scholarly journals Lectin binding sites in kidney. A comparative study of 14 animal species.

1983 ◽  
Vol 31 (4) ◽  
pp. 531-537 ◽  
Author(s):  
H Holthöfer
Keyword(s):  
Animal Species ◽  
Specific Binding ◽  
Lectin Binding ◽  
Basement Membranes ◽  
Fresh Water Fish ◽  
Dolichos Biflorus ◽  
Tissue Sections ◽  
Distal Tubules ◽  
Species Specific ◽  
Lectin Binding Sites

Six fluorochrome-coupled lectins with different sugar specificities were used to stain frozen tissue sections of kidneys from 14 animal species including mammals, avians, reptiles, and fresh water fish. Each lectin seemed to have a species-, but not strain-, specific binding pattern. Some lectins, however, bound to the same parts of the nephron in all animals studied. Wheat germ agglutinin (WGA) bound prominently to glomeruli in all kidneys. Dolichos biflorus agglutinin (DBA) seemed to bind to only a group of distal tubules in most animals, whereas either proximal or distal tubules were revealed with soybean (SBA) and peanut (PNA) agglutinins. Heterogeneity of basement membranes in different nephron parts was seen in the binding of some lectins. Ulex europeus agglutinin (UEA I), binding specifically to endothelial cells in human tissues, did not react with the endothelium of any other species, but SBA and PNA seemed to prominently stain vascular endothelia of cow and hen vessels, respectively. These results show a species-specific compartmentalization of saccharides to certain parts of the nephron, while there appears to be some common features in saccharide distribution between different animal species as well.

Ultrastructural localization of lectin-binding sites in different basement membranes

1993 ◽  
Vol 25 (6) ◽  
pp. 464-468 ◽  
Author(s):  
Mehrdad Salamat ◽  
Werner G�tz ◽  
J�rgen Werner ◽  
Rainer Merken
Keyword(s):  
Binding Sites ◽  
Lectin Binding ◽  
Ultrastructural Localization ◽  
Basement Membranes ◽  
Lectin Binding Sites

Nerve-induced secretion of glycoconjugates from cat submandibular glands: a correlative study with lectin probes on tissues and saliva.

1992 ◽  
Vol 40 (11) ◽  
pp. 1751-1759 ◽  
Author(s):  
D C Winston ◽  
G B Proctor ◽  
J R Garrett ◽  
B A Schulte ◽  
G N Thomopoulos
Keyword(s):  
Lectin Binding ◽  
Tissue Kallikrein ◽  
Western Blots ◽  
Dolichos Biflorus ◽  
Submandibular Glands ◽  
Cellular Origin ◽  
Tissue Sections ◽  
Secretory Glycoproteins ◽  
Submandibular Saliva

Horseradish peroxidase-conjugated lectins were used on tissue sections to localize the main secretory glycoproteins in cat submandibular glands and on Western blots to evaluate their movement into saliva with selective nerve stimulation. Central acinar cells bound lectins from Arachis hypogaea (PNA) specific for the terminal disaccharide Gal beta 1, 3GalNac, Griffonia simplifolia (GSA I-B4) specific for terminal alpha Gal, and Lotus tetragonolobus (LTA) specific for fucose. Lectins from Limax flavus (LFA) specific for sialic acid and Dolichos biflorus (DBA) specific for terminal alpha GalNac reacted preferentially with demilunar cells, whereas apical granules in striated ducts were recognized principally by LTA. Parasympathetic stimulation promoted the release of lectin-reactive glycoconjugates from both central and demilunar cells. In contrast, sympathetic stimulation caused almost complete release of LTA-reactive granules in striated ducts and only moderate secretion from demilunar cells. Lectin blots of stimulated saliva discriminated many of the constituent bands, providing information about their glycosylation. Several bands were common to both parasympathetic and sympathetic saliva, and many bands gave wider ranges of lectin binding than anticipated from the histochemistry. The major component in parasympathetic saliva was a glycoconjugate of less than 12 KD which reacted with every lectin tested. Lectin blots of sympathetic saliva showed a prominent diffuse LTA-reactive band around 33 KD, which was attributed to tissue kallikrein. The identity and cellular origin of most bands in stimulated submandibular saliva are still unclear but the technique shows considerable promise for improving the recognition and characterization of individual glycoconjugates.

Lectin Binding Characteristics of Laryngeal Cancer

1989 ◽  
Vol 100 (3) ◽  
pp. 207-209 ◽  
Author(s):  
Raphael Feinmesser ◽  
Jeremy L. Freeman ◽  
Arnold Noyek ◽  
Peter Van Nostrand
Keyword(s):  
Laryngeal Cancer ◽  
Binding Sites ◽  
Specific Binding ◽  
Lectin Binding ◽  
Peanut Lectin ◽  
Binding Characteristics ◽  
Mn Blood Group ◽  
Glycoprotein Structure ◽  
Oncodevelopmental Antigen ◽  
Lectin Binding Sites

Previous reports have shown specific binding characteristics of peanut lectin to a variety of lymphatic and epithelial tumors. This study demonstrates the presence of lectin binding sites on cell membrane of laryngeal cancer cells, but not on adjacent normal epithelial linings. It also demonstrates the presence of glycoconjugates responsible for lectin adherence in fetal larynges. The Thomsen-Friedenreich antigen is a glycoprotein structure participating in the structure of the MN blood group antigen. It is also the structure that binds the peanut agglutinin. Perhaps this antigen, which we found on fetal larynges as well as on malignant laryngeal epithelial lining, is another oncodevelopmental antigen.

scholarly journals Descriptive Comparison of ELISAs for the Detection of Toxoplasma gondii Antibodies in Animals: A Systematic Review

Pathogens ◽  
2021 ◽  
Vol 10 (5) ◽  
pp. 605
Author(s):  
K. L. D. Tharaka D. Liyanage ◽  
Anke Wiethoelter ◽  
Jasmin Hufschmid ◽  
Abdul Jabbar
Keyword(s):  
Systematic Review ◽  
Toxoplasma Gondii ◽  
Animal Species ◽  
Specific Binding ◽  
Protein A ◽  
Cross Reactivity ◽  
Meat Juice ◽  
Wide Range ◽  
Eimeria Spp ◽  
Species Specific

Toxoplasma gondii is the zoonotic parasite responsible for toxoplasmosis in warm-blooded vertebrates. This systematic review compares and evaluates the available knowledge on enzyme-linked immunosorbent assays (ELISAs), their components, and performance in detecting T. gondii antibodies in animals. Four databases were searched for published scientific studies on T. gondii and ELISA, and 57 articles were included. Overall, indirect (95%) and in-house (67%) ELISAs were the most used types of test among the studies examined, but the ‘ID Screen® Toxoplasmosis Indirect Multi-species’ was common among commercially available tests. Varying diagnostic performance (sensitivity and specificity) and Kappa agreements were observed depending on the type of sample (serum, meat juice, milk), antigen (native, recombinant, chimeric) and antibody-binding reagents used. Combinations of recombinant and chimeric antigens resulted in better performance than native or single recombinant antigens. Protein A/G appeared to be useful in detecting IgG antibodies in a wide range of animal species due to its non-species-specific binding. One study reported cross-reactivity, with Hammondia hammondi and Eimeria spp. This is the first systematic review to descriptively compare ELISAs for the detection of T. gondii antibodies across different animal species.

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.

Glycosylation of developing human glomeruli: lectin binding sites during cell induction and maturation.

1987 ◽  
Vol 35 (1) ◽  
pp. 33-37 ◽  
Author(s):  
H Holthöfer ◽  
I Virtanen
Keyword(s):  
Binding Sites ◽  
Mesangial Cells ◽  
Ricinus Communis ◽  
Lectin Binding ◽  
Helix Pomatia ◽  
Cell Types ◽  
Basement Membranes ◽  
Phenotypic Change ◽  
Neuraminidase Treatment ◽  
Nephron Development

Expression of cellular glycoconjugates during differentiation of human fetal kidney was studied using fluorochrome-labeled lectins. Each lectin revealed a characteristic binding pattern during the phenotypic change of the nephrogenic mesenchyme and during distinct stages of nephron development. The uninduced mesenchymal cells were positive for Pisum sativum (PSA), Concanavalin A (ConA), Wistaria floribunda (WGA), and Ricinus communis (RCA-I) lectins. However, these lectins failed to react with the uninduced cells of the S-shaped bodies, whereas Maclura pomifera (MPA), Triticum vulgaris (WGA) and, after neuraminidase treatment, Arachis hypogaea (PNA) agglutinins bound intensely to the presumptive podocytes. During later stages of nephrogenesis, MPA positively on the podocytes weakened and could not be observed in adult kidney glomeruli. Binding sites for Helix pomatia (HPA) agglutinin in glomeruli were also expressed only transiently during nephrogenesis. During further development PSA, ConA, WFA, and RCA-I reacted with mesangial cells in addition to the glomerular basement membranes. The segment-specific lectin binding patterns of the tubuli emerged in parallel with the appearance of brush border and Tamm-Horsfall antigens of the proximal and distal tubuli. The results show that nephron site-specific saccharides appear in a developmentally regulated manner and in parallel with morphologic maturation of the nephron. Lectins therefore appear to be useful tools for study of induction and maturation of various nephron cell types.

Specific binding of acrosome-reaction-inducing substance to the head of starfish spermatozoa

Zygote ◽  
1993 ◽  
Vol 1 (2) ◽  
pp. 121-127 ◽  
Author(s):  
Akira Ushiyama ◽  
Takeo Araki ◽  
Kazuyoshi Chiba ◽  
Motonori Hoshi
Keyword(s):  
Acrosome Reaction ◽  
Specific Binding ◽  
Molecular Size ◽  
Polystyrene Latex ◽  
Anterior Region ◽  
Head Region ◽  
Signal Molecule ◽  
Jelly Coat ◽  
Plot Analysis ◽  
Species Specific

In the starfish, spermatozoa undergo the acrosome reaction upon encountering the jelly coat of eggs. A highly sulphated glycoprotein in the jelly coat is called acrosome-reaction-inducing substance (ARIS) because it is the key signal molecule to trigger the acrosome reaction. The activity of ARIS is mainly attributed to its sulphate and saccharide residues. The extremely large molecular size and speciesspecific action of ARIS suggest the presence of a specific ARIS receptor on the sperm surface, but no experimental evidence for the receptor has been presented. We therefore measured specific binding of ARIS and its pronase digest (P-ARIS), which retains the full activity of ARIS, to homologous spermatozoa by using fluorescien-isothiocyanate-labelled ARIS and125 I-labelled P-ARIS, respectively. The spermatozoa had the ability to bind ARIS, as well as P-ARIS, specifically. The binding was species-specific, and mostly localised to the head region of spermatozoa. Scatchard plot analysis indicated the presence of one class of ARIS receptor on the surface of acrosome-intact speramatozoa. Furthermore, the specific binding of P-ARIS to the anterior region of sperm heads was microscopically confirmed by using P-ARIS conjugated to polystyrene latex beads with intense fluorescence. It is concluded that starfish spermatozoa have a specific receptor for ARIS on the surface of the anterior region of heads.

scholarly journals Characterization of glycoconjugates of human gastrointestinal mucosa by lectins. II. Lectin binding to the isolated glycoproteins of normal and malignant gastric mucosa.

1984 ◽  
Vol 32 (7) ◽  
pp. 690-696 ◽  
Author(s):  
J Fischer ◽  
G Uhlenbruck ◽  
P J Klein ◽  
M Vierbuchen ◽  
R Fischer
Keyword(s):  
Molecular Weight ◽  
Gastric Mucosa ◽  
High Molecular Weight ◽  
Lectin Binding ◽  
Gel Filtration ◽  
Molar Ratio ◽  
Gastric Cancer Cells ◽  
Tissue Sections ◽  
Gradient Gel Electrophoresis ◽  
Triton X

Using affinity chromatography on HPA-, PNA-, Con A, and WGA-agarose columns only a part (10-30%) of the high molecular weight mucous glycoproteins could be isolated from the Triton X-100 solubilized components of normal as well as carcinomatous gastric mucosa. The main part of the mucus was not bound by the lectins, which corresponds to our earlier lectin histochemical observations on paraffin-embedded tissue sections. The lectin-bound mucous glycoproteins had a relatively lower molecular weight, ranging from about 250-1,000 kilodaltons, as indicated by polyacrylamide gradient gel electrophoresis and by gel filtration on Biogel A 1.5 m column. In gas chromatographic analysis the molar ratio of aminohexoses to galactose was found to be much higher (3:1) in the lectin-bound mucous substances than in the whole high molecular weight mucus (1:1). This finding indicates that lectins have a higher affinity to the hexosamine rich components of mucus, which may be special forms of mucous glycoprotein molecules or the incompletely glycosylated core and backbone regions of the oligosaccharide chains of mucus. Extremely high hexosamine values (10:1) were found in the PNA isolated mucus of gastric adenocarcinoma. Since it is known that PNA binds to the terminal disaccharide, beta-galactose-(1-3)-N-acetylgalactosamine, which is localized at the reducing end of the oligosaccharide chains of mucus, it is highly probable that the elongation of the oligosaccharide side chains is disturbed in gastric cancer cells.

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