Stereoselective synthesis of a 9-O-sulfo Neu5Gc-capped O-linked oligosaccharide found on the sea urchin egg receptor

2019 ◽  
Vol 6 (1) ◽  
pp. 54-61 ◽  
Author(s):  
Anindya Das ◽  
Pei-Jhen Li ◽  
Avijit K. Adak ◽  
Hsin-Ru Wu ◽  
Mohammad Tarique Anwar ◽  
...  
Keyword(s):  
Total Synthesis ◽  
Sea Urchin ◽  
Stereoselective Synthesis ◽  
Egg Cell ◽  
Cell Surfaces ◽  
Sea Urchin Egg

The first total synthesis of a serine bearing α2→5-Oglycolyl-linked oligoNeu5Gc found on sea urchin egg cell surfaces has been accomplished.

scholarly journals Electrophoretic movement of fertilized sea-urchin eggs

1982 ◽  
Vol 55 (1) ◽  
pp. 105-113
Author(s):  
N. Oshima
Keyword(s):  
Electric Field ◽  
Surface Charge ◽  
Electrophoretic Mobility ◽  
Sea Urchin ◽  
Egg Cell ◽  
Migration Speed ◽  
Protamine Sulphate ◽  
Sea Urchin Egg ◽  
Fertilization Membrane ◽  
Whole Egg

The eccentric shift of the sea-urchin egg within the fertilization membrane under an electric field was analysed by measuring the electrophoretic mobility of the isolated fertilization membrane and that of the egg deprived of the fertilization membrane. In addition, the migration speed of the egg proper was measured within the fertilization membrane under the conditions that: either (1) the movement of the whole egg was arrested, or (2) protamine sulphate was adsorbed on the fertilization membrane to reduce its mobility. The results led to conclusions that: (1) both the fertilization membrane and the egg cell with the hyaline layer are negatively charged; (2) movement of the normal fertilized eggs is due mainly to the surface charge of the fertilization membrane; and (3) the eccentric position of the egg within the fertilization membrane is due to migration of the egg proper, which is independent of the movement of the whole egg.

scholarly journals The Occurrence of Novel 9-O-SulfatedN-Glycolylneuraminic Acid-capped 25-O-linked Oligo/PolyNeu5Gc Chains in Sea Urchin Egg Cell Surface Glycoprotein

1996 ◽  
Vol 271 (12) ◽  
pp. 6694-6701 ◽  
Author(s):  
Shinobu Kitazume ◽  
Ken Kitajima ◽  
Sadako Inoue ◽  
Stuart M. Haslam ◽  
Howard R. Morris ◽  
...  
Keyword(s):  
Cell Surface ◽  
Sea Urchin ◽  
Surface Glycoprotein ◽  
Egg Cell ◽  
Cell Surface Glycoprotein ◽  
Sea Urchin Egg

scholarly journals Identification of the sea urchin egg receptor for sperm using an antiserum raised against a fragment of its extracellular domain.

1992 ◽  
Vol 116 (3) ◽  
pp. 647-658 ◽  
Author(s):  
K R Foltz ◽  
W J Lennarz
Keyword(s):  
Cell Surface ◽  
Sea Urchin ◽  
Egg Cell ◽  
Cortical Granule ◽  
Dependent Manner ◽  
Western Blots ◽  
Cell Surface Glycoprotein ◽  
Sperm Binding ◽  
Sea Urchin Egg ◽  
Species Specific

Sea urchin egg fertilization requires the species-specific interaction of molecules on the sperm and egg surfaces. Previously, we isolated an extracellular, 70-kD glycosylated fragment of the S. purpuratus egg receptor for sperm by treating the eggs with lysylendoproteinase C (Foltz, K. R., and W. J. Lennarz. 1990. J. Cell Biol. 111:2951-2959). To characterize the receptor further, we have generated a polyclonal antiserum (anti-70KL) against the purified 70-kD fragment. Anti-70KL was found to react with a single polypeptide of approximately 350 kD on Western blots, presumed to be the intact receptor, in an egg cell surface preparation. This polypeptide appeared to be tightly associated with the plasma membrane/vitelline layer complex, as it was released from these preparations only by detergent treatment. Immunofluorescence microscopy revealed that the receptor was distributed evenly over the egg surface. The anti-70KL was species specific both in its ability to recognize the egg surface protein and to inhibit sperm binding. Fab fragments generated from affinity-purified anti-70KL also bound to the egg surface and inhibited sperm binding in a concentration-dependent manner. Interestingly, treatment with Fabs caused a small percentage of eggs to undergo cortical granule exocytosis, even in the absence of external Ca2+. These results confirm earlier findings indicating that the receptor is a cell surface glycoprotein of high molecular weight that species specifically binds sperm. This antiserum provides a powerful tool for further investigation of gamete interactions and the structure of the sperm receptor.

Nuclear Envelope Formation In Vitro: A Sea Urchin Egg Cell-Free System

2008 ◽  
pp. 207-223 ◽  
Author(s):  
Richard D. Byrne ◽  
Vanessa Zhendre ◽  
Banafshé Larijani ◽  
Dominic L. Poccia
Keyword(s):  
Nuclear Envelope ◽  
Sea Urchin ◽  
Egg Cell ◽  
Free System ◽  
Cell Free System ◽  
Sea Urchin Egg ◽  
Nuclear Envelope Formation

Immunogold and immunoblot studies on a cell surface protein found in primary mesenchyme cells and in the cortical secretory vesicles of the sea urchin egg

1987 ◽  
Vol 45 ◽  
pp. 832-833
Author(s):  
G.L. Decker ◽  
M.C. Valdizan
Keyword(s):  
Cell Surface ◽  
Sea Urchin ◽  
Surface Protein ◽  
Egg Cell ◽  
Secretory Vesicles ◽  
Cell Surface Protein ◽  
Surface Complexes ◽  
Mesenchyme Cells ◽  
Lowicryl K4m ◽  
Primary Mesenchyme Cells

A monoclonal antibody designated MAb 1223 has been used to show that primary mesenchyme cells of the sea urchin embryo express a 130-kDa cell surface protein that may be directly involved in Ca2+ uptake required for growth of skeletal spicules. Other studies from this laboratory have shown that the 1223 antigen, although in relatively low abundance, is also expressed on the cell surfaces of unfertilized eggs and on the majority of blastomeres formed prior to differentiation of the primary mesenchyme cells.We have studied the distribution of 1223 antigen in S. purpuratus eggs and embryos and in isolated egg cell surface complexes that contain the cortical secretory vesicles. Specimens were fixed in 1.0% paraformaldehyde and 1.0% glutaraldehyde and embedded in Lowicryl K4M as previously reported. Colloidal gold (8nm diameter) was prepared by the method of Mulpfordt.

Concise Total Synthesis of Curvulone B

Synlett ◽  
2020 ◽  
Author(s):  
Debendra K. Mohapatra ◽  
Shivalal Banoth ◽  
Utkal Mani Choudhury ◽  
Kanakaraju Marumudi ◽  
Ajit C. Kunwar
Keyword(s):  
Total Synthesis ◽  
Stereoselective Synthesis ◽  
Ring System ◽  
Bond Forming ◽  
Cross Metathesis ◽  
Bond Forming Reactions ◽  
Key Steps

AbstractA concise and convergent stereoselective synthesis of curvulone B is described. The synthesis utilized a tandem isomerization followed by C–O and C–C bond-forming reactions following Mukaiyama-type aldol conditions for the construction of the trans-2,6-disubstituted dihydropyran ring system as the key steps. Other important features of this synthesis are a cross-metathesis, epimerization, and Friedel–Crafts acylation.

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.

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