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PubMed1988

A survey of lectin binding in Paramecium.

To better understand the general distribution of glycoproteins and the distribution of specific glycoprotein-bound sugar residues in Paramecium, a survey of the binding pattern of selected lectins was carried out in P. tetraurelia, P. caudatum, and P. multimicronucleatum. Lectins studied were concanavalin A (Con A), Griffonia simplicifolia agglutinins I and II (GS I and GS II), wheat germ agglutinin (WGA), Ulex europaeus (UEA I), peanut agglutinin (PNA), Ricinis communis toxin (RCA60) and agglutinin (RCA120), soybean agglutinin (SBA), Bauhinia purpurea agglutinin (BPA), Dolichos biflorus agglutinin (DBA), and Maclura pomifera agglutinin (MPA). Those giving the most distinctive patterns were Con A, GS II, WGA, UEA I, and PNA. No significant differences were found between the three species. Concanavalin A, a mannose/glucose-binding lectin, diffusely labeled the cell surface and cytoplasm and, unexpectedly, the nuclear envelopes. Events of nuclear division, and nuclear size and number were thus revealed. Both WGA and GS II, which are N-acetylglucosamine-binding lectins, labeled trichocyst tips, the cell surface, and the oral region, revealing stages of stomatogenesis. The lectin WGA, in addition, labeled the compartments of the phagosome-lysosome system. The lectin PNA, an N-acetyl galactosamine/galactose-binding protein, was very specific for digestive vacuoles. Finally, UEA I, a fucose-binding lectin, brightly labeled trichocysts, both their tips and body outlines. We conclude that a judicious choice of lectins can be used to localize glycoproteins and specific sugar residues as well as to study certain events of nuclear division, cellular morphogenesis, trichocyst discharge, and events in the digestive cycle of Paramecium.

Animals↗
PubMed1986

Detection of mucus glycoconjugates in human conjunctiva by using the lectin colloidal gold technique in TEM. I. A quantitative study in normal subjects.

We applied a specific cytochemical reaction to characterize the glycoconjugates produced by goblet and non-goblet epithelial cells of normal human conjunctiva. For this purpose we utilized the lectins, proteins of vegetal origin, which are extremely sensitive in binding glycosidic residues. In particular, we used WGA, PNA, SBA and ConA conjugated with colloidal gold as ultrastructural marker for Transmission Electron Microscopy. This technique allowed us also to perform a quantitative analysis, by counting colloidal gold particles present on mucus granules. In this way we analyzed the content both of goblet and non-goblet epithelial cells. In the former, WGA, PNA, SBA and ConA receptors, here reported in decreasing density, were present. In the latter WGA was always positive, SBA and PNA sometimes were negative, ConA was always negative. We speculate the different contribution to mucus production by these two sources may be important in evaluating tear film stability alterations occurring in those diseases in which non-goblet epithelial cell vesicles increase.

Carbohydrate Metabolism↗
PubMed1986

Detection of mucus glycoconjugates in human conjunctiva by using the lectin-colloidal gold technique in TEM. II. A quantitative study in dry-eye patients.

The mucus glycoconjugates produced by conjunctival goblet cells in dry-eye patients were studied by a specific cytochemical reaction in Transmission Electron Microscopy (TEM). Four lectins, proteins of vegetal origin which specifically bind glycosidic residues, (WGA, PNA, SBA and ConA) were used conjugated with colloidal gold as ultrastructural marker. We performed a quantitative analysis by counting the colloidal gold particles present on mucus granules. The results were compared with normal conditions. We found a decrease in sialic acid, N-acetyl-glucosamine, N-acetyl-galactosamine and galactose-N-acetyl-galactosamine and an increase in mannose. The different content of glycoconjugates in goblet cells may reflect in the change of physical and functional properties of mucus. We think these data may be useful in the search for a therapeutic mucomimetic drug.

Carbohydrate Metabolism↗
PubMed1998

Lectin binding in the human endometrium in early luteal phase following controlled ovarian hyperstimulation.

A lectin histochemical study was performed to investigate the glycoconjugate saccharidic moieties on the endometrial epithelium and stroma in 12 women undergoing controlled ovarian hyperstimulation (COH) for in-vitro fertilisation for embryo transfer (IVF-ET) in early luteal phase. 7 control subjects were also evaluated. For this purpose a battery of seven horseradish peroxidase-conjugated lectins (PNA, SBA, DBA, WGA, ConA, LTA and UEA I) was used. Cytochemical controls were performed for specificity of lectin-sugar reaction. As far as the endometrial glands and stroma are concerned, the obtained data showed no differences in the endometrial lectin binding between the subjects of the control group and the ones undergoing COH, with the exception of PNA reactivity at the level of the apical portion of the glandular cells, which was detected only in COH women. It is noteworthy that, although the endometrial dating using the Noyes's criteria showed marked dissynchronies between the stroma and the glands in COH subjects, a uniformity of lectin binding, revealing the same type and localization of terminal oligosaccharides, was observed in all the examined subjects. The uniformity in distribution of the sugar residues detected in the endometrial specimens following COH might be due to the massive FSH and/or hCG treatment which probably determines an endometrial environment almost equal in all the examined subjects. In all the treated subjects reactivity with sialidase-WGA and ConA, revealing the presence of N-acetyl-D-glucosamine and D-mannose respectively, was detected at the level of the lining epithelium.

Adult↗
PubMed1984

Lectin-binding patterns of breast carcinoma: significance on structural atypism.

We have investigated lectin-binding profiles of the human breast epithelia and the structural atypism in intraductal carcinoma. The lectino-histochemical probes using biotin-labeled peanut agglutinin (PNA), soybean agglutinin (SBA) and wheat germ agglutinin (WGA) with avidin-biotin peroxidase complex were performed on formalin-fixed and paraffin-embedded specimens from 24 patients. While normal and benign hyperplastic epithelia were stained almost in luminal borders and apical cytoplasmic surfaces, intraductal carcinoma additionally showed conspicuous staining of intracytoplasmic lumina and supranuclear cytoplasmic margins. The lectin-binding pattern found in papillary hyperplasia was completely different from that in intraductal carcinoma; the former was an irregular network structure along luminal borders, whereas the latter was not only a cribriform but also a rosette structure along intracytoplasmic lumina and supranuclear cytoplasms. Such lectin-binding patterns seemed to reflect the change of cell polarity in malignant transformation. The significance of these observations in elucidation of structural atypism was discussed in relation to 3-D structure of intraductal carcinoma.

Biotin↗
PubMed2002

Histochemistry of six lectins in the tissues of the flat fish Paralichthys olivaceus.

Lectins are glycoproteins that specifically bind carbohydrate structures and may participate in the biodefense mechanisms of fish. In this study, the binding of three lectins, Dolichos biflorus agglutinin (DBA), soybean agglutinin (SBA), Bandeiraea simplicifolia BS-1 (isolectin B4), Triticum vulgaris (WGA), Arachis hypogaea (PNA) and Ulex europaeus (UEA-I) were studied in the gill, liver, intestine, kidney, heart, and spleen of the flat fish Paralichthys olivaceus. DBA was detected in intestinal mucous cells, as well as in gill epithelial and mucous cells. It was weakly detected in renal tubule epithelial cells and in bile duct epithelial cells. The strong SBA staining was seen in the intestinal club cells, in bile duct epithelial cells and renal tubule epithelial cells. There were intense positive reactions for isolectin B4 in gill epithelial and mucous cells, and the strong isolectin B4 staining was seen in epithelial cells of the bile duct and intestine. The strong WGA staining was seen in the gill mucosal cells, sinusoid, renal tubule epithelial cells and mucosal cells of the intestine. UEA-I was detected in the gill epithelial and mucosal cells, bile duct epithelial cells and renal tubular epithelial cells. These results suggest that the six lectins examined were localized in the covering epithelia of the various organs of the flat fish and they may participate in the biodefense mechanism of the intra body surface in which is exposed to various antigens.

Animals↗
PubMed1991

Lectin binding of endometrium in women with unexplained infertility.

OBJECTIVE: To investigate whether peri-implantation phase endometrium in women with unexplained infertility differs from the endometrium of normal fertile women. DESIGN: Assessment of the function of the endometrium by using endometrial biopsy specimens and lectin histochemistry. SETTING: Infertility Clinic, Jessop Hospital for Women, Sheffield, United Kingdom. PATIENTS: Eighteen normal fertile women (group I) and 18 women with unexplained infertility (group II). INTERVENTIONS: Endometrial biopsies were obtained from both groups at 5, 7, and 9 days after the luteinizing hormone (LH) surge. MAIN OUTCOME MEASURES: Five biotinylated lectins, concanavalin A (ConA), wheat germ agglutinin (WGA), soybean agglutinin, Peanut, and Ulex europaeus I were used as analytical probes to study endometrial glycoconjugates. Histochemical staining was performed using the avidin-biotin peroxidase method. The lectin binding by endometrial glands, surface epithelium, stromal cells, and vessels was assessed. RESULTS: In group I, ConA stained the subnuclear glandular cytoplasm, glandular lumen, stroma cells, and surface epithelium. In group II, ConA binding to glandular or surface epithelium was none or equivocal. In group I, WGA bound to glandular cytoplasm and stroma cells on days LH + 5 and LH + 7. In group II, WGA binding was absent in glands but present in stroma. CONCLUSIONS: Reproductive failure of women with unexplained infertility may be associated with defective biosynthesis and distribution of glycoconjugates that subsequently results in an unfavorable endometrial environment during the peri-implantation phase.

Adult↗
PubMed1986

Detection of the urinary 'PUM' polymorphism by the tumour-binding monoclonal antibodies Ca1, Ca2, Ca3, HMFG1, and HMFG2.

A series of human urinary mucin-like glycoproteins, previously detected using lectins to stain gels after electrophoresis, and showing genetic polymorphism (Karlsson et al., 1983) can also be detected using the tumour-binding monoclonal antibodies, Ca1, Ca2, Ca3, HMFG1, and HMFG2. The evidence from immunoprecipitation and immunoadsorbant chromatography experiments is that the epitopes recognized by these antibodies are carried on the same molecules as the lectin-binding determinants. The discovery that the antibodies bind specifically to a family of molecules which show genetic polymorphism provides a powerful new tool for the analysis of the material expressed aberrantly in cancer.

Antibodies, Monoclonal↗
PubMed1983

Cell surface glycoproteins of 13762NF mammary adenocarcinoma clones of differing metastatic potentials.

Rat 13762NF mammary adenocarcinoma cell surface glycoproteins from s.c. tumor- or lung metastases-derived cell clones of differing spontaneous metastatic potentials were examined for their relationship to metastasis. After treatment with neuraminidase, lectin-binding assays showed that highly metastatic clone MTLn3 cells express approximately twice the quantity of peanut agglutinin (PNA) binding sites (approximately 2.3 X 10(8) sites/cell) than clones of lower metastatic potential. However, the number of wheat germ agglutinin (WGA)-binding sites on the various cell clones decreased slightly as the metastatic potential of the clones increased. The quantities of concanavalin A (conA)-binding sites were similar (approximately 1.7 X 10(8) sites/cell) in all cell clones and growth conditions. Glycoprotein analysis was performed by electrophoresis on polyacrylamide gels in the presence of sodium dodecyl sulfate (SDS-PAGE) and subsequent staining with 125I-labeled lectins. SDS-PAGE gels stained with 125I-labeled conA revealed mainly one glycoprotein (Mr approximately 150 kD), and the amounts of this glycoprotein did not correlate with metastasis. Differences in WGA-binding glycoproteins were detected between s.c. tumor- and lung metastases-derived cell clones. Several desialylated glycoproteins were detected with 125I-labeled PNA after SDS-PAGE, and the labeling intensity of one (Mr approximately 580 kD) correlated with the metastatic potentials of the various cell clones. This high Mr galactoprotein was further analyzed by [3H]glucosamine metabolic labeling, solubilization, sequential gel filtration, and chondroitinase ABC treatment prior to SDS-PAGE. The 580 kD galactoprotein was expressed in increased amounts on the more highly metastatic clones. Chemical labeling of cell surface sialic acid residues using periodate treatment followed by [3H]borohydride reduction showed an additional change in a major sialoglycoprotein (Mr approximately 80 kD), which decreased in labeling intensity on clones of increasing metastatic potential. The results suggest quantitative changes in cell surface glycoproteins rather than major qualitative alterations are associated with differences in the metastatic behavior of 13762NF tumor cell clones.

Adenocarcinoma↗
PubMed2002

Quantitative determination of dietary lectin activities by enzyme-linked immunosorbent assay using specific glycoproteins immobilized on microtiter plates.

An immunoenzymatic method for the quantitative determination of dietary lectin activities employing immobilized glycoproteins was studied. Lectins from wheat germ (WGA), peanut (PNA), and jack bean (ConA) were added to microtiter plates coated with ovalbumin or asialofetuin and quantified by enzyme-linked immunosorbent assay (ELISA) with lectin-specific antibodies. ELISA responses for lectin activity were dose-dependent in the concentration range 30-1000 ng/mL for WGA and 80-1000 ng/mL for both PNA and ConA. Inhibition assays carried out with different saccharides confirmed that the binding of lectins to immobilized glycoproteins was specific. The proposed method is specific and sensitive, allowing the quantitative determination of lectin activities on raw samples by simple dilution of the extracts. Examples of application to wheat germ and roasted peanut extracts are reported.

Antibodies↗
PubMedDate not supplied

Capacitated and acrosome reacted spermatozoa of goat (Capra indicus): a fluorescence and electron microscopic study.

Plasma membrane alterations accompanying in vitro capacitation and acrosome reaction of goat spermatozoa were studied using lectin labelling, scanning electron microscopy, and freeze-fracture methods. Fluorescein isothiocyanate linked lectins namely; Canavalia ensiformis (ConA), Maclura pomifera (MPA), Arachis hypogaea (PNA), Glycine max (SBA) and Triticum vulgaris (WGA) agglutinin were used to examine the distribution of surface carbohydrates during these two events. The head and the sperm tail reveal altered lectin labelling features after capacitation and acrosome reaction. After capacitation the surface coat components for MPA, SBA, and WGA are shed from the spermatozoon head. ConA receptors on the head are retained after capacitation but are partially shed in the acrosome reacted spermatozoa. SBA receptor sites appear on the sperm tail of the capacitated spermatozoa. Unusual morphological changes attending capacitation involve the sperm tail-end which develops a novel entity, which we have termed 'spatula'. The 'spatula' shows strong binding with ConA and WGA only. In the acrosome reacted spermatozoa the spatulated tail-end unwinds with a concomitant loss of lectin labelling. Highly ordered membrane particles, 'ladders' of the middle piece of the epididymal sperm tail, disappear and IMP clearings appear on the middle piece and in the spatulated ends of the capacitated spermatozoa. But in the acrosome reacted sperm IMPs reappear and are randomly disposed on the middle-piece and are clustered in small patches on the principal-piece. IMP free areas appear on the plasma membrane covering the acrosome and the outer acrosomal membrane (OAM) of the capacitated spermatozoa. The plasma membrane and OAM fuse at multiple foci and appear as acrosomal 'ghosts' which remain associated with the sperm head even after acrosome reaction.

Acrosome↗
PubMed1986

Lectin binding to normal human endometrium.

Avidin-biotin-peroxidase labelling technique was used to localize the binding sites of peanut agglutinin (PNA), Ulex europaeus (UEA-I), wheat germ agglutinin (WGA), concanavalin A (Con A), and Ricinus communis (RCA-I) in 30 samples of endometrium at different stages of the menstrual cycle and in early pregnancy. PNA and UEA-I exhibit weak binding to the apical portions of epithelial cells in proliferative and secretory phases, but become strongly positive in pregnancy. WGA and RCA-I show weak binding to glandular epithelium in the proliferative phase, but increase their affinity in the secretory phase. Con A demonstrates strong affinity to decidual cells.

Concanavalin A↗
PubMed1999

Human ocular drusen possess novel core domains with a distinct carbohydrate composition.

Ocular drusen are extracellular deposits that form between the retinal pigmented epithelium (RPE) and Bruch's membrane. Although the presence of large and/or numerous drusen in the macula is a significant risk factor for development of age-related macular degeneration (AMD), a major cause of irreversible blindness, little is known about their origin or composition. We have expanded on our previous investigations related to drusen-associated glycoconjugates by examining lectin binding patterns after removal of terminal sialic acid residues. Strikingly, intense and distinct labeling of drusen subdomains is revealed by Arachea hypogea agglutinin (PNA) after neuraminidase treatment. PNA binding is confined to discrete domains within both hard and soft drusen. These "cores" are positioned centrally within drusen and are typically juxtaposed to Bruch's membrane. Only one core per druse is observed. PNA labeling of drusen cores does not co-localize with associated lipids and is abrogated by digestion with O-glycosidase but not N-glycosidase. The association of cores with small drusen suggests that they may participate in drusen biogenesis. (J Histochem Cytochem 47:1533-1539, 1999)

Adult↗
PubMed1988

Quantitation of lectin binding sites in human colon mucins by use of peanut and wheat germ agglutinins.

We have developed a novel method for quantitation of lectin binding sites in mucins derived from colon tissues. Binding of peanut agglutinin and wheat germ agglutinin was measured in extracts from normal and malignant human colon epithelium. Binding of wheat germ agglutinin was used as an estimate of the total mucin present in the tissue extract. Peanut agglutinin was found to bind to mucin from normal colon, but at levels that may be difficult to appreciate by fluorescence microscopy. The yield of mucin extracted from colon cancer was more variable than that from normal colon, and the binding ratio of peanut agglutinin to wheat germ agglutinin was greater in extracts from tumors than in normal tissues. Our findings confirm the histological observation that peanut agglutinin binds more avidly to mucins from colon cancer than to those from normal colon. The finding of peanut agglutinin binding sites in mucins front normal colon was not expected. The quantitative technique may have detected small numbers of binding sites not readily appreciable by fluorescence microscopy. Alternatively, the chromatographic method for measuring lectin binding may be sufficiently sensitive to detect nonspecific binding of the lectin to terminal galactose residues other than the Thomsen-Friedenreich antigen.

Arachis↗
PubMed1997

Binding of lectins to novel migration promoters on cardiac mesenchymal cells in the chick.

Chicken serum promotes migration of cardiac mesenchymal cells of chick embryos in vitro. In the present study, migration promotion of unknown migration promoters in chicken serum was examined by using lectins. Cardiac mesenchymal cells of the conotruncal and atrioventricular cushions were cultured on collagen type-I gel with medium including chicken serum. A concentration (100 micrograms/ml) of Concanavalin A (Con A), peanut agglutinin (PNA), pisum sativum agglutinin (PSA), soybean agglutinin (SBA) or wheat germ agglutinin (WGA) was added to the medium. Con A, PSA, and WGA inhibited migration, while PNA and SBA did not affect migration of cardiac mesenchymal cells. WGA inhibited migration in a concentration dependent manner. Preincubation of WGA with specific binding monosaccharides (alpha-D-N-acetylglucosamine and alpha-D-N-acetylneuraminic acid) clearly reduced the inhibition ability of WGA, while preincubation of Con A and PSA with alpha-D-mannose and alpha-D-glucose did not. On the other hand, Con A-binding proteins, eluted from a Con A affinity column with the buffer including alpha-D-mannose and alpha-D-glucose, promoted migration of cardiac mesenchymal cells, as did WGA-binding proteins. These proteins promoted migration in a concentration dependent manner. Western blotting showed that PSA bound the subunits of collagen type-I, but ConA and WGA did not. In migration inhibition assays by monosaccharides, only N-acetylneuraminic acid inhibited migration of cardiac mesenchymal cells. These results suggested that chicken serum contains novel migration promoters for chick cardiac mesenchymal cells. The promoters are proposed to have the terminal N-acetylglucosamine, N-acetylneuraminic acid, and glucose and/or mannose residues.

Animals↗
PubMed1987

Lectin reactivity in human large bowel.

The affinity of six lectins (Arachis hypogaea, Concanavalin A, Bandeiraea simplicifolia I. Dolichus biflorus, Triticum vulgaris and Lotus tetragonolobus) was studied in 10 normal human large intestines. The results showed that each lectin had its own characteristic staining pattern. They differed in their affinity for different cellular components, local distribution within crypts and regional distribution between right (ascending colon) and left (rectum) segments of the large bowel. Arachis hypogaea stained predominantly the supranuclear golgi cisternae and Concanavalin A the cytoplasm. Triticum vulgaris stained preferentially the mucin of the well differentiated cells of the upper crypt while Lotus tetragonolobus characteristically stained the glycocalyx and apical portion of the less differentiated basal cells of the lower crypt. Goblet-cell mucin of the ascending colon had greater affinity for Bandeiraea simplicifolia I and that of the rectum for Triticum vulgaris. Lotus tetragonolobus stained more frequently and extensively the goblet-cell mucin of the upper crypts of the ascending colon than that of the rectum. The goblet cell mucins of the upper crypts were consistently stained in both the right and left segments of the large bowel by Dolichus biflorus while the mucins of the less differentiated cells of the lower crypts were less consistently stained in the ascending colon.

Autopsy↗
PubMedDate not supplied

Lectin-binding sites on human sperm during acrosome reaction: modifications judged by electron microscopy/flow cytometry.

Biochemical surface modifications occur during the capacitation and acrosome reaction of human sperm and among those, variations in the expression of carbohydrates moieties. A sequential study was performed with electronic microscopy and flow cytometry techniques, where the binding of 4 lectins was assessed on normal human sperm samples during in vitro induction of the acrosome reaction with calcium ionophore A-23187. Triticum vulgaris agglutinin (WGA) was shown to bind strongly the whole surface of sperm before induction of the acrosome reaction, and in lesser amounts after incubation with calcium ionophore. Arachis hypogea agglutinin (PNA) and mostly Concanavalia ensiformis agglutinin (Con-A) and Ulex europaeus agglutinin (UEA-1) binding evolved in an opposite pattern with an increase of the labeling parallel to that of GB24 antibody binding. Electron microscopy showed that the fluorescence patterns observed correlated with increased access to the inner membrane of the acrosome. This was significant 60 min after the induction of acrosome reaction. Lectin binding could be a useful tool to examine the ability of sperm samples to undergo the acrosome reaction.

Acrosome↗
PubMed1991

Lectin histochemistry of ovarian mucinous cystadenomas.

The lectin histochemistry of ovarian mucinous cystadenoma was studied using a panel of lectins comprising Triticum vulgaris, Lotus tetragonolobus, Arachis hypogaea, Griffonia simplicifolia I, concanavalin A, and Dolichus biflorus. All 23 cases examined in this study stained extensively with T. vulgaris. Of all the lectins, D. biflorus was the least reactive. Concanavalin A stained mainly the perinuclear zone, whereas the other lectins frequently stained the cytoplasm, glycocalyx, and extracellular luminal mucin. This pattern of lectin reactivity resembles endocervical more than intestinal epithelium and suggests that ovarian mucinous cystadenomas are of müllerian nature. The lack of difference in lectin reactivity between cystadenomas with and without goblet/Paneth cells supports a common histogenetic origin of both groups.

Concanavalin A↗