Tension at the Surface of Sea-Urchin Egg: A Critical Examination of Cole's Experiment

1964 ◽  
Vol 41 (4) ◽  
pp. 893-906 ◽  
Author(s):  
MITSUKI YONEDA
Keyword(s):  
Surface Area ◽  
Sea Urchin ◽  
Contact Area ◽  
Surface Force ◽  
Critical Examination ◽  
Compression Method ◽  
Osmotic Swelling ◽  
Technical Errors ◽  
Sea Urchin Egg ◽  
Hemicentrotus Pulcherrimus

1. The compression method for calculating the surface force of the sea-urchin egg, developed by Cole (1932), has been critically repeated using unfertilized eggs of Hemicentrotus pulcherrimus. 2. Estimation of contact area involved in Cole's equation introduces technical errors. 3. The tension recalculated by another equation including surface area as a parameter is found to remain constant irrespective of change in surface area. This is in conflict with the classical belief that the cortex of the egg of sea urchin is elastic. 4. Neither osmotic swelling nor osmotic shrinkage of the egg affects the tension.

scholarly journals A 45,000-mol-wt protein-actin complex from unfertilized sea urchin egg affects assembly properties of actin.

1984 ◽  
Vol 99 (3) ◽  
pp. 994-1001 ◽  
Author(s):  
H Hosoya ◽  
I Mabuchi
Keyword(s):  
Sea Urchin ◽  
Actin Filament ◽  
Actin Polymerization ◽  
Initial Rate ◽  
Gel Filtration ◽  
Molar Ratio ◽  
Capping Protein ◽  
Sea Urchin Egg ◽  
Rate Of Polymerization ◽  
Hemicentrotus Pulcherrimus

A one-to-one complex of a 45,000-mol-wt protein and actin was purified from unfertilized eggs of the sea urchin, Hemicentrotus pulcherrimus, by means of DNase l-Sepharose affinity and gel filtration column chromatographies. Effects of the complex on the polymerization of actin were studied by viscometry, spectrophotometry, and electron microscopy. The results are summarized as follows: (a) The initial rate of actin polymerization is inhibited at a very low molar ratio of the complex to actin. (b) Acceleration of the initial rate of polymerization occurs at a relatively high, but still substoichiometric, molar ratio of the complex to actin. (c) Annealing of F-actin fragments is inhibited by the complex. (d) The complex prevents actin filaments from depolymerizing. (e) Growth of the actin filament is inhibited at the barbed end. In all cases except b, a molar ratio of less than 1:100 of the 45,000-mol-wt protein-actin complex to actin is sufficient to produce these significant effects. These results indicate that the 45,000-mol-wt protein-actin complex from the sea urchin egg regulates the assembly of actin by binding to the barbed end (preferred end or rapidly growing end) of the actin filament. The 45,000-mol-wt protein-actin complex can thus be categorized as a capping protein.

Tension at the Surface of the Dividing Sea-Urchin Egg

1972 ◽  
Vol 57 (3) ◽  
pp. 575-587 ◽  
Author(s):  
MITSUKI YONEDA ◽  
KATSUMA DAN
Keyword(s):  
Sea Urchin ◽  
Computer Method ◽  
Sharp Peak ◽  
Compression Method ◽  
Sea Urchin Egg ◽  
Cyclic Changes

1. Cyclic changes in tension correlating with the division cycle were demonstrated by compression method of Cole. 2. A sharp peak in the tension was found 8 min before the onset of cleavage at 13°C 3. A computer method indicated that the tension reached a maximum at the start of cleavage, after which it steadily decreased throughout the course of cleavage. 4. A rough estimation revealed that the force of constriction at the equatorial ring amounted to 6 x 10-3 dyne, which compares well with Rappaport's result (1967).

Molecular cloning and characterization of ryanodine receptor from unfertilized sea urchin eggs

2002 ◽  
Vol 282 (3) ◽  
pp. R727-R737 ◽  
Author(s):  
Mieko Shiwa ◽  
Takashi Murayama ◽  
Yasuo Ogawa
Keyword(s):  
Ryanodine Receptor ◽  
Sea Urchin ◽  
Sea Urchins ◽  
Structural Features ◽  
Release Channel ◽  
Terminal Domain ◽  
Sea Urchin Egg ◽  
Cyclic Adp Ribose ◽  
Hemicentrotus Pulcherrimus

Unfertilized eggs of sea urchins ( Hemicentrotus pulcherrimus) demonstrated cyclic ADP-ribose (cADPR)-induced Ca2+ release and caffeine-induced Ca2+ release, both of which were considered to be mediated through the ryanodine receptor (RyR). We cloned cDNAs for sea urchin egg RyR (suRyR), which encode a 597-kDa protein of 5,317 amino acids. suRyR shares common structural features with known RyRs: the well-conserved COOH-terminal domain, which forms a functional Ca2+ channel, and a large hydrophilic NH2-terminal domain. suRyR shows amino acid sequence identity (43–45%) similar to the three mammalian RyR isoforms. Phylogenetic analysis indicates that suRyR branched from three isoforms of vertebrates before they diverged, suggesting that suRyR may be the only RyR isoform in the sea urchin. Four in-frame insertions were found in suRyR cDNAs, one of which was novel and unique, in that it had a cluster of serine residues. The transcripts with and without these insertions were found in the egg RNA. These results suggest that suRyR may be expressed as a functional Ca2+-induced Ca2+ release channel, which might also be involved in cADPR-induced Ca2+ release.

scholarly journals Involvement of Huntingtin in Development and Ciliary Beating Regulation of Larvae of the Sea Urchin, Hemicentrotus pulcherrimus

2021 ◽  
Vol 22 (10) ◽  
pp. 5116
Author(s):  
Hideki Katow ◽  
Tomoko Katow ◽  
Hiromi Yoshida ◽  
Masato Kiyomoto
Keyword(s):  
Sea Urchin ◽  
The Body ◽  
Brdu Incorporation ◽  
Wild Type ◽  
Blastula Stage ◽  
Ciliary Beating ◽  
Marker Proteins ◽  
Disease Protein ◽  
Pattern Regulation ◽  
Hemicentrotus Pulcherrimus

The multiple functions of the wild type Huntington’s disease protein of the sea urchin Hemicentrotus pulcherrimus (Hp-Htt) have been examined using the anti-Hp-Htt antibody (Ab) raised against synthetic oligopeptides. According to immunoblotting, Hp-Htt was detected as a single band at around the 350 kDa region at the swimming blastula stage to the prism larva stage. From the 2-arm pluteus stage (2aPL), however, an additional smaller band at the 165 kDa region appeared. Immunohistochemically, Hp-Htt was detected in the nuclei and the nearby cytoplasm of the ectodermal cells from the swimming blastula stage, and the blastocoelar cells from the mid-gastrula stage. The Ab-positive signal was converged to the ciliary band-associated strand (CBAS). There, it was accompanied by several CBAS-marker proteins in the cytoplasm, such as glutamate decarboxylase. Application of Hp-Htt morpholino (Hp-Htt-MO) has resulted in shortened larval arms, accompanied by decreased 5-bromo-2-deoxyuridin (BrdU) incorporation by the ectodermal cells of the larval arms. Hp-Htt-MO also resulted in lowered ciliary beating activity, accompanied by a disordered swirling pattern formation around the body. These Hp-Htt-MO-induced deficiencies took place after the onset of CBAS system formation at the larval arms. Thus, Hp-Htt is involved in cell proliferation and the ciliary beating pattern regulation signaling system in pluteus larvae.

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
Sign in / Sign up

Export Citation Format

Share Document