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Query: UMLS:C1519176 (PSA)
 5,490 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Lectin-binding patterns of the three olfactory receptors, olfactory epithelium (OE), vomeronasal organ (VNO) and septal olfactory organ of Masera (MO), and their associated glands, Bowman's gland (BG) of the OE, Jacobson's gland (JG) of the VNO, and anonymous gland (MG) of the MO were examined in the rat with 21 biotinylated lectins. On the free surface of the receptors, all lectins showed moderate to intense staining in at least one of receptors, although PHA-E in the VNO, BSL II and PNA in the MO, and DBA, BSL I, VVA, SJA, PSA and LCA in both the OE and the MO showed no staining. In the soma of receptor neurons, 16 lectins showed staining in at least one of receptors, although SJA showed no staining in both the OE and the MO, and BSL I showed staining in a small number of cells in these receptors. In the associated glands, 15 lectins showed staining in at least one of them, although PNA in the JG, LEL in the MG, and s-WGA and DBA in both the BG and the MG showed no staining. These findings suggest that the VNO takes charge of an olfactory discrimination different from that of the OE and MO, although the latter two take charge of that similar to each other.
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PMID:[Lectin-binding patterns of the olfactory receptors (olfactory epithelium, vomeronasal organ and septal olfactory organ of Masera) in the rat]. 811 43

The distribution of lectin receptors in the human tonsil was studied using 16 biotinylated lectins. The avidin-biotin-peroxidase complex (ABC) method was used on frozen and paraffin-embedded tissue sections. Cell suspensions were also analysed by dual flow cytometry using respective fluorescein isothiocyanate-conjugated lectins and phycoerythrin-labeled anti-CD3 and anti-human immunoglobulin. Frozen sections fixed with acetone and paraffin-embedded materials fixed in three solutions were compared for lectin affinity; ethanol-fixed sections gave best results followed by frozen and buffered formalin-fixed ones, then nonbuffered formalin. Con-A, RCA-1, LcH, WGA, MPA, PHA, PSA, PNA, SJA and GSA-1 reacted with all tissue components of the tonsil in immunohistochemical studies, but binding intensity was fixative dependent. Binding of Lotus and BPA to lymphocytes was limited to germinal center lymphocytes. Other tissue components were also reactive but staining intensity was weaker in Lotus compared with BPA. SBA and DBA did not react with lymphocytes, but reacted with macrophages/histiocytes, vascular endothelia, and epithelial cells. LBA and LPA were constantly negative with all tissue components irrespective of fixatives. Flow cytometric analyses showed that all but three (DBA, LBA and LPA) partially or totally stained lymphocyte surfaces. Lotus receptors were expressed exclusively on B-lymphocytes.
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PMID:Distribution of lectin receptors in the human hyperplastic tonsil: histochemical and flow cytometric analyses. 846 May 51

The carbohydrate histochemistry of normal porcine small intestine from eight one- to four week-old pigs was investigated by the use of twenty one biotinylated-labeled lectins with avidin-biotin-peroxidase complex method. Five patterns of staining were seen. First, lectins were reacted with brush borders in enterocytes only, i.e. DBA, LEL, STL and PNA. Second, reactivity of lectins were specific for goblet cells, i.e. PSA. Third, lectins were reacted with both brush borders and goblet cells, i.e. RCA I, BSL II, DSL, WGA, Jacalin, ECL, ConA, LCA, UEA-1, PHA-E and PHA-L. Fourth, lectins were positive for brush borders but binding patterns of goblet cells were variable, i.E. BSL I and VVA. Fifth, the binding patterns were variable for brush borders and goblet cells. The binding patterns for SBA, SJA and s-WGA were variable. DSL bound weakly at first-week old pigs, and as the pigs aged, lectin reactivity on the brush borders of enterocytes as well as goblet cells increased. In contrast, STL, PNA and LEL bound strongly at first- and second-week old pigs, and as the pigs aged, lectin reactivity on the brush borders of ileal enterocytes decreased. Our results suggest the distinct age-region-, and cell types-related changes in epithelial glycocalyx as well as goblet cell mucins in the porcine jejunum and ileum.
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PMID:Age-related lectin histochemical changes in the porcine small intestine. 859 97

Distinct glycoconjugate expression between dome enterocytes and villus enterocytes in ileum from twelve 3-week-old conventional pigs was examined by the use of twenty one biotinylated lectins with avidin-biotin-peroxidase complex method. Three patterns of staining were seen. First, lectins bind to dome enterocyte and villus enterocyte to approximately equal staining, i.e. DSL, WGA, s-WGA and ConA. Second, lectins display a markedly higher affinity for villus enterocyte than dome enterocyte, i.e. DBA, SBA, RCA I, SJA, VVA, BSL II, LEL, PNA, Jacalin, and ECL. Third, lectins exhibit negative staining to dome enterocyte only, i.e. PSA, LCA, UEA-I, and STL. Four lectins; PSA, LCA, UEA-I, STL may be useful negative marker to differentiate glycoconjugate expression between dome enterocyte and villus enterocyte. The staining patterns are slightly different among these negative markers. Three lectins, PSA, LCA, and UEA-1, are negative marker to differentiate dome enterocytes and villus enterocytes. But STL is also negative to dome epithelial surface and moderately positive to villus brush border. It is suggested that the present lectin-binding studies provide the marker of dome enterocyte as compared with villus enterocytes.
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PMID:Lectin histochemical characteristics of the epithelial surface of ileal Peyer's patches in 3-week-old pigs. 936 44

Cerebella from suckling and adult rats were examined histochemically with 19 different biotin-labeled lectins. Purkinje cells from postnatal rats had a marked ability to combine with many lectins, but minimal ability was found in adult rats except for Con-A, LEL, and MAL lectins. The cell body of Purkinje cells on postnatal day 7 was strongly labeled with 6 lectins (Con-A, LTL, MAL, SJA, UEA-I, and VVA). Only moderate staining was observed with these lectins on postnatal day 5. The dendritic tree of the cells showed a moderate labeling ability with LTL and UEA-I on postnatal days 15 and 20. The dendritic tree was strongly labeled with MAL on postnatal days 10, 15, 20 and adult. Positive reactions were observed in the cells when cerebellar sections from rats on postnatal day 7 were incubated with 3 other lectins (AAL, LEL, and SBA). The cells on postnatal day 7 were rarely labeled with BSL-II, DBA, DSL, LCA, PNA, PSA, RCA120, SSA, STL, and WGA. Purkinje cells on postnatal day 7 may be rich in N-linked oligosaccharides, with terminal sugar structures that resemble blood-group-related antigens (type H) and/or tumor-related antigens. These glycoconjugates may be present at low levels in the Purkinje cells of adult rats. Dendrites of Purkinje cells of adult rats were strongly labeled by Con-A, LEL, and MAL. The dendrites of Purkinje cells may be rich in highly branched oligosaccharides.
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PMID:Compositional changes in glycoconjugates recognized histochemically with lectins in Purkinje cells in suckling and adult rats. 961 15

Conventional histochemistry and the binding patterns of 22 biotinylated lectins were examined for characterisation of glycoconjugates in the components of the olfactory mucosa of the armadillo Chaetophractus villosus. The mucous lining the olfactory epithelium showed binding sites for DSL, WGA, STL, LEL, PHA-E and JAC. Only the basilar processes of the supporting cells stained for Con-A and S-Con A. The olfactory receptor neurons stained with LEL, LCA, Con A, S-Con A, JAC and PNA. The layer of basal cells did not react with any of the lectins studied. Bowman's glands in the lamina propria showed subpopulations of acinar cells reacting with SBA, S-WGA, WGA, STL, Con A, PSA, PNA, SJA, VVA, JAC and S-Con A, but in our optical studies with lectins we were unable to differentiate between mucous and serous cells in the way that is possible on electron microscopy. The ducts of Bowman's glands were labelled with S-WGA, STL, LEL, PHA-E, BSL-I and JAC. This histochemical study on the glycoconjugates of the olfactory mucosa in the order Xenarthra provides a basis for further experimental investigations.
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PMID:Identification and localisation of glycoconjugates in the olfactory mucosa of the armadillo Chaetophractus villosus. 1038 77

Glomeruli within the main olfactory bulb (MOB) are known as areas of synapse formation between axon terminals of olfactory neurons in the olfactory epithelium and dendrites of the first relay neurons (mitral and tufted cells) in the MOB, so that they serve as functional units in olfaction. We examined expression patterns of glycoconjugates in the glomeruli of the hamster MOB by lectin histochemistry using 21 biotinylated lectins. Thirteen lectins, WGA, s-WGA, DSL, DBA, SBA, WA, SJA, RCA-I, PNA, ECL, UEA-I, PSA and LCA, showed differential binding patterns among the glomeruli. To evaluate these differential binding patterns of lectins, we analysed staining intensity of each of the 13 lectins on the level of individual glomeruli by image analysis, and classified staining intensity into five grades (negative, 1+, 2+, 3+, 4+) on the basis of results obtained. This classification enables us to make detailed comparison among individual glomeruli. We further analysed the grade of staining intensity of each of the 13 lectins in the same glomerulus in adjacent serial sections by image analysis, and found that individual glomeruli varied in combination of grades of staining intensity and kinds of lectins. These results indicate that glycoconjugates are expressed heterogeneously in individual glomeruli, and that heterogeneous expression may contribute to the topographic organization of the primary olfactory pathway.
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PMID:Heterogeneous expression of glycoconjugates among individual glomeruli of the hamster main olfactory bulb. 1057 58

Conventional carbohydrate histochemistry and the binding patterns of 21 lectins were analysed to characterise the glycoconjugate content in the components of the vomeronasal organ of the armadillo Chaetophractus villosus. The mucomicrovillous complex of the sensory epithelium bound most of the lectins studied. No reaction was observed with Con A, PSA, S-Con A and SBA, and the sustentacular cells were-stained with UEA-I, DSL, LEL, STL and Con A. The vomeronasal receptor neurons were labelled with S-WGA, WGA, PNA, UEA-I, STL, Con A, S-Con A, ECL and RCA120. The basal cell layer reacted with S-WGA, WGA, LCA, UEA-I, DSL, LEL, STL, Con A, JAC and VVA. The nonsensory epithelium exhibited a differential staining in relation to the different components. The mucociliary complex stained with ECL, DBA, JAC, RCA120, STL, LCA, PHA-E, PHA-L, LEL, BSL-I and VVA. However, SJA and UEA-I stained the mucus complex lining a subpopulation of columnar cells. The cytoplasm and cell membranes of columnar cells was labelled with DBA, DSL and LCA. The apical region of these cells exhibited moderate reactivity with LEL and SJA. None of the lectins bound specifically to secretory granules of the nonsecretory cells. Basal cells of the nonsensory epithelium were labelled with DSL, LEL, LCA, BSL-I and STL. The vomeronasal glands showed a positive reaction with WGA, DSL, LEL, LCA, DBA, PNA, RCA120 and SBA. Subpopulations of acinar cells were observed with ECL, S-WGA, Con A, S-Con A and DBA. PNA and RCA120 stained the cells lining the glandular ducts. In comparison with previous results obtained in the olfactory mucosa of the same group of armadillos, the carbohydrate composition of the vomeronasal organ sensory epithelium differed from the olfactory sensory epithelium. This is probably related to the different nature of molecules involved in the perireceptor processes.
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PMID:Characterisation of glycoconjugate sugar residues in the vomeronasal organ of the armadillo Chaetophractus villosus (Mammalia, Xenarthra). 1085 58

PH-20 is a glycoprotein located on the surface of the sperm plasma membrane and on the inner acrosomal membrane. The best understood function of sperm surface PH-20 is its hyaluronidase activity, which results in hydrolysis of the hyaluronic acid-rich cumulus matrix during sperm penetration of this extracellular oocyte investment. In this study, we investigated whether alterations in the secondary and tertiary structures of sperm surface PH-20 would affect its enzyme activity. Proteins were isolated from the sperm plasma membrane by treatment of living cells with phosphatidylinositol-specific phospholipase C (PI-PLC). PH-20 was purified from the PI-PLC released proteins by immunoaffinity chromatography. Two-dimensional electrophoresis of purified PH-20 revealed 6 isoforms with isoelectric points ranging from 5.1 to 6.0. Removal of the N-linked glycans from PH-20 with N-glycosidase F shifted the molecular weight from 64 kd to approximately 54 kd, its deduced molecular weight based on sequence analysis, suggesting that most if not all, of the potential N-glycosylation sites are linked to oligosaccharides. The lectins Con A and PSA recognized purified sperm surface PH-20 after Western blotting, suggesting that mannose is a major sugar within or at the terminal end of the linked glycan. The lectins UEA and LPA did not recognize PH-20 Western blot, suggesting that fucose and sialic acid are not terminal sugars of sperm surface PH-20. Deglycosylation of sperm surface PH-20 resulted in a complete loss of its hyaluronidase activity. The reduction of disulfide bonds with beta-mercaptoethanol or dithiothreitol also resulted in loss of enzyme activity. We conclude that the hyaluronidase activity of sperm surface PH-20 is dependent on structural features established by sulfhydryl linkages, as well as glycosylation.
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PMID:Importance of glycosylation and disulfide bonds in hyaluronidase activity of macaque sperm surface PH-20. 1186 14

A screening method to determine the binding behavior of lectins toward recombinant human erythropoietin (rHuEPO) was developed. Twenty-three different lectins were tested for this purpose. rHuEPO isoforms were separated by isoelectric focusing using the International Olympic Committee (IOC) and World Anti-Doping Agency (WADA) accredited method for the direct detection of the prohibited doping substance erythropoietin (EPO). For the visualization of the rHuEPO isoforms lectins were used instead of antibodies. Optimization of the screening protocol enabled the detection of a maximum number of rHuEPO isoforms. By means of this protocol information about the binding properties of a lectin toward each individual rHuEPO isoform was accessible. All evaluated lectins showed significant differences in their binding behavior. The most intense response was obtained with WGA, DSL, PHA-E, LEL, PSA, and LCA. While WGA, DSL, PHA-E, and LEL were able to bind all isoforms detected by the standard antibody, LCA and PSA demonstrated a clear preference for rHuEPO isoforms located in the more basic region of the electropherogram. Further lectins tested were ConA, succWGA, PHA-L, RCA, SNA, MAA, STL, ECL, GSL-II, SJA, SBA, UEA-I, Jacalin, PNA, DBA, GSL-I, and VVA. Compared to the lectins mentioned above, they showed reduced sensitivity. Endogenous and recombinant EPO only differ in the composition of their N- and O-glycan moieties. As lectins possess the unique ability to recognize subtle differences in glycan substructures, they represent an interesting approach for their structural characterization. Furthermore, they might be useful for affinity enrichment/purification of rHuEPO in doping control.
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PMID:Detection of isoforms of recombinant human erythropoietin by various plant lectins after isoelectric focusing. 1570 48


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