Calcium-induced decrease in membrane fluidity of sea urchin egg cortex after fertilization

Nature ◽  
1980 ◽  
Vol 286 (5769) ◽  
pp. 185-186 ◽  
Author(s):  
Judith Campisi ◽  
Carl J. Scandella
Keyword(s):  
Membrane Fluidity ◽  
Sea Urchin ◽  
Sea Urchin Egg ◽  
Egg Cortex

scholarly journals STUDIES ON SULFHYDRYL GROUPS DURING CELL DIVISION OF SEA URCHIN EGG

1960 ◽  
Vol 8 (3) ◽  
pp. 603-607 ◽  
Author(s):  
Hikoichi Sakai
Keyword(s):  
Cell Division ◽  
Sea Urchin ◽  
Sulfhydryl Groups ◽  
Cell Stage ◽  
Sea Urchin Eggs ◽  
Maximum Value ◽  
Sea Urchin Egg ◽  
Egg Cortex

Masses of cortices of both unfertilized and fertilized sea urchin eggs can be isolated by crushing eggs in hypotonic MaCl2 (0.1 M) solution. The amount of cortical material in terms of protein-N increases steadily after fertilization until the monaster stage and thereafter remains almost constant until well into the two-cell stage. The amount of bound—SH per protein-N of the egg cortex also increases after fertilization, reaches a maximum value at the amphiaster stage and thereafter decreases rapidly as the cleavage of the cell proceeds.

scholarly journals STUDIES ON SULFHYDRYL GROUPS DURING CELL DIVISION OF SEA URCHIN EGG

1960 ◽  
Vol 8 (3) ◽  
pp. 609-615 ◽  
Author(s):  
Hikoichi Sakai
Keyword(s):  
Cell Division ◽  
Sea Urchin ◽  
Soluble Protein ◽  
Sulfhydryl Groups ◽  
Sh Groups ◽  
Sea Urchin Egg ◽  
Whole Egg ◽  
Egg Cortex

Sea urchin egg proteins extracted with KCl are mostly TCA-soluble and, conversely, those extracted with TCA are KCl-soluble. Both groups are water-insoluble and show fluctuations in—SH content during the division cycle. The fluctuation of the—SH groups of the KCl-soluble protein of the whole egg is due to a —SH⇌—S—S— interchange within the freely reacting groups and not within the sluggish and masked —SH groups of the protein. The —SH content of the KCl-soluble protein of the egg cortex also fluctuates in a similar way.

scholarly journals Phorbol ester treatment stimulates tyrosine phosphorylation of a sea urchin egg cortex protein.

1990 ◽  
Vol 110 (4) ◽  
pp. 1049-1053 ◽  
Author(s):  
W P Jiang ◽  
R A Gottlieb ◽  
W J Lennarz ◽  
W H Kinsey
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Tyrosine Phosphorylation ◽  
Sea Urchin ◽  
Phorbol Ester ◽  
Signal Transduction Pathway ◽  
Exchange System ◽  
Sea Urchin Egg ◽  
Weight Protein ◽  
Egg Cortex

Fertilization of the sea urchin egg results in the phosphorylation, on tyrosine, of a high molecular weight protein localized in the egg cortex. In the present study, treatment of unfertilized eggs with the phorbol ester 12-O-tetradecanoylphorbol 13-acetate stimulated tyrosine phosphorylation of the high molecular weight cortical protein to levels three- to fivefold higher than that occurring in response to fertilization. Experiments using agents that inhibit the egg Na+/H+ exchange system or mimic the fertilization-induced shift in cytoplasmic pHi, suggest a signal transduction pathway in which protein kinase C activates the egg Na+/H+ exchange system and the resultant cytoplasmic pHi shift promotes tyrosine phosphorylation of the high molecular weight cortical protein.

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