scholarly journals Inside or Outside the Pits : Variable Mobility in Conspecific Sea Urchin, Anthocidaris crassispina (A. Agassiz)

1994 ◽  
Vol 36 (4) ◽  
pp. 255-266 ◽  
Author(s):  
Yoichi Yusa ◽  
Tomoko Yamamoto
Keyword(s):  
Sea Urchin ◽  
Anthocidaris Crassispina

scholarly journals Properties of an antiserum against native dynein 1 from sea urchin sperm flagella.

1977 ◽  
Vol 73 (1) ◽  
pp. 182-192 ◽  
Author(s):  
K Ogawa ◽  
D J Asai ◽  
C J Brokaw
Keyword(s):  
Atpase Activity ◽  
Sea Urchin ◽  
Strongylocentrotus Purpuratus ◽  
Beat Frequency ◽  
Bend Angle ◽  
Tryptic Fragment ◽  
Effective Inhibition ◽  
Dynein Arms ◽  
Sea Urchin Sperm ◽  
Anthocidaris Crassispina

Effects of an antiserum against native dynein 1 from sperm flagella of the sea urchin Strongylocentrotus purpuratus were compared with effects of an antiserum previously obtained against an ATPase-active tryptic fragment (fragment 1A) of dynein 1 from sperm flagella of the sea urchin, Anthocidaris crassispina. Both antisera precipitate dynein 1 and do not precipitate dynein 2. Only the fragment 1A antiserum precipitates fragment 1A and produces a measurable inhibition of dynein 1 ATPase activity. Both antisera inhibit the movement and the movement-coupled ATP dephosphorylation of reactivated spermatozoa. The inhibition of movement by the antiserum against dynein 1 is much less than by the antiserum against fragment 1A, suggesting that a specific interference with the active ATPase site may be required for effective inhibition of movement. Both antisera reduce the bend angle as well as the beat frequency of reactivated S. purpuratus spermatozoa, suggesting that the bend angle may depend on the activity of the dynein arms which generate active sliding.

scholarly journals Sea urchin (Anthocidaris crassispina) egg zinc-binding protein. Cellular localization, purification and characterization

1983 ◽  
Vol 211 (1) ◽  
pp. 109-118 ◽  
Author(s):  
H Ohtake ◽  
T Suyemitsu ◽  
M Koga
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Sea Urchin ◽  
Cellular Localization ◽  
Binding Protein ◽  
Gel Permeation Chromatography ◽  
Total Amino Acid ◽  
Amino Acid Residues ◽  
Gel Permeation ◽  
Anthocidaris Crassispina

Gel-filtration analysis of cytosol fraction obtained from unfertilized sea-urchin (Anthocidaris crassispina) eggs on Sephadex G-75 revealed the presence of two Zn-binding-protein fractions. The major Zn-binding protein fraction had a low molecular weight and a low absorbance at 280 nm, properties similar to those of the metallothionein found in the regenerating rat liver. These fractions were further purified by DEAE-cellulose and Sephadex G-50 chromatography. Homogeneity of the Zn-binding protein was judged by polyacrylamide-disc-gel electrophoresis and gel-permeation chromatography in the presence of 6 M-guanidinium chloride. The molecular weight determined by gel-permeation chromatography was 3900. This value is in good agreement with the minimum molecular weight calculated from the amino acid composition, which was 3655. Zn-binding protein is composed of 36 amino acid residues and the distinctive features include an extremely high content of cysteine, which accounted for one-third of the total amino acid residues, and a complete absence of aromatic amino acids, as well as of methionine, histidine and arginine. Zn-binding protein contained 4.1 g-atoms of zinc per mol and a trace of cadmium, but no copper, iron or calcium. The molar ratio of reactive thiol groups to metal ion was calculated to be 2.73:1. Possible roles of this Zn-binding protein in the homoeostasis of zinc in unfertilized sea-urchin eggs are discussed.

scholarly journals Inhibitory Effects of Echinochrome A, Isolated from Shell of the Sea Urchin Anthocidaris crassispina, on Antigen-Stimulated Degranulation in Rat Basophilic Leukemia RBL-2H3 Cells through Suppression of Lyn Activation

2016 ◽  
Vol 11 (9) ◽  
pp. 1934578X1601100
Author(s):  
Tomohiro Itoh ◽  
Azusa Fujiwara ◽  
Masayuki Ninomiya ◽  
Toshimichi Maeda ◽  
Masashi Ando ◽  
...  
Keyword(s):  
Sea Urchin ◽  
Intracellular Signaling ◽  
Immunoglobulin E ◽  
Inhibitory Effect ◽  
Biologically Active ◽  
Type I ◽  
Dependent Manner ◽  
Echinochrome A ◽  
Basophilic Leukemia ◽  
Anthocidaris Crassispina

Echinochrome A (Echi-A) was isolated from the sea urchin Anthocidaris crassispina and its structure determined using 1D and 2D-NMR. In the present study, we examined the inhibitory effect of Echi-A on antigen-stimulated degranulation in rat basophilic leukemia RBL-2H3 cells, which were suppressed in a dose dependent manner. The antigens bind to the high affinity immunoglobulin E receptor, which is expressed on the surface of mast cells and basophils and activate intracellular signal transduction, resulting in the release of biologically active mediators such as histamine. In order to disclose the inhibitory mechanisms of degranulation by Echi-A, we examined the elevation in intracellular Ca2+ concentration ([Ca2+]i), production levels of intracellular reactive oxygen species (ROS) and early intracellular signaling events. Both elevation of [Ca2+]i and intracellular ROS production were markedly suppressed in cells treated with Echi-A. Echi-A also suppressed the activation of Lyn, Syk, and PLCγ1/2 in antigen-stimulated cells. These results indicated that inhibition of antigen-stimulated degranulation in RBL-2H3 cells by Echi-A is mainly due to the inactivation of Lyn/Syk/PLCγ signaling pathways. Our findings suggest that Echi-A could be a beneficial agent for alleviating the symptoms of type I allergy.

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