Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C1519176 (PSA)
 5,490 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The distribution of binding sites for 13 lectins with different specificities was studied in adult and new-born rat kidney tissue by staining paraffin sections with the ABC method. Various segments of the uriniferous tubule in both rats showed differential affinity for lectins. None of these lectins showed any reactivity with the immature developmental components of kidney like S-shaped bodies and mesonephric blastema. In the new-born rat kidney, the reactivity of 4 lectins (DBA, PNA, SBA and WGA) on the proximal tubules was very weak compared with the adult rat. Seven lectins (RCA-I, BSL-I, WGA, UEA-I, PHA-E, PSA, LCA), which stained the glomerulus of adult rats, failed to react with glomerular turf in new-born rat kidneys. On the contrary, 4 lectins (RCA-I, WGA, UEA-I and PHA-E) out of these 7 lectins stained the surface of podocyte in the new-born kidney. Colloidal iron stained glomerular turf in adult rats also showed less reactivity in immature glomerulus. These results suggested that changes in lectin binding reactivity are associated with the development and the differentiation of the rat kidney.
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PMID:[Lectin reactivity in the kidney of newborn rat compared to adult rat]. 128 87

The role of glycochains of cell surface glycoproteins in the cell to collagen interaction was examined by studying the effect of lectins on the fibroblast-mediated collagen gel contraction. Lectins of Phaseolus vulgaris agglutinin (PHA), concanavalin A (ConA), lentil seed agglutinin (LCA), pea agglutinin (PSA), Ricinus communis agglutinin-60 (RCA), and wheat germ agglutinin (WGA) dose-dependently inhibited gel contraction, while lectins of mushroom agglutinin (ABA), peanut agglutinin (PNA), pokeweed mitogen (PWM), and soybean agglutinin (SBA) did not. Of these lectins, PHA seemed to be worthy of further analysis, because PHA, but not other lectins, inhibited spreading of fibroblasts on collagen fibrils but not on plastic or gelatin, suggesting that cell-surface glycoproteins responsive to the lectin are involved in the specific binding of fibroblasts to native collagen fibrils. The inhibitory effect of PHA-E4, an isolectin of PHA, was more intense than that of PHA-L4, another isolectin of PHA. The collagen gel contraction was also inhibited by tunicamycin and monensin in a concentration-dependent and reversible manner. These results strongly suggest that PHA-E4-reactive glycoproteins of the fibroblast surface play an important role in cell to collagen binding during the gel contraction. Five membrane proteins including beta 1 subunits of the integrin family were obtained by affinity chromatography with PHA-E4.
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PMID:Recognition of collagen by fibroblasts through cell surface glycoproteins reactive with Phaseolus vulgaris agglutinin. 132 83

The use of fluorescein-conjugated Pisum sativum agglutinin (FITC-PSA) was evaluated for its ability to distinguish acrosome-intact from acrosome-damaged stallion spermatozoa. Incubation of fresh (acrosome-intact) and frozen-thawed (acrosome-damaged) spermatozoa with FITC-PSA resulted in acrosome-intact spermatozoa that exhibited no fluorescence, while acrosome-damaged spermatozoa exhibited fluorescent staining over the rostral portion of the head and equatorial segment. Experiments using mixtures of various ratios of acrosome-intact and acrosome-damaged spermatozoa determined the precision (intrasample coefficient of variation), and linearity (increased percentage of spermatozoa with PSA binding, with increased percentage of frozen-thawed spermatozoa in a sample) of FITC-PSA binding. The binding of FITC-PSA increased in samples as the portion of frozen-thawed (acrosome-damaged) to fresh (acrosome-intact) spermatozoa increased. A positive correlation existed (r = 0.98, P less than 0.05) between the percentage of FITC-PSA bound sperm and the proportion of damaged spermatozoa added to a sample. Location of PSA lectin binding on acrosome-damaged spermatozoa, determined by electron microscopy using gold-conjugated PSA, was to components of the outer acrosomal membrane and acrosomal matrix. These results demonstrate that FITC-PSA binding may be useful in determining acrosomal integrity of fresh and frozen-thawed stallion spermatozoa.
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PMID:Assessment of Pisum sativum agglutinin in identifying acrosomal damage in stallion spermatozoa. 151 46

Cryostat sections from rat gracilis muscles were incubated with different biotinylated lectins: Con A (Concanavilin A), WGA (Wheat germ agglutinin), SBA (soybean agglutinin), GS I and GS II (Griffonia simplicifolia agglutinin), LCA (Lens culinaris agglutinin), PNA (peanut agglutinin) and PSA (Pisum sativum agglutinin). The sections were subsequently treated with alkaline phosphatase conjugated avidin. The lectin binding sites were visualized after incubation in substrate media containing: (1) 5-bromo-4-chloro indoxyl phosphate and Nitro Blue tetrazolium or copper sulphate; (2) naphthol AS-MX phosphate or naphthol AS-BI phosphate and various types of diazonium salts; (3) alpha-naphthylphosphate and Fast Blue BB; (4) beta-glycerophosphate according to the method of Gomori. The results obtained with the alkaline phosphatase methods were compared with those seen with a streptavidin-horseradish peroxidase procedure. Several chromogen protocols for visualizing alkaline phosphatase activity showed differences in the ability to detect lectin binding sites. A sarcoplasmic reaction was evident for Con A, GS II, WGA, LCA, and PSA after incubation in the indoxyl phosphate medium. Sarcoplasmic reaction for GS II was also noticed after incubation with naphthol AS-MX Fast Blue BB and beta-glycerophosphate. The latter substrate also gave rise to a sarcoplasmic Con A reaction. With the indoxylphosphate tetrazolium salt method some muscle fibres showed a very strong intracellular reaction after incubation with Con A and GS II while the staining intensity was weak in other fibres. The same muscle fibres were stained with PAS. No sarcoplasmic reactions were observed with either naphthol phosphate media or with the diaminobenzidine peroxidase methods. Further, the staining of the muscle fibre periphery, connective tissue, an capillaries was intensified using the indoxyl method. The indoxylphosphate-tetrazolium salt method seems to be suitable for future investigations of lectin binding sites in muscle sections.
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PMID:Lectin binding in skeletal muscle. Evaluation of alkaline phosphatase conjugated avidin staining procedures. 171 10

A selection of lectins was used to investigate developmentally regulated changes in the distribution of cell surface oligosaccharides during the gastrulation and neurulation stages of early chick embryo development. Lectins from three specificity classes were used: glucose/mannose specificity (concanavalin A [Con A], Lens culinaris agglutinin [LCA], Pisum sativum agglutinin [PSA]); N-acetylglucosamine specificity (Lycopersicon esculentum agglutinin [LEA], wheat germ agglutinin [WGA], succinylated WGA [sWGA]); N-acetylgalactosamine/galactose specificity (Dolichos biflorus agglutinin [DBA], soybean agglutinin [SBA], Sophora japonica agglutinin [SJA], Bandeiraea (Griffonia) simplicifolia lectin I [BSL I], peanut agglutinin [PNA], Artocarpus integrifolia lectin [Jacalin], Ricinus communis agglutinin-1 [RCA-1], Erythrina cristagalli lectin [ECL]). At gastrulation stages, patterns of lectin binding could be distinguished in the epiblast, mesoderm, and endoderm cell layers. The primitive streak failed to bind any of the lectins, but LEA and WGA bound to the epiblast in regions lateral to the streak, indicating the loss of some glucosamine residues medially in preparation for the ingression movements of gastrulation. Several lectins showed marked binding to the mesoderm cells after their passage through the primitive streak; these were LCA, PSA, WGA, sWGA, BSL, and most particularly PNA. Therefore, the epithelial-mesenchymal transformation from epiblast to mesoderm at the primitive streak is accompanied by cell surface oligosaccharide changes in the epiblast and mesoderm that involve all classes of lectins including the PNA-binding sequence Gal beta 1-3GalNAc. Ultrastructurally, PNA was shown to bind extracellularly to matrix fibrils. Jacalin, having the same sugar specificity as PNA, but binding to serine/threonine linked chains rather than asparagine linked chains showed no binding to the mesoderm.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Changes in glycoconjugate expression during early chick embryo development: a lectin-binding study. 174 24

The lectin binding pattern of bone marrow cells in normal and reactive states and in various neoplastic disorders was investigated using trephine biopsy specimens taken from the iliac crest. The tissue samples were routinely processed (fixed in formalin and embedded in paraffin wax) and subjected to mild decalcification with EDTA. The following results were obtained. (1) More than half of the 23 fluoresceinated lectins used reacted with normal blood cells and/or their neoplastic derivatives. Inhibition tests with the appropriate sugars confirmed the specificity of binding for the majority, but not all, of the lectins. (2) WGA, Con A, PSA, STA and RCA60 and RCA120 produced a particularly intense reaction with normal, reactive and neoplastic myeloid cells. Erythroblasts exhibited weak staining in a few cases by a few lectins (WGA producing the strongest staining), while megakaryocytes nearly always remained unstained. Neoplastic lymphoid cells in various lymphoproliferative disorders and plasmacytoma cells generally reacted with the same lectins as the myeloid cells. (3) Since neoplastic myeloid cells in various myelodysplastic and myeloproliferative disorders exhibited a lectin binding pattern similar to that of myeloid cells in normal and reactive bone marrow, it is unlikely that lectin histochemistry of the bone marrow will prove of great value in the diagnosis of myelodysplastic-myeloproliferative disorders.
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PMID:Lectin histochemistry of human bone marrow: investigation of trephine biopsy specimens in normal and reactive states and neoplastic disorders. 178 64

Ion transport cells in gerbil inner ear were differentiated histochemically by staining glycoconjugates (GCs) with a battery of horseradish peroxidase-conjugated lectins. Strong staining with PSA and LCA showed a high content of N-linked oligosaccharides in transport cell GCs. Reactivity with PHA-L and PHA-E identified GC with triantennary and with bisected biantennary N-linked oligosaccharides, respectively, in these cells. High affinity for DSA and PWM demonstrated abundant N-acetyl lactosamine in N-linked side chains. Ion transporting epithelial cells reacting with lectins specific for N-linked oligosaccharides included strial marginal cells and outer sulcus cells of the cochlea and dark cells, transitional cells, and planum semilunatum cells of the vestibular system. In general, all of the inner ear transport epithelial cells revealed a similar lectin binding profile, with the one exception that SBA reacted strongly with ion transporting cells in the vestibular system but only weakly with those in the cochlea. Fibrocytes specialized for ion transport located in distinct areas in the suprastrial and inferior regions of the spiral ligament also stained with lectins that demonstrate N-glycosylation. However, transport fibrocytes differed from transport epithelial cells in two ways. First, they reacted e with HPA, DBA, VVA, and SJA specific for O-linkages and second, they failed to react with UEA I. The staining pattern for N-glycosylated GC resembled that for Na+, K(+)-ATPase in inner ear, suggesting a relationship between these constituents.
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PMID:Distribution of glycoconjugates in ion transport cells of gerbil inner ear. 184 71

The interaction of a series of synthetic, branched trisaccharides with five D-mannose-specific lectins was studied by precipitation-inhibition assay. The branched methyl alpha-D-mannotrioside, alpha-D-Manp-(1----3)-[alpha-D-Manp-(1----6)]-alpha-D-Man pOMe, the best inhibitor of the Con A-Dextran interaction, was 42 times more potent than alpha-D-ManpOMe, and 3-6 times more potent than the two trisaccharides substituted with D-glucosyl groups, and 8-15 times those with D-galactosyl groups. Surprisingly, methyl O-alpha-D-mannopyranosyl-(1----3)-alpha-D-mannopyranoside was bound to Con A 8-fold more avidly than methyl alpha-D-mannopyranoside. However, the related pea lectin (PSA) was singularly different from Con A in its carbohydrate-binding activity, showing no significantly enhanced binding to any of the sugars examined. The trisacchrides containing terminal, nonreducing, (1----3)-linked alpha-D-mannopyranosyl groups, i.e., alpha-D-Manp-(1----3)-[alpha-D-Glep-(1----6)]alpha-D-Manp OMe, alpha-D-Manp-(1----3)]-alpha-D-Galp-(1----6)]-alpha-D-ManpOMe++ +, and alpha-D-Manp-(1----3)-[alpha-D-Manp-(1----6)]-alpha-D-Man pOMe, were the best inhibitors of the snowdrop lectin (GNA)-D-mannan precipitation system. On the other hand, all branched trisaccharides exhibited very similar inhibitory potencies toward the daffodil lectin (NPA)-D-mannan interaction, whereas alpha-D-Manp-(1----3)-[alpha-D-Galp-(1----6)]-alpha-D-ManpOMe++ + and alpha-D-Manp-(1----3)-[alpha-D-Manp-(1----6)]-alpha-D-Man pOMe were somewhat better inhibitors than the other branched trisaccharides of the amaryllis lectin (HHA)-D-mannan precipitation reaction. (ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Interactions of five D-mannose-specific lectins with a series of synthetic branched trisaccharides. 193 32

Influence on the clearance of background radioactivity from the blood was studied by using a chemically galactosylated antibody to the radiopharmaceutical. Sodium iodide I 125-labelled Pisum sativum agglutinin (125I-PSA) was used as the model tumor-imaging radiopharmaceutical in this series of experiments. Rabbit (anti-PSA) immunoglobulin G (IgG) was chemically galactosylated with varying amounts of cyanomethylgalactose. Galactose concentration ranged from 11 to 17 mol/mol protein. Antibody activity was not affected by chemical galactosylation under the experimental conditions used. Blood clearance of the galactosylated anti-PSA (GAP) in normal mice was enhanced to varying degrees, depending on the degree of galactosylation; similarly, liver uptake was increased with the degree of galactosylation. Following injection of 125I-PSA in normal mice, the lectin was rapidly removed from the blood by subsequent injection of GAP. Increased hepatic uptake of the complex (lectin-galactosylated antibody) via protein-carbohydrate recognition caused the pronounced decrease in the 125I-PSA blood level. The effective time for 125I-PSA removal was as short as 15 min. The potency was dependent on the degree of galactosylation of the antibody. In sarcoma 180 (S-180) tumor-bearing mice, the capacity for blood clearance of 125I-PSA was also positively correlated to the degree of galactosylation. Moreover, the variation in the delivered dose ratio of antibody to lectin proved to lead to a further increase in background clearance. As a result, especially the tumor:blood ratio was significantly improved by a single administration of chemically galactosylated antibody, as compared with the value measured in the presence of unmodified antibody. These initial studies suggest that administration of GAP may improve nuclear imaging with radiopharmaceuticals.
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PMID:Rapid background reduction of circulating sodium iodide I 125-labelled Pisum sativum agglutinin used as a tumor-imaging radiopharmaceutical by the chemically galactosylated antibody. 220 46

The interactions of fish trypanosome culture forms with 11 purified lectins were compared using the agglutination test in microwell plates. Altogether, ten stocks of ten different freshwater fish species were examined. Three basic types of cell-lectin interactions were observed on the microscopical level. The strong agglutination of all stocks regardless their original host was found in the presence of Con A, PSA, RCA60, and RCA120, which implies the presence of relatively high amounts of sugar residues of D-mannose and D-galactose in the surface of culture forms of these parasites. Weak agglutinations of some stocks were observed in the presence of LCA, PNA, SBA, and WGA lectins, but their low intensity makes them not sufficiently reliable for stock characterization. The lectins UEA I, HPA, and PHA caused no agglutination. In conclusion, in case of unequivocal results no remarkable differences in the interactions of various stocks of trypanosomes culture forms with used lectins were observed. These results imply the high degree of similarity of their main cell surface saccharide structures.
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PMID:The interaction of fish trypanosome culture forms with some lectins. 233 95


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