

scholarly journals Different Ca2+-releasing abilities of sperm extracts compared with tissue extracts and phospholipase C isoforms in sea urchin egg homogenate and mouse eggs

2000 ◽  
Vol 346 (3) ◽  
pp. 743-749 ◽  
Author(s):  
Keith T. JONES ◽  
Miho MATSUDA ◽  
John PARRINGTON ◽  
Matilda KATAN ◽  
Karl SWANN
Keyword(s):  
Phospholipase C ◽  
Sea Urchin ◽  
Tissue Extracts ◽  
Sea Urchin Egg ◽  
Boar Sperm ◽  
Specific Activities ◽  
Mammalian Eggs ◽  
Mouse Eggs

A soluble phospholipase C (PLC) from boar sperm generates InsP3 and hence causes Ca2+ release when added to sea urchin egg homogenate. This PLC activity is associated with the ability of sperm extracts to cause Ca2+ oscillations in mammalian eggs following fractionation. A sperm PLC may, therefore, be responsible for causing the observed Ca2+ oscillations at fertilization. In the present study we have further characterized this boar sperm PLC activity using sea urchin egg homogenate. Consistent with a sperm PLC acting on egg PtdIns(4,5)P2, the ability of sperm extracts to release Ca2+ was blocked by preincubation with the PLC inhibitor U73122 or by the addition of neomycin to the homogenate. The Ca2+-releasing activity was also detectable in sperm from other species and in whole testis extracts. However, activity was not observed in extracts from other tissues. Moreover recombinant PLCβ1, -γ1, -γ2, -∆1, all of which had higher specific activities than boar sperm extracts, were not able to release Ca2+ in the sea urchin egg homogenate. In addition these PLCs were not able to cause Ca2+ oscillations following microinjection into mouse eggs. These results imply that the sperm PLC possesses distinct properties that allow it to hydrolyse PtdIns(4,5)P2 in eggs.

ACID-SOLUBLE NUCLEOTIDES IN THE SEA URCHIN EGG

Embryologia ◽  
1966 ◽  
Vol 9 (3) ◽  
pp. 170-183 ◽  
Author(s):  
TOMIO YANAGISAWA ◽  
NAOHIDE ISONO
Keyword(s):  
Sea Urchin ◽  
Sea Urchin Egg
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