The use of colloidal gold complexes in an ultrastructural study of lectin-binding sites and matrix deposition of normal human primary breast epithelium on collagen gels

1984 ◽  
Vol 16 (8) ◽  
pp. 819-834 ◽  
Author(s):  
Linda A. Peachey ◽  
Marie A. Smolira
Keyword(s):  
Ultrastructural Study ◽  
Binding Sites ◽  
Colloidal Gold ◽  
Lectin Binding ◽  
Collagen Gels ◽  
Breast Epithelium ◽  
Gold Complexes ◽  
Matrix Deposition ◽  
Normal Human ◽  
Lectin Binding Sites

scholarly journals Applications of immunocolloids in light microscopy. II. Demonstration of lectin-binding sites in paraffin sections by the use of lectin-gold or glycoprotein-gold complexes.

1983 ◽  
Vol 31 (4) ◽  
pp. 547-552 ◽  
Author(s):  
J Roth
Keyword(s):  
Binding Sites ◽  
Colloidal Gold ◽  
Rat Kidney ◽  
Lectin Binding ◽  
High Specificity ◽  
Step Method ◽  
Gold Complexes ◽  
Tissue Sections ◽  
One Step ◽  
Lectin Binding Sites

A new procedure is presented for the light microscopic demonstration of specific sugar sequences of oligosaccharides in glycoconjugates by lectins combined with the colloidal gold marker system. Tissue sections from aldehyde-fixed and paraffin embedded rat kidney were stained either in a one-step method with lectin directly bound to particles of colloidal gold or in a two-step method using non-labeled lectin and glycoprotein labeled with colloidal gold. In both methods the presence of lectin-binding sites in the tissue sections is revealed by the appearance of a red coloration that is due to the accumulation of gold particles. The high specificity of the technique is combined with a good sensitivity and resolution as demonstrated by a differential plasma membrane staining in renal epithelial cells. The lectin-gold or glycoprotein-gold complexes remain stable for months and produce a permanent nonbleaching staining.

scholarly journals Coloidal gold, ferritin and peroxidase as markers for electron microscopic double labeling lectin techniques.

1978 ◽  
Vol 26 (3) ◽  
pp. 163-169 ◽  
Author(s):  
J Roth ◽  
M Binder
Keyword(s):  
Particle Size ◽  
Cell Surface ◽  
Quantitative Evaluation ◽  
Binding Sites ◽  
Colloidal Gold ◽  
Lectin Binding ◽  
Electron Microscopic ◽  
Double Labeling ◽  
Optimal Amount ◽  
Lectin Binding Sites

Three markers, colloidal gold, ferritin and peroxidase, were checked for usefulness in double labeling of lectin-binding sites. The amount of various lectins for the stabilization of good sols of a different particle size was evaluated. Several lectin-gold complexes were prepared for electron microscopic labeling purposes, and the optimal amount of various lectins needed for stabilization of gold solutions of a different particle size was determined. The following combinations were investigated for their usefulness in labeling two different lectin-binding sites: lectin-gold and lectin-gold (different particle size), lectin-gold and lectin-ferritin, as well as lectin-ferritin and lectin-peroxidase. Of these combinations the latter did not give satisfactory results for double labeling. In all single and double labeling techniques with the above mentioned markers the quantitative evaluation of the number of lectin-binding sites is not feasible, but these techniques will be of considerable value for the investigation of the dynamics of different lectin-binding sites on the cell surface.

scholarly journals Applications of immunocolloids in light microscopy. III. Demonstration of antigenic and lectin-binding sites in semithin resin sections.

1984 ◽  
Vol 32 (10) ◽  
pp. 1075-1083 ◽  
Author(s):  
J M Lucocq ◽  
J Roth
Keyword(s):  
Submandibular Gland ◽  
Binding Sites ◽  
Lectin Binding ◽  
Protein A ◽  
Gold Complexes ◽  
Specific Staining ◽  
Maximum Information ◽  
Nomarski Differential Interference Contrast ◽  
Lowicryl K4m ◽  
Lectin Binding Sites

Previous studies have demonstrated that antigens or lectin-binding sites can be localized in sections from paraffin-embedded tissues with protein A or lectins bound to colloidal gold or colloidal silver (Roth J: J Histochem Cytochem 30:691, 1982 and 31:547, 1983). In the present study the protein A-gold technique and lectin-gold complexes have been applied to semithin sections (0.5-1.5 micron) of Epon- or low temperature Lowicryl K4M-embedded rat pancreas, kidney and submandibular gland. The results show that an increase in resolution and, therefore, in amount of information can be obtained. The optimal mode of imaging was determined on sections without counterstaining. Bright-field illumination gives the maximum information about the staining signal, while phase-contrast and Nomarski differential interference contrast give predominantly structural and, to a lesser extent, staining information. Polarization epi- and transillumination microscopy is inferior in all aspects. The application of a battery of lectin-gold complexes to rat submandibular gland revealed a specific staining pattern for each lectin in acinar and excretory duct cells.

Lectin-Binding Sites in Normal Human Testis/Lektinbindungsstellen normaler humaner Hoden

Andrologia ◽  
2009 ◽  
Vol 21 (2) ◽  
pp. 127-130 ◽  
Author(s):  
U. Wollina ◽  
G. Schreiber ◽  
C. Zollmann ◽  
C. Hipler ◽  
E. Günther
Keyword(s):  
Binding Sites ◽  
Lectin Binding ◽  
Human Testis ◽  
Normal Human ◽  
Lectin Binding Sites

Changes to desmosomal antigens and lectin-binding sites during differentiation in normal human epidermis: a quantitative ultrastructural study

1989 ◽  
Vol 92 (4) ◽  
pp. 667-677
Author(s):  
C.J. Skerrow ◽  
D.G. Clelland ◽  
D. Skerrow
Keyword(s):  
Electron Microscopy ◽  
Binding Sites ◽  
Light Microscope ◽  
Lectin Binding ◽  
Human Epidermis ◽  
Immunogold Electron Microscopy ◽  
Horny Layer ◽  
Subsequent Decrease ◽  
Normal Human ◽  
Lectin Binding Sites

During epidermal differentiation, desmosomes undergo a series of changes in their abundance, structure and properties, which has previously been defined by conventional electron microscopy and the use of antibodies to desmosomal proteins at the light-microscope level. Such changes in a major adhesive organelle would be expected to have a significant role in the maintenance of epidermal organization, and therefore require more detailed characterization. In the present study, modifications to certain desmosomal components in normal human epidermis have been located and quantified by immunogold electron microscopy. Antibodies to desmosomal protein dp3 and glycoprotein dg1 were used to label the cytoplasmic regions of the junctions and lectins concanavalin A (ConA) and wheat germ agglutinin (WGA) to probe the extracellular glycosylated material. Binding was measured at histologically defined levels and expressed as gold particles per microns of desmosome length (linear particle density: LPD). In addition, desmosome frequency, expressed as the percentage of the cell membrane length occupied by desmosomes, was measured. Highly significant changes in desmosome frequency, diameter and LPD were observed between epidermal strata and, in basal and upper horny cells, between different regions of the same cell surface. These parameters rose to a maximum in the spinous or granular layers: their subsequent decrease continued without interruption across the interface between the living and terminally differentiated horny layers. Remaining reactivity with antibodies, but not lectins, was almost completely abolished immediately before the final disintegration of the desmosome structure in the lower horny layer. In contrast, numerous large, highly immunoreactive desmosomes were retained up to the outer surface in the grossly thickened horny layer found in callus. Though the overall pattern of a rise followed by a fall was similar for all parameters measured, differences were observed between probes. Thus, the extent of the rise in available antigen between the lateral and apical surfaces of the basal cell was greater for dg1 than for dp3; the subsequent decrease in dp3 antigens in upper epidermal layers was more rapid than that for dg1, and changes to both antigens preceded those to lectin-binding sites. These results show that differences in desmosome frequency and in the size and antibody-binding characteristics of individual junctions underlie the heterogeneous distribution of desmosomal components within epidermis that is found by light-microscope immunocytochemistry. They further suggest that the disintegration of desmosomes within normal horny layer, which is an essential preliminary to desquamation, is the culmination of a sequence of events that begins in the upper living tissue and initially involves cytoplasmic components.(ABSTRACT TRUNCATED AT 400 WORDS)

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
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