scholarly journals Distribution of tubulin-containing structures in the egg of the sea urchin Strongylocentrotus purpuratus from fertilization through first cleavage.

1980 ◽  
Vol 84 (3) ◽  
pp. 668-679 ◽  
Author(s):  
P Harris ◽  
M Osborn ◽  
K Weber
Keyword(s):  
Sea Urchin ◽  
Indirect Immunofluorescence ◽  
Immunofluorescence Microscopy ◽  
Strongylocentrotus Purpuratus ◽  
Microtubule Depolymerization ◽  
Mitotic Apparatus ◽  
Indirect Immunofluorescence Microscopy ◽  
Sperm Aster

Eggs of the sea urchin Strongylocentrotus purpuratus were examined by indirect immunofluorescence microscopy for tubulin-containing structures at intervals from fertilization through first cleavage. The staining revealed that the monaster is made up not only of the sperm aster but also of tubulin-staining fibers originating elsewhere in the egg. The monaster does not divide directly but is broken down first before the amphiaster or interphase asters begin to form. The interphase asters reach a peak of development at the streak stage and are in turn broken down before the formation of the mitotic apparatus. The breakdown of the monaster, interphase asters, as well as the asters of the mitotic apparatus proceeds from the cell center or aster centers to the periphery of the cell and is followed by growth of new asters, also proceeding outward from the aster centers. The pattern suggests a transient wavelike movement of some condition, or factor, which favors microtubule depolymerization.

Non-plasmalemmal localisation of the major ganglioside in sea urchin eggs

Zygote ◽  
1993 ◽  
Vol 1 (3) ◽  
pp. 215-223 ◽  
Author(s):  
Hidehiko Shogomori ◽  
Kazuyoshi Chiba ◽  
Hideo Kubo ◽  
Motonori Hoshi
Keyword(s):  
Endoplasmic Reticulum ◽  
Sea Urchin ◽  
Indirect Immunofluorescence ◽  
Immunofluorescence Microscopy ◽  
Mitotic Apparatus ◽  
Sea Urchin Eggs ◽  
Indirect Immunofluorescence Microscopy ◽  
The One ◽  
Major Ganglioside ◽  
Hemicentrotus Pulcherrimus

SummaryM5 ganglioside (NeuGcα2–6Glcβl-' Cer) is the predominant glycosphingolipid in sea urchin eggs. Distribution of M5 ganglioside was studied in unfertilised and fertilised eggs of the sea urchin Hemicentrotus pulcherrimus by indirect immunofluorescence microscopy. In the cortices of unfertilised eggs, anti-M5 antibody strongly stained the submembranous, polygonal and tubular network of endoplasmic reticulum that was revealed by a membrane-staining dye, DiIC18(3). In addition to the cortical network of endoplasmic reticulum, at least two morphologically distinct vesicles were positive to the antibody. In the cortices isolated from fertilised eggs 30 min after insemination, the antibody stained only a similar network of endoplasmic reticulum, presumably the one reconstructed 5–10 min after fertilisation. During mitosis the endoplasmic reticulum is known to aggregate within the asters of the mitotic apparatus. Indeed, the antibody stained the asters and (more strongly) the vesicular components attaching to the periphery of the mitotic apparatus.

scholarly journals "Spiral asters" and cytoplasmic rotation in sea urchin eggs: induction in Strongylocentrotus purpuratus eggs by elevated temperature.

1985 ◽  
Vol 100 (4) ◽  
pp. 1056-1062 ◽  
Author(s):  
T E Schroeder ◽  
D E Battaglia
Keyword(s):  
Elevated Temperature ◽  
Sea Urchin ◽  
Elevated Temperatures ◽  
Strongylocentrotus Purpuratus ◽  
Inhibitory Effects ◽  
Cytological Evidence ◽  
Sea Urchin Eggs ◽  
Indirect Immunofluorescence Microscopy ◽  
Bright Field Microscopy ◽  
Sperm Aster

"Spiral asters" composed of swirls of subcortical microtubules were recently described in fertilized eggs of the sea urchin Strongylocentrotus purpuratus. In our study, these structures did not occur at culture temperatures below 16 degrees C. When the culture temperature was elevated, however, "spiral asters" routinely appeared during a susceptible period before mitotic prophase when the sperm aster-diaster normally exists. A massive and protracted rotation of the cytoplasm (excluding an immobile cortex and perinuclear region) began within 1 min of exposure to elevated temperature. Fibrils of the "spiral aster" could be seen within this rotating mass even by bright-field microscopy. The identity of microtubules in these structures was confirmed by indirect immunofluorescence microscopy. A mechanistic association between "spiral aster" formation and cytoplasmic rotation was indicated by the simultaneous inhibitory effects of microtubule and dynein poisons. Inhibitors of microfilaments, however, had no effect. We infer that elevated temperature induces unique changes in the microtubules of the pre-prophase sperm aster-diaster, resulting in cytoplasmic rotation and the spiral configuration of microtubules. Comparative cytological evidence supports the idea that "spiral asters" do not normally occur in fertilized sea urchin eggs. Biogeographic evidence for S. purpuratus indicates that fertilization and development naturally occur below 15 degrees C, hence "spiral asters" in eggs of this species should be regarded as abnormalities induced in the laboratory by unnaturally elevated temperatures.

scholarly journals Localization of protein disulfide isomerase to the external surface of the platelet plasma membrane

Blood ◽  
1995 ◽  
Vol 86 (6) ◽  
pp. 2168-2173 ◽  
Author(s):  
DW Essex ◽  
K Chen ◽  
M Swiatkowska
Keyword(s):  
Indirect Immunofluorescence ◽  
Blood Cells ◽  
Disulfide Bonds ◽  
Protein Disulfide Isomerase ◽  
Immunofluorescence Microscopy ◽  
External Surface ◽  
Platelet Surface ◽  
Disulfide Isomerase ◽  
Indirect Immunofluorescence Microscopy ◽  
Protein Disulfide

Protein disulfide isomerase (PDI) is an enzyme that catalyzes the formation as well as the isomerization of disulfide bonds. In this study, antibodies against PDI were used to show PDI antigen on the platelet surface by indirect immunofluorescence microscopy and by flow cytometry. The platelets were not activated, as evidenced by the absence of staining by an antibody against P-selectin. Permeabilized platelets showed little cytosolic PDI by indirect immunofluorescence microscopy, suggesting that the majority of platelet PDI is localized to the platelet surface. PDI activity against “scrambled” RNase was shown with intact platelets. The activity was inhibited by inhibitors of PDI and by an antibody against PDI. Other blood cells showed little PDI. Platelet surface PDI may play a role in the various physiological and pathophysiologic processes in which platelets are involved.

scholarly journals Studies on the Mitotic Apparatus of the Sea Urchin by Means of Antigen-Antibody Reactions in Agar

1959 ◽  
Vol 6 (3) ◽  
pp. 447-455 ◽  
Author(s):  
Hans A. Went
Keyword(s):  
Sea Urchin ◽  
Strongylocentrotus Purpuratus ◽  
Structural Elements ◽  
Agar Gel ◽  
Mitotic Apparatus ◽  
Insoluble Form ◽  
Molecular Origin ◽  
Antigen Antibody ◽  
Gel Diffusion ◽  
Immunochemical Relationship

The primary purpose of the experiments reported in this paper was to gain information on the molecular origin of the mitotic apparatus. Antisera were prepared against unfertilized sea urchin (Strongylocentrotus purpuratus) egg antigens and mitotic apparatus antigens. These were permitted to react with various antigen solutions in Ouchterlony agar gel diffusion plates, and the resultant precipitation patterns analysed. The results revealed that the mitotic apparatus contains probably no more than two antigens (precursor-1 component and precursor-2 component) and that these are shared by the unfertilized egg. Absorption and fractionation techniques indicated that in the unfertilized egg the precursor-1 component is present both as a "soluble" protein and as an insoluble form tenaciously associated with intracellular structural elements. A survey of dividing and non-dividing tissues for the precursor-1 component revealed that it was restricted to tissues in which mitotic activity could be detected microscopically. No immunochemical relationship could be detected between the mitotic apparatus and proteins extracted, by various methods, from the lantern muscle.

scholarly journals Localization of actin and microfilament-associated proteins in the microvilli and terminal web of the intestinal brush border by immunofluorescence microscopy.

1978 ◽  
Vol 79 (3) ◽  
pp. 839-845 ◽  
Author(s):  
A Bretscher ◽  
K Weber
Keyword(s):  
Epithelial Cells ◽  
Indirect Immunofluorescence ◽  
Brush Border ◽  
Immunofluorescence Microscopy ◽  
Intestinal Epithelial Cells ◽  
Intestinal Epithelial ◽  
Indirect Immunofluorescence Microscopy ◽  
Terminal Web ◽  
Intestinal Brush Border ◽  
Associated Proteins

Indirect immunofluorescence microscopy was used to localize microfilament-associated proteins in the brush border of mouse intestinal epithelial cells. As expected, antibodies to actin decorated the microfilaments of the microvilli, giving rise to a very intense fluorescence. By contrast, antibodies to myosin, tropomyosin, filamin, and alpha-actinin did not decorate the microvilli. All these antibodies, however, decorated the terminal web region of the brush border. Myosin, tropomyosin, and alpha-actinin, although present throughout the terminal web, were found to be preferentially located around the periphery of the organelle. Therefore, two classes of microfilamentous structures can be documented in the brush border. First, the highly ordered microfilaments which make up the cores of the microvilli apparently lack the associated proteins. Second, seemingly less-ordered microfilaments are found in the terminal web, in which region the myosin, tropomyosin, filamin and alpha-actinin are located.

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