Cortical microtubule involvement in bordered pit formation in secondary xylem vessel elements ofAesculus hippocastanum L. (Hippocastanaceae): A correlative study using electron microscopy and indirect immunofluorescence microscopy

PROTOPLASMA ◽  
1997 ◽  
Vol 197 (1-2) ◽  
pp. 64-75 ◽  
Author(s):  
N. J. Chaffey ◽  
J. R. Barnett ◽  
P. W. Barlow
Keyword(s):  
Electron Microscopy ◽  
Indirect Immunofluorescence ◽  
Immunofluorescence Microscopy ◽  
Secondary Xylem ◽  
Cortical Microtubule ◽  
Xylem Vessel ◽  
Correlative Study ◽  
Pit Formation ◽  
Indirect Immunofluorescence Microscopy ◽  
Vessel Elements

scholarly journals Intermediate-sized filaments of human endothelial cells.

1979 ◽  
Vol 81 (3) ◽  
pp. 570-580 ◽  
Author(s):  
W W Franke ◽  
E Schmid ◽  
M Osborn ◽  
K Weber
Keyword(s):  
Electron Microscopy ◽  
Endothelial Cells ◽  
Smooth Muscle ◽  
Indirect Immunofluorescence ◽  
Immunofluorescence Microscopy ◽  
Major Protein ◽  
Human Endothelial Cells ◽  
Specific Antibodies ◽  
Indirect Immunofluorescence Microscopy ◽  
Polypeptide Band

Human endothelial cells prepared from unbilical cords are characterized in parallel by electron microscopy and indirect immunofluorescence microscopy using specific antibodies against different classes of intermediate-sized filaments. The strongly developed, loose bundles of intermediate-sized filaments typically found in these cells are not decorated by antibodies against prekeratin or antibodies against smooth muscle desmin. They are, however, strongly decorated by antibodies directed against murine "vimentin," i.e., the 57,000 mol wt polypeptide which is the major protein of the intermediate-sized filaments predominant in various cells of mesenchymal origin. Cytoskeletal preparations greatly enriched in intermediate-sized filaments show the enrichment of a polypeptide band comigrating with murine vimentin. This shows that the intermediate-sized filaments that are abundant in human endothelial cells are predominantly of the vimentin type and can be demonstrated by their cross-reaction with the vimentin of rodents. These data also strengthen the evidence for several subclasses of intermediate-sized filaments, which can be distinguished by immunological procedures.

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.

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 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.

Sign in / Sign up

Export Citation Format

Share Document