scholarly journals Cytochemical demonstration of lectin binding sites in rod photoreceptor cells and interphotoreceptor matrix of rat retinas by labeling frozen thin-sections with various lectins.

1989 ◽  
Vol 22 (6) ◽  
pp. 605-616 ◽  
Author(s):  
TAKASHI KITAOKA ◽  
KAZUSHI FUJIMOTO ◽  
SATOKI UENO ◽  
YOSHIHITO HONDA ◽  
KAZUO OGAWA
Keyword(s):  
Binding Sites ◽  
Lectin Binding ◽  
Photoreceptor Cells ◽  
Rod Photoreceptor ◽  
Thin Sections ◽  
Cytochemical Demonstration ◽  
Interphotoreceptor Matrix ◽  
Lectin Binding Sites

Localization of lectin binding sites in the lens of rats: A study by a labeling frozen thin-section method

1990 ◽  
Vol 48 (3) ◽  
pp. 918-919
Author(s):  
Toshikazu Tanaka ◽  
Masahiro Sakai ◽  
Nobuo Ihara ◽  
Yoshihito Honda ◽  
Kazuo Ogawa
Keyword(s):  
Thin Section ◽  
Binding Sites ◽  
Structural Characteristics ◽  
Lectin Binding ◽  
Light Microscope Level ◽  
Thin Sections ◽  
Section Method ◽  
Cell Membrane Proteins ◽  
Complex Procedure ◽  
Lectin Binding Sites

In various tissues, many investigators have reported that sugar residues of cell-membrane proteins participate important functions such as cellular recognition, adhesion and differentiation. As an organ, the lens has distinct polarity from anterior to posterior face as one of its unique structural characteristics. However, a only few studies have been performed about the localization of sugar residues at light-microscope level. The purpose of this study is to detect lectin binding sites in lenses of normal rats and Ihara Cataract Rats (ICR) by utilizing a labeling frozen thin-section method.The lectins, concanavalin A (Con A) and wheat germ agglutinin (WGA) were used in this study. Wistar rats and ICR rats which develop hereditary cataracts were used as experimental animals. For light microscopy, frozen semi-thin sections were stained with the lectins, using an avidin-biotin-complex procedure and visualized by incubation with 0.1% diaminobenzidine (DAB) and 0.01% H2O2 in PBS.

scholarly journals Regional distribution of N-acetyl-D-galactosamine residues in the glycocalyx of glomerular podocytes.

1983 ◽  
Vol 96 (5) ◽  
pp. 1189-1196 ◽  
Author(s):  
J Roth ◽  
D Brown ◽  
L Orci
Keyword(s):  
Basement Membrane ◽  
Cell Surface ◽  
Binding Sites ◽  
Wheat Germ ◽  
Lectin Binding ◽  
Glomerular Cell ◽  
Thin Sections ◽  
Foot Process ◽  
Wheat Germ Lectin ◽  
Lectin Binding Sites

Helix pomatia lectin (HPL) bound to colloidal gold was used as a specific cytochemical probe for the localization of terminal nonreducing N-acetyl-D-galactosamine residues in thin sections of rat kidney. In the glomerulus, lectin-binding sites were associated only with the podocyte foot process bases and were not found on the free cell surface of podocytes or on any other glomerular components. Gold-particle label was often arranged in the form of clusters which extended from the foot process base to the lamina rare externa and lamina densa of the basement membrane. In contrast, wheat germ lectin (WGL)-binding sites (beta-[1 leads to 4] linked N-acetyl-D-glucosamine residues and N-acetylneuraminic acid residues) were found in all regions of the podocyte plasma membrane and on the cell surface of all other glomerular cell types. In addition, WGL-binding sites were present in all three layers of the glomerular basement membrane (GBM) as well as in the mesangial matrix. A quantitative evaluation of the pattern of labeling for HPL-binding sites together with the sugar specificity of this lectin suggest that a component of the glycocalyx is being detected rather than a basement membrane component. This was confirmed by the absence of H. pomatia lectin-binding sites in preparations of isolated GBM which retained, however, wheat germ lectin-binding sites. These data show that the glycocalyx of the foot process base is a highly specialized cell surface domain with respect to its carbohydrate composition.

Localization of fluorescence-labeled lectin binding sites on photoreceptor cells of the monkey retina

1983 ◽  
Vol 36 (1) ◽  
pp. 113-123 ◽  
Author(s):  
Fumiyuki Uehara ◽  
Munefumi Sameshima ◽  
Takashi Muramatsu ◽  
Norio Ohba
Keyword(s):  
Binding Sites ◽  
Lectin Binding ◽  
Photoreceptor Cells ◽  
Lectin Binding Sites

Detection of glycoconjugates by lectins and glycosylated ferritin in the ciliary membrane of the quail oviduct

1978 ◽  
Vol 36 (2) ◽  
pp. 298-299
Author(s):  
Daniel Sandoz ◽  
Emmanuelle Boisvieux-Ulrich ◽  
Bernadette Chailley
Keyword(s):  
Binding Sites ◽  
Wheat Germ ◽  
External Surface ◽  
Lectin Binding ◽  
Good Resolution ◽  
Con A ◽  
Thin Sections ◽  
Ciliary Membrane ◽  
Wheat Germ Lectin ◽  
Lectin Binding Sites

The freeze-fractures of ciliary membrane show very few intramembrane particles except'for the ciliary necklace, located at the base of the organelle, which is composed of several sinuous arrays of particles (Fig.a). In the quail oviduct, it is also possible to distinguish these particles in thin sections, they appear as beads on the external surface of the ciliary membrane (Fig.b).Glycosylated ferritin allows the detection with a good resolution of the lectin binding sites of the plasma membrane.Pieces of quail oviduct (magnum) were incubated, after glutaralde- hyde fixation,either with Concanavaline A (major affinity : mannosyl or glucosyl residues), or wheat germ lectin (WGA)(major affinity : N-acetyl- glucosamine or N-acety1-neuraminic acid residues). The bound Con A molecules were visualized by Mannosyl-Ferritin. Control specimens were incubated directly with Mannosyl-Ferritin without prior incubation with Con A or with Con A in presence of 0-methyl-α -D-mannosyl-pyranoside.

Lectin-binding sites in chick limb buds

1989 ◽  
Vol 27 ◽  
pp. 82
Author(s):  
M. Narita ◽  
K. Yamashita ◽  
M. Yasuda
Keyword(s):  
Binding Sites ◽  
Lectin Binding ◽  
Limb Buds ◽  
Lectin Binding Sites

Ultrastructural demonstration of lectin binding sites in the Golgi apparatus of rat epiphyseal chondrocytes

1988 ◽  
Vol 89 (2) ◽  
pp. 177-184 ◽  
Author(s):  
A. Velasco ◽  
J. Hidalgo ◽  
M. M�ller ◽  
G. Garcia-Herdugo
Keyword(s):  
Golgi Apparatus ◽  
Binding Sites ◽  
Lectin Binding ◽  
Lectin Binding Sites

scholarly journals Visualization of intracellular concanavalin A binding sites in retinal photoreceptors.

1978 ◽  
Vol 26 (10) ◽  
pp. 822-828 ◽  
Author(s):  
I Nir
Keyword(s):  
Concanavalin A ◽  
Binding Sites ◽  
Photoreceptor Cells ◽  
Con A ◽  
Thin Sections ◽  
Glycol Methacrylate ◽  
Outer Segments ◽  
Retinal Photoreceptors ◽  
Carbohydrate Components ◽  
The Relationship

Localization of carbohydrate components in retinal photoreceptor cells and membranes was studied. Frog and rat retinas were fixed with glutaraldehyde and embedded in glycol methacrylate or in a mixture of glycol methacrylate, glutaraldehyde and urea. Thin sections were incubated with ferritin-labeled concanavalin A (F-Con A) and stained with osmium vapors. Intensive binding was observed in both rod and cone outer segments. In the rod inner segment, differential binding of F-Con A was demonstrated. While numerous ferritin granules were observed in the myoid zone, only a few were seen in the ellipsoid zone, except for a local accumulation along the plasma membrane. In the rod outer segment, Con A binding sites were closely associated with the disk membranes. Ferritin granules were observed on both sides of the membranes. The relationship between the localization of Con A binding sites and the orientation of visual pigment molecules within the rod outer segments disk membranes was discussed.

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