Reassociation of cortical secretory vesicles with sea urchin egg plasma membrane: Assessment of binding specificity

1990 ◽  
Vol 115 (1) ◽  
pp. 83-93 ◽  
Author(s):  
Robert C. Jackson ◽  
Paul A. Modern
Keyword(s):  
Plasma Membrane ◽  
Sea Urchin ◽  
Binding Specificity ◽  
Secretory Vesicles ◽  
Sea Urchin Egg

Characterization of cortical secretory vesicles from the sea urchin egg

1983 ◽  
Vol 96 (1) ◽  
pp. 37-45 ◽  
Author(s):  
Susan J. Decker ◽  
William H. Kinsey
Keyword(s):  
Sea Urchin ◽  
Secretory Vesicles ◽  
Sea Urchin Egg

scholarly journals Isolation and partial characterization of the plasma membrane of the sea urchin egg.

1980 ◽  
Vol 87 (1) ◽  
pp. 248-254 ◽  
Author(s):  
W H Kinsey ◽  
G L Decker ◽  
W J Lennarz
Keyword(s):  
Plasma Membrane ◽  
Cell Surface ◽  
Sea Urchin ◽  
Plasma Membranes ◽  
Binding Property ◽  
Marker Enzyme ◽  
Surface Complex ◽  
Sea Urchin Egg ◽  
Peripheral Proteins ◽  
Cortical Vesicles

The cell surface complex (Detering et al., 1977, J. Cell Biol. 75, 899-914) of the sea urchin egg consists of two subcellular organelles: the plasma membrane, containing associated peripheral proteins and the vitelline layer, and the cortical vesicles. We have now developed a method of isolating the plasma membrane from this complex and have undertaken its biochemical characterization. Enzymatic assays of the cell surface complex revealed the presence of a plasma membrane marker enzyme, ouabain-sensitive Na+/K+ ATPase, as well as two cortical granule markers, proteoesterase and ovoperoxidase. After separation from the cortical vesicles and purification on a sucrose gradient, the purified plasma membranes are recovered as large sheets devoid of cortical vesicles. The purified plasma membranes are highly enriched in the Na+/K+ ATPase but contain only very low levels of the proteoesterase and ovoperoxidase. Ultrastructurally, the purified plasma membrane is characterized as large sheets containing a "fluffy" proteinaceous layer on the external surface, which probably represent peripheral proteins, including remnants of the vitelline layer. Extraction of these membranes with Kl removes these peripheral proteins and causes the membrane sheets to vesiculate. Polyacrylamide gel electrophoresis of the cell surface complex, plasma membranes, and Kl-extracted membranes indicates that the plasma membrane contains five to six major proteins species, as well as a large number of minor species, that are not extractable with Kl. The vitelline layer and other peripheral membrane components account for a large proportion of the membrane-associated protein and are represented by at least six to seven polypeptide components. The phospholipid composition of the Kl-extracted membranes is unique, being very rich in phosphatidylethanolamine and phosphatidylinositol. Cholesterol was found to be a major component of the plasma membrane. Before Kl extraction, the purified plasma membranes retain the same species-specific sperm binding property that is found in the intact egg. This observation indicates that the sperm receptor mechanisms remain functional in the isolated, cortical vesicle-free membrane preparation.

scholarly journals THE MEMBRANE CAPACITANCE OF THE SEA URCHIN EGG

1957 ◽  
Vol 3 (1) ◽  
pp. 103-110 ◽  
Author(s):  
Lord Rothschild
Keyword(s):  
Plasma Membrane ◽  
Sea Urchin ◽  
Sea Water ◽  
Unit Area ◽  
Membrane Capacitance ◽  
Percentage Reduction ◽  
Cortical Granules ◽  
Sea Urchin Egg

1. The surface of the unfertilized sea urchin egg is folded and the folds are reversibly eliminated by exposing the egg to hypotonic sea water. If the plasma membrane is outside the layer of cortical granules, unfolding may explain why the membrane capacitance per unit area decreases (and does not increase) when a sea urchin egg is put into hypotonic sea water. 2. The degree of surface folding markedly increases after fertilization, which provides an explanation for the increase in membrane capacitance per unit area observed after fertilization. 3. The percentage reduction in membrane folding in fertilized eggs after immersion in hypotonic sea water is probably sufficient to explain the decrease in membrane capacitance per unit area observed in these conditions.

scholarly journals Effects of Dithiothreitol on Fertilization and Early Development in Sea Urchin

Cells ◽  
2021 ◽  
Vol 10 (12) ◽  
pp. 3573
Author(s):  
Nunzia Limatola ◽  
Jong Tai Chun ◽  
Sawsen Cherraben ◽  
Jean-Louis Schmitt ◽  
Jean-Marie Lehn ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Plasma Membrane ◽  
Early Development ◽  
Sea Urchin ◽  
Actin Filaments ◽  
Cortical Granule ◽  
Cortical Actin ◽  
Phenotypic Changes ◽  
Sea Urchin Egg ◽  
Cortical Granule Exocytosis

The vitelline layer (VL) of a sea urchin egg is an intricate meshwork of glycoproteins that intimately ensheathes the plasma membrane. During fertilization, the VL plays important roles. Firstly, the receptors for sperm reside on the VL. Secondly, following cortical granule exocytosis, the VL is elevated and transformed into the fertilization envelope (FE), owing to the assembly and crosslinking of the extruded materials. As these two crucial stages involve the VL, its alteration was expected to affect the fertilization process. In the present study, we addressed this question by mildly treating the eggs with a reducing agent, dithiothreitol (DTT). A brief pretreatment with DTT resulted in partial disruption of the VL, as judged by electron microscopy and by a novel fluorescent polyamine probe that selectively labelled the VL. The DTT-pretreated eggs did not elevate the FE but were mostly monospermic at fertilization. These eggs also manifested certain anomalies at fertilization: (i) compromised Ca2+ signaling, (ii) blocked translocation of cortical actin filaments, and (iii) impaired cleavage. Some of these phenotypic changes were reversed by restoring the DTT-exposed eggs in normal seawater prior to fertilization. Our findings suggest that the FE is not the decisive factor preventing polyspermy and that the integrity of the VL is nonetheless crucial to the egg’s fertilization response.

Calcium-induced fusion of sea urchin egg secretory vesicles with planar phospholipid bilayer membranes

1999 ◽  
Vol 16 (1) ◽  
pp. 89-94 ◽  
Author(s):  
Alexandr Chanturiya, ◽  
Michael Whitaker, ◽  
Joshua Zimmerberg
Keyword(s):  
Sea Urchin ◽  
Phospholipid Bilayer ◽  
Secretory Vesicles ◽  
Bilayer Membranes ◽  
Sea Urchin Egg

scholarly journals Calcium Can Disrupt the SNARE Protein Complex on Sea Urchin Egg Secretory Vesicles without Irreversibly Blocking Fusion

1998 ◽  
Vol 273 (50) ◽  
pp. 33667-33673 ◽  
Author(s):  
Masahiro Tahara ◽  
Jens R. Coorssen ◽  
Kim Timmers ◽  
Paul S. Blank ◽  
Tim Whalley ◽  
...  
Keyword(s):  
Sea Urchin ◽  
Protein Complex ◽  
Secretory Vesicles ◽  
Snare Protein ◽  
Sea Urchin Egg
Sign in / Sign up

Export Citation Format

Share Document