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At least 163 records · Page 9Linked to original sources
PubMed1988

[Lectin-binding sugar chain in bladder tumors].

We studied the lectin binding patterns of 40 initial superficial and 10 subsequent invasive bladder tumors by the avidin-biotin-peroxidase complex (ABC) method using the following biotin-labeled lectins: PNA, DBA, UEA-I, BS-I, ConA and WGA. We observed the relationship between lectin binding and subsequent course of initial superficial tumors, grade and stage (T). DBA or WGA staining tumors and Con A negative tumors revealed no recurrence or superficial recurrence. Low grade tumors were DBA or BS-I positive and high grade tumors were ConA positive. Low staging tumors possessed DBA or WGA positiveness and high staging tumors had ConA positiveness. From these results we considered that negative staining of WGA or DBA, or positive staining of ConA was a change accompanying the malignant potentiality.

Adult↗
PubMed1996

A histochemical study of the distribution of lectin binding sites in the developing branchial area of the trout Salmo trutta.

A histochemical study of the branchial area of brown trout embryos from 35 to 71 d of incubation is reported. A battery of 6 different horseradish peroxidase-labelled lectins, the PAS reaction and Alcian blue staining were used to study the distribution of carbohydrate residues in glycoconjugates along the pharyngeal and branchial epithelia. Con A and WGA reacted at every site of the branchial region thus showing the ubiquitous presence of alpha-D-mannose and N-acetyl-D-glucosamine. WGA, DBA and SBA were good markers for the hatching gland cells (HGCs) and mucous cells. Other lectins, such as PNA and UEA I, reacted only for a short time at some sites during the considered period of incubation. From 35 d until posthatching stages, a manifest strong reaction was noted both in the dorsal epithelium of branchial arches and the HGCs as shown by SBA reactivity. This may be significant with regard to the controversial origin of HGCs, which is thought to be endodermal.

Acetylglucosamine↗
PubMed1990

Ultrastructural localization of lectin binding sites in human melanocytes.

The ultrastructural localization of carbohydrate residues in human melanocytes of normal epidermis and of one compound naevus was studied. The following lectins were used in a post-embedding technique: 1. peanut agglutinin (PNA), which reacts specifically with N-acetylgalactosamine; 2. Concanavalia ensiformis (Con A) indicating alpha-D-glucose and alpha-D-mannose binding sites; 3. Ulex europaeus agglutinin (UEA I) specific for alpha-L-fucose; 4. Wheat germ agglutinin (WGA), reacting specifically with N-acetyl-glucosamine and neuraminic acid (sialic acid); and 5. Limax flavus agglutinin (LFA), also specific for sialic acid (Neu5Ac-alpha-2,3-Gal and Neu5Ac-alpha-2,6-Gal). When incubated with WGA, Con A and LFA strong labelling was seen within the cytoplasm and in the plasma membrane of melanocytes, whereas incubations with PNA and UEA I revealed an occasional gold particle only. The determination of the distribution of carbohydrate residues in normal melanocytes is a prerequisite for future studies of abnormal melanocytes.

Arachis↗
PubMed1986

Binding specificities of the lectins PNA, WGA and UEA I to polyvinylchloride-adsorbed glycosphingolipids.

The binding specificities of the lectins PNA (peanut agglutinin), WGA (wheat germ agglutinin), and UEA I (Ulex europeus agglutinin I) against glycosphingolipids were investigated using an enzyme-linked immunosorbent assay (ELISA), utilizing the biotin-avidin system for detection of bound lectin. PNA showed the highest affinity to GA1, but also bound, though less strongly, to GM1 and GD1b. WGA bound to 3'-nLM1 and 6'-nLM1, the former twice as strongly as the latter, but not to any sialic acid containing glycolipid of the gangliotetraose series. UEA I showed a high affinity for the Lea glycolipid which has an alpha 1-4 linked fucose but not for the glycolipids with alpha 1-3 or alpha 1-2 linked fucose. Interestingly, 3'-nLM1 and nLA1, glycolipids lacking fucose, also bound UEA I. The results show that lectins should be used with caution for establishing terminal sugar sequences in glycosphingolipids.

Enzyme-Linked Immunosorbent Assay↗
PubMed1984

Selective staining of human platelet glycoproteins using nitrocellulose transfer of electrophoresed proteins and peroxidase-conjugated lectins.

Platelet proteins (0.5-5 micrograms) were electrophoresed in a one-dimensional or an unreduced-reduced, two-dimensional sodium dodecyl sulfate gel system. The separated proteins were then transferred electrophoretically to nitrocellulose and reacted with peroxidase-conjugated lectins. Visualization of specific glycoproteins which bound the lectins was made by the chromogenic reaction catalyzed by peroxidase utilizing 3,3'-diaminobenzidine as the substrate. Wheat germ agglutinin specifically reacted with and allowed the visualization of glycoprotein Ib. Peanut agglutinin also specifically stained glycoprotein Ib after treatment of the nitrocellulose transferred proteins with neuraminidase. Ricinus communis agglutinin I stained thrombospondin, a 260 kDa protein, and factor VIII. Concanavalin A stained mainly glycoproteins IIb, III, IV, and V. Glycoproteins Ia, Ic, IIa, and other minor glycoproteins could be separated by unreduced-reduced, two-dimensional gel electrophoresis and were stained weakly with wheat germ agglutinin conjugates. These techniques were found to be reproducible as well as easily applied to the analysis and identification of platelet glycoproteins, particularly when dealing with a limited amount of platelets.

Animals↗
PubMed2005

Lectin reactivity of expanded mouse blastocysts after exposure to sera from women with unexplained recurrent spontaneous abortion.

Embryotoxic factors existing in maternal sera may influence their effects via specific binding to, or alteration of cell surface molecules in the conceptus. This study was undertaken to determine the effects of sera from women with unexplained recurrent spontaneous abortion (URSA) on cell surface glycoconjugates of the early conceptus. Four cell stage embryos were cultured in medium supplemented with sera from women with URSA, from normal women, or in medium without serum. Developmental competence was assessed as the stage distribution of embryos advancing to during 96h in culture. Hatched (expanded) blastocysts were stained with wheat germ agglutinin (WGA), peanut agglutinin (PNA) and dolichos biflorus agglutinin (DBA) to detect surface glucoconjugates. We observed that patient sera could be divided into high- and low-risk groups on the basis of the ability to decrease the number of four-cell embryos reaching the expanded blastocyst stage. Furthermore, the intensity of reactivity to PNA changed after exposure to high-risk sera. Morula formation was reduced and blastocyst formation was delayed. Although the sera from women with URSA had embryotoxic effects, no influence on the glycoconjugate patterns were evident in hatched blastocysts, aside from PNA reactivivity. We suggest altered developmental display of PNA-reactive proteins was a biomarker for poor developmental quality due to emrbyotoxic factors in serum from URSA patients.

Abortion, Habitual↗
PubMed1982

Distribution of exposed and hidden carbohydrates of Schistosoma mansoni adult worms demonstrated by selective binding of fluorochrome-conjugated lectins.

The distribution of exposed and hidden lectin-binding glycoconjugates in adult Schistosoma mansoni worms was studied. Fluorochrome-conjugated lectins were allowed to react both with intact worms and with frozen sections of worms. The results show a selective reactivity of lectins with tegumental surface structures, the intestine, eggs and basement membranes. Strong binding of wheat germ agglutinin (WGA) was seen to the exposed surface of intact worms. Peanut agglutinin (PNA), Ricinus communis agglutinin (RCA) and concanavalin A (Con A) gave a weaker reaction. There was a preferential affinity of PNA and RCA to the spikes covering the tubercles of male worms whereas Con A gave a more uniform staining pattern. Internal structures exposed in frozen sections of worms gave distinct staining reactions. Binding sites for Con A were widely distributed throughout the worm. PNA produced a more selective binding and was the only lectin staining basement membranes as distinct structures. There was a strong selective staining of the gut with soybean agglutinin (SBA) and RCA. Eggs seen in large quantitites inside female parasites reacted strongly with SBA and PNA and less intensely with RCA and WGA. The observed selectivity of lectin binding may reflect physiological function. The results may be important as a basis for using lectin affinity-chromatography for purification and characterization of worm constituents.

Animals↗
PubMed1997

A two-site lectinoenzymatic assay for determination of tumour marker glycoproteins in rectal secretions.

A method is described for a titre-tray based two-site lectinoenzymatic assay of glycoproteins. WGA lectin, reacting with the core-part of glycans, was combined with lectins PNA and DBA, the latter two reacting with terminal parts of glycans. A standard curve was obtained with bovine submaxillary gland asialomucin, and measurements of human rectal secretion were calibrated against this curve. The assay showed an intra-assay reproducibility of 2.4-7.5%, and inter-assay reproducibility of 3.9-20.8%. Recovery tests showed a linearity close to predicted values. The selected standard was ideal as inhibition of lectin binding by monosaccharides showed similar inhibition profiles for human rectal secretion and for asialomucin standard. Neuraminidase treatment dramatically increased the PNA binding to human rectal secretion immobilized on WGA. Western blotting of human rectal secretion demonstrated a large range of lectin-reactive glycoproteins, the main fraction reacting with all lectins being approximately 250 kDa. The assay described is well suited for studies of the glycan part of tumour marker glycoproteins, and changes occurring in these. It has a high sensitivity by ignoring that the glycans may be present on different molecules. Examination of rectal secretions from various cancer patients showed significantly increased PNA binding, as well as an increased PNA/DBA binding ratio, in patients with colorectal cancer (p<3x10(-3)) and, unexpectedly, in patients with other cancers (p<5x10(-3)).

Animals↗
PubMed2001

Mucin histochemistry of the digestive tract of the red-legged frog Rana aurora aurora.

Mucous cells from the digestive tract of the red-legged frog, Rana aurora aurora, were examined by standard histochemical methods and by lectin histochemistry. Two different goblet cell types were found in the oesophageal epithelium. Type I cells produced acidic glycoproteins with beta1,4GlcNAc oligomers, Gal beta1,3GalNAc sequences, sulphated esters on internal residues and abundant non-O-acylated terminal sialic acid bound to penultimate GalNAc. These cells also reacted with Con-A after periodate oxidation-borohydride reduction (PCS). Type II goblet cells mainly differed from type I cells in their negative reaction with PCS. Oesophageal glands consisted of mucous and serous cells. Mucous cells produced neutral stable class III mucosubstances with GalNAc, beta1,4GlcNAc and Gal beta1,3GalNAc residues. Gastric surface cells produced sulpho-sialoglycoproteins with Gal beta1,3GalNAc residues and Gal beta1,3GalNAc-sialic acid as terminal sequences. These cells did not contain stable class III mucosubstances. The mucus produced by foveolar cells was similar in composition but did not contain sulphated groups and was rich in GalNAc residues. The fundic glands consisted of mucous neck cells, endocrine cells and oxyntic cells. The neck cells produced neutral mucins containing D-mannose and/or D-glucose, beta1,4GlcNAc oligomers and Gal beta1,3GalNAc terminal dimers and were PCS-positive. Pyloric glands were of the mucus-secreting type, which produced glycoproteins with the same basic features as those produced in fundic neck cells. A single type of intestinal goblet cells produced acidic glycoproteins rich in beta1,4GlcNAc oligomers, sulphated esters on oligosaccharide chains and terminal O-acylated sialic acid bound to penultimate Gal beta1,3GalNAc. The different carbohydrate structures observed along the digestive tract of the frog may reflect specific functions of the mucus.

Animals↗
PubMed1998

Changes in glycoconjugate expression of the sinus mucosa during experimental sinusitis: a lectin histochemical study of the epithelium and goblet cell development.

Lectin expression in both normal and inflamed sinus mucosa in rabbit was investigated histochemically. A different staining pattern was observed in the inflamed mucosa, i.e. the degree of staining reactivity with Canavalia ensiformis (ConA) decreased, whereas staining with Ulex europaeus agglutinin-I (UEA-I), Arachis hypoga (PNA) with neuraminidase pretreatment and Triticum vulgaris (WGA) intensified, indicating an enhanced fucosylation as well as sialylation. Goblet cells were stained with UEA-I, WGA, PNA and PNA with neuraminidase pretreatment, but scarcely with ConA. Positive PNA staining of basal cells and epithelial secretory granules was observed in the inflamed mucosa, especially close to areas where goblet cell development was prolific. It was therefore assumed that basal cells can differentiate into goblet cells-through epithelial secretory cells accompanied by sialylation and/or sulphonation of their mucins. It is concluded that the changes in glycoconjugate expression as well as goblet cell development in the inflamed mucosa are of importance for both local host resistance and defence mechanisms against microorganisms during the early stages of the inflammatory process.

Animals↗
PubMed1986

Cell surface carbohydrates in proliferative epidermal lesions. II. Masking of peanut agglutinin (PNA) binding sites in solar keratoses, Bowen's disease, and squamous cell carcinoma by neuraminic acid.

Seventy-six skin biopsies of proliferative lesions were studied by using 4 different lectins and an avidin-biotin-peroxidase complex. In solar keratosis, Bowen's disease and squamous cell carcinoma, malignant-appearing keratinocytes exhibited loss of membrane staining with Concanavalia ensiformis agglutinin (Con A), but revealed cytoplasmic staining. When incubated with peanut agglutinin (PNA), the malignant keratinocytes did not stain. However, the PNA binding sites were not absent, but masked by sialic acid. Following cleavage of the sialic acid with neuraminidase, free PNA binding sites could be demonstrated in the plasma membranes. In contrast, the keratinocytes in keratoacanthomas showed membrane staining with Con A and also contained free PNA binding sites. These histochemical findings confirm and extend our earlier observations regarding cell surface carbohydrates in premalignant and malignant epidermal lesions.

ABO Blood-Group System↗
PubMed1986

Strain characterization and grouping of Campylobacter jejuni and Campylobacter coli by interaction with lectins.

Strains of Campylobacter jejuni and Campylobacter coli were characterized and grouped by their distinct reaction patterns with lectins. Heating of the Campylobacter cultures to 100 degrees C and holding for 30 to 60 min greatly enhanced their reactivity with lectins and permitted the grouping of all but 3 of 155 cultures tested in this study without interference of autoagglutination and other nonspecific activities. The lectin reaction patterns of the heated cultures were stable and reproducible. They were strain specific and independent of the heat-stable antigenic types. The lectin-reactive sites of C. jejuni and C. coli may be useful as additional markers for strain characterization. Based on these observations, a simple slide agglutination procedure is described for differentiating strains of C. jejuni and C. coli by their interaction with a selected group of commercially available lectins.

Agglutination↗
PubMed1983

Lectin histochemistry of 1,2-dimethylhydrazine-induced rat colon neoplasia.

Lectins linked to fluorescein were used as carbohydrate probes to examine the goblet cell mucin and epithelial cell surface glycoconjugate alterations in an experimental rodent model of colonic neoplasia induced with parenteral 1,2-dimethylhydrazine dihydrochloride. Lectins derived from Triticum vulgare (WGA), Ricinus communis (RCA1), and Limulus polyphemus (LPA) showed reduced labeling of goblet cell mucin in these tumors, while binding with peanut lectin from Arachis hypogaea (PNA), a lectin ordinarily failing to bind to mucin in normal colon, was positive. In addition, RCA1 and LPA showed increased cell surface labeling of neoplastic epithelial cells. Finally, alterations were observed in lectin binding to "transitional" colonic mucosa adjacent to colonic tumors from carcinogen-treated rats. These findings indicate that significant alterations in both membrane and mucin glycoconjugates occur in colonic tumors and mucosa adjacent to tumors in a chemically induced experimental animal model of human colon cancer.

1,2-Dimethylhydrazine↗
PubMed1992

Lectin binding sites as markers of neonatal porcine uterine development.

To identify lectin binding sites and to determine if lectin binding patterns change with age in developing neonatal porcine uterine tissues, gilts (n = 3/day) were hysterectomized on Day 0 (birth), 7, 14, 28, 42, or 56. Lectin binding was visualized in Bouin's-fixed uterine tissues with seven biotinylated lectins (ConA, DBA, PNA, RCA-I, SBA, UEA-I, and WGA) and avidin-peroxidase staining procedures. Lectin specificities were demonstrated by pre-incubating lectins with appropriate inhibitory sugars (0.2 M). Staining intensity was evaluated visually (absent, weak, moderate, or strong) for three endometrial tissues; luminal epithelium, glandular epithelium, and stroma. Staining intensities for DBA, PNA, SBA, and WGA were not affected by neonatal age. Staining with these lectins was greater in uterine epithelium (moderate or strong) than in stroma (weak). In contrast, binding patterns for ConA, UEA-I, and RCA-I were affected by neonatal age. Strong epithelial staining associated with ConA binding was observed on all days, whereas stromal ConA staining decreased in intensity from moderate to weak after Day 14. Epithelial staining with UEA-I increased from moderate to strong after Day 28, whereas stromal UEA-I staining decreased from moderate to weak after day 28. Staining with RCA-I was homogeneous for luminal epithelium and stroma but variegated for glandular epithelium on and after Day 7. These observations indicate that a variety of lectin binding sites are present in developing neonatal porcine endometrial tissues and that developmentally related alterations in the distribution and/or orientation of glycoconjugates containing alpha-D-mannose, beta-D-galactose, beta-D-acetyl-N-galactosamine, and alpha-L-fucose residues occur between birth and Day 56 as these tissues mature.

Aging↗
PubMed2000

A histochemical study of inflammatory lesions of the maxillary sinus mucosa using biotinylated lectins.

The distribution of glycoconjugates in normal maxillary sinus tissues, in cases of maxillary sinusitis and in postoperative maxillary cysts (POMC), was examined using seven different lectins as probes. The results showed that wheatgerm agglutinin (WGA), peanut agglutinin (PNA), Ulex europaeus agglutinin-1 (UEA-1), Ricinus communis agglutinin-1 (RCA-1), and concanavalin A (ConA) strongly react with the cilia and goblet cells. The binding of WGA, PNA, UEA-1, and RCA-1 was increased in maxillary sinusitis and POMC compared with normal maxillary sinus epithelium, whereas that of ConA was decreased. The decreased binding of ConA suggested that there were fewer mannoside residues in the maxillary sinus epithelium in the inflammatory lesion. The PNA bound to the cilia, goblet cells and mucous glandular cells in maxillary sinusitis and POMC, but not in normal, uninflamed cells, indicating that D-galactose was produced by the inflammatory condition. Similar binding patterns of PNA and RCA-1 were found in the cilia and on the surface of the epithelium and in the goblet cells. It is assumed that the carbohydrate moiety in the sinus mucosa is altered in inflammatory conditions.

Acetylgalactosamine↗
PubMed1985

Distribution of lectin binding sites in rabbit oviduct.

The carbohydrate histochemistry of the rabbit oviduct has been examined by the use of four lectins conjugated with horseradish peroxidase as histochemical reagents. Each lectin gave a very distinct typical pattern of binding, but for each lectin there was no difference between the distribution of binding sites in ampulla and isthmus. Wheat germ lectin bound exclusively with the connective tissue of the oviduct folds; winged pea lectin was detected only in the ciliated cells; peanut lectin binding sites were visualized in the secretory cells; the binding reactivity of soybean lectin was limited to the basal part of the cilia. Although it is very difficult at present to correlate the distribution of lectin binding sites with the function of the positive cells, some hypotheses have been advanced.

Animals↗