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)

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 present study examined the glycoconjugates of the lateral prostate using a battery of lectins. The results indicated that the secretory epithelium was rich in mannose (Man), N-acetylglucosamine (GlcNAc), galactose (Gal), N-acetylgalactosamine (GalNAc), and complex oligosaccharides. Con A (concanavalin A), LCA (Lens culinaris agglutinin), PSA (Pisum sativum agglutinin), WGA (wheat germ agglutinin), PWM (pokeweed mitogen), RCA-I (Racinus communis isolectin I), and PHA-P (Phaseolus vulgaris agglutinin-P) reacted intensely with both epithelia and stroma, while SBA (soybean agglutinin) and PNA (peanut agglutinin), which bind to terminal Gal, GalNAc, and Gal beta 1,3 GalNAc appeared to be specific to the secretory epithelium. SBA and PNA were useful as markers in the study of the secretory function of the prostate gland. The present study has shown that the Golgi apparatus of prostatic epithelial cells was rich in fucose (Fuc), oligomers of GlcNAc, Gal beta 1,3 GalNAc, Gal, and Man containing glycoconjugates, indicating that the gland was actively involved in glycosylation. The present study has also shown that LTA (Lotus tetragonolobus agglutinin) is a good marker for the epithelial Golgi. PNA also bound to the epithelial basement membrane and the connective tissue in the lamina propria. The present study has thus established, for the first time, the glycoconjugate patterns in the lateral prostate of the guinea pig.
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PMID:Glycoconjugates of the lateral prostate of the guinea pig: a lectin histochemical study. 192 63

Thirteen different, biotinylated plant lectins were tested for their ability to recognize specifically the glycoproteins of the two different plant rhabdoviruses potato yellow dwarf virus and eggplant mottled dwarf virus. All viruses were propagated on the same plant host species, Nicotiana rustica L. The lectin-binding to the viral proteins was tested after electrophoretic separation and transfer to nitrocellulose membranes. Besides purified virus also partially pure virus preparations were used for the tests, in order to determine the specificity. The lectins had been selected for specificities to either one of the following monosaccharides: mannose, glucose, galactose, N-acetyl-D-galactosamine, N-acetyl-D-glucosamine and fucose. In the test panel of thirteen lectins, seven were found to react with the viral glycoproteins. Among these, four (LCA, VFA, PSA, Con A) belonged to the mannosyl- or glycosyl-specific group. However, these four lectins reacted also with other host proteins when partially pure virus preparations were used as samples. The other three lectins (GSA2b, STA, WGA) were specific for N-acetyl-D-glucosamine and detected almost exclusively the viral glycoproteins. Two of these lectins, STA and WGA, were extremely suitable for virus-specific assays, since they did not react with glycoproteins in healthy controls that were identical or comparable in their electrophoretic mobility with the rhabdovirus glycoproteins. No binding to viral glycoproteins was observed with galactose-, N-acetyl-galactosamine- and fucose-specific lectins. The assay for rhabdovirus glycoproteins in plants with the lectins was approximately 8-16 times less sensitive than with virus-specific antibodies.
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PMID:Lectins as probes for the assay of rhabdovirus infections in plants. 368 Apr 62

Alterations in the expression of glycoconjugate structures during cartilage development in the chondrocranium, nasal skeleton, Meckel's cartilage, limb buds, vertebral bodies and ribs were investigated comparatively in 13 to 21-d-old rat embryos. The binding patterns of 24 biotinylated lectins were analysed in serial sections and compared with results obtained using histochemical methods. Proteoglycan distribution, assessed by conventional staining procedures, was not associated with lectin binding sites. During early fetal development, hyaluronate concentrations were enhanced in areas of prospective chondrogenesis. With few exceptions, the lectins showed a general increase in intensity of binding to mesenchymal structures. Con A (Canavalia ensiformis), DSL (Datura stramonium), and WGA (Triticum vulgare) displayed a ubiquitous distribution of binding sites. After incubation with LCA (Lens culinaris), PSA (Pisum sativum), STL (Solanum tuberosum), and VAA (Viscum album), characteristic differences in binding intensity between focal areas of developing mesenchyme were seen. DBA (Dolichus biflorus), ECL (Erythrina cristagalli), GSL I (Griffonia simplicifolia), LTA (Lotus tetragonobolus), SJA (Saphora japonica), UEA I (Ulex europaeus) and VVL (Vicia villosa) consistently failed to bind. During chondrogenesis a general reduction of lectin staining was detected. In early stages of development GSL II (Griffonia simplicifolia) was a specific marker of the prechondral blastema in the viscerocranium. PNA (Arachis hypogaea) selectively labelled the prevertebral blastema. In contrast, condensing mesenchyme of limb buds and viscerocranium was not stained. Using RCA (Ricinus communis), it was possible to distinguish chondroblasts from mature cells. All chondrocytes were stained by PSA, PHA-E, PHA-L (Phaseolus vulgaris E and L), and WGA, whereas Con A, LCA, and GSL II detected distinct differences between cartilage with different localisations. Cartilage matrix was constantly negative. Applying GSL II it was possible to distinguish specific segments of the perichondrium. From our results we conclude that especially high mannose oligosaccharides are amplified during development. Terminal sialic acid molecules, branched intralaminar glucose and/or mannose, respectively, internal galactose-(beta 1,4)-N-acetylglucosamine sequences as well as galactose-(beta 1,3)-N-acetylgalactosamine sequences in a preterminal position are diffusely distributed in mesenchymal tissue. In contrast, no evidence for the presence of terminal GlcNAc(beta 1,4)GlcNAc sequences and terminal alpha-fucosyl residues in (1,2) or (1,3)-linkage was obtained. Chondrogenesis appears to be correlated with a general reduction in the extent of expression of oligosaccharide structures. No proof of terminal N-acetylgalactosamine and alpha-galactose moieties was found, whereas our staining results document the expression of terminal beta-galactose structures in restricted areas of the developing mesenchyme.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:Glycoconjugate expression of chondrocytes and perichondrium during hyaline cartilage development in the rat. 759 87

The distribution of endogenous lectins, visualized by labelled neoglycoproteins, and of defined oligosaccharide structures, reactive with plant lectins, during fetal development of the fingers was analyzed in sections of human 3- to 8-month-old fetal specimens. Chondrogenesis as well as ossification were correlated with characteristic modulations in the expression of both glycoligand-binding molecules and characteristic carbohydrate structures. Occurrence of xylose-specific receptors was judged to be an early sign of cartilage development. Similarly, alpha-mannosyl residues that had been attached to labelled carrier proteins were strongly bound by the extracellular matrix already during early stages of finger maturation. Staining intensity for heparin gradually increased during chondrogenesis, whereas affinity for mannose showed a stage-related decline. Binding of mannose-6-phosphate was confined to hypertrophied cartilage of primary ossification centers. Accessible binding sites for terminal N-acetylneuraminic acid and N-acetylgalactosamine moieties were detected only in osteoid. In addition to monitoring the sugar-binding capacity, presence and developmental regulation of distinct carbohydrate structures were also assessed. PSA and SBA enabled the demonstration of an abrupt loss of staining affinity in the zone of maturing hypertrophic cartilage. Succinylated WGA proved to be an apparently useful marker of evolving bone tissue. GSL-II binding was restricted to chondroclasts and osteoclasts. The findings of this investigation are consistent with the supposed role of glycoconjugate-lectin interactions in cartilage and bone development.
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PMID:Distribution patterns of neoglycoprotein-binding sites (endogenous lectins) and lectin-reactive glycoconjugates during cartilage and bone formation in human finger. 877 14

In the present study, the expression of glycoconjugates in the guinea pig seminal vesicle was localized and partially characterized by lectin histochemistry using a battery of 30 different lectins specific for different carbohydrate residues. The results indicate that the glandular epithelium of the guinea pig seminal vesicle exhibits complex glycoconjugates rich in Man, beta-GlcNAc, beta-Gal, alpha/beta-GalNAc, Fuc and complex NeuAc(alpha2,6)Gal/GalNAc residues, as shown by its positive reactions to most lectins used. The Golgi region of the luminal secretory epithelial cells expresses a complex glycoconjugate pattern, as shown by its strong reactions to Man-(PSA, GNA), beta-GlcNAc-(S-WGA, PWA, DSA, UDA), beta-Gal-(RCA-I and -II), alpha/beta-GalNAc-(SBA, Jac, VVA, BPA) and complex NeuAc-(SNA) specific lectins, indicating that the secretory epithelial cells are active in glycosylation and secretion process. It was also shown in the present study that the basal and luminal epithelial cells are different in their glycoconjugates. The basal epithelial cells are rich in NeuAc(alpha2,3)Gal residues as they are stained specifically by MAA. The fibroblasts in the epithelial-smooth muscle interface and the smooth muscle cells close to the glandular epithelium are shown to express more glycoconjugates as they are stained intensely by GS-I-B4, GS-II and SBA. However, their role in the epithelial-stromal interaction in the seminal vesicle remains to be elucidated. In summary, the present study reports for the first time on the lectin binding patterns of the guinea pig seminal vesicle, and the results show that the seminal vesicle epithelium elaborates and secretes glycoconjugates in a complex pattern. Some of the lectins might be useful as histochemical markers for the secretory activity and specific structural components in the guinea pig seminal vesicle.
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PMID:Characterization of glycoconjugates of guinea pig seminal vesicle by lectin histochemistry. 1019 44

The present histochemical and cytochemical study using a lectin panel (WGA, GSI-A4, GSI-B4, PSA UEA-I, PNA, LCA, Con-A, DBA, MPA, BPA) has demonstrated that, in Podarcis sicula, the differentiation of small follicle cells into pyriform cells by means of intermediate cells is accompanied by the appearance of glycoproteins bearing alpha-GalNAc terminated O-linked side chains on the cell surface. The distribution of DBA- and MPA-binding sites over the follicular epithelium changed during the different stages of oocyte growth. DBA- and MPA-binding sites first appeared at the beginning of folliculogenesis within the zona pellucida (ZP) and on the surface of small cells, i.e., the stem cells of pyriform cells. Afterward, labeling was evident on the cell surfaces of intermediate cells and, later on, also of pyriform cells. On the other hand, no labeling was detected on the small cells located under the basal lamina, which, reportedly, do not differentiate into pyriform cells (Filosa et al. J. Embryol. Exp. Morphol., 1979; 15:297-316). Once pyriform cells were differentiated, the distribution of DBA- and MPA-binding sites over the follicular epithelium remained unchanged until intermediate and pyriform cells underwent apoptosis (Motta et al. J. Exp. Zool., 1996; 276:233-241) and the follicular epithelium transformed into a monolayer composed of small follicle cells only (Filosa Mon. Zool. Ital., 1973; 7:151-165). During this stage of oocyte growth, DBA and MPA labeling gradually decreased to completely disappear in the follicular epithelium of vitellogenic follicles. It is noteworthy that the observed changes in the distribution of DBA- and MPA-binding sites represent the first evidence recognized by lectins of a gradual modification of surface glycoprotein distribution over the follicular epithelium in the ovarian follicles of nonmammalian vertebrates so far studied. Finally, the zona pellucida (ZP), characterized by the presence of GalNAc, GluNAc, Man, and Gal, was demonstrated to be first synthetized by the oocyte and later on by the follicle cells.
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PMID:Pyriform cell differentiation in Podarcis sicula is accompanied by the appearance of surface glycoproteins bearing alpha-galNAc terminated chains. 1133 65

The present investigation demonstrates that in squamate reptiles, as already reported for Podarcis sicula (Andreuccetti et al., 2001), the differentiation of pyriform cells from small, stem follicle cells is characterized by the progressive appearance on the cell surface of glycoproteins bearing alpha-GalNAc terminated O-linked side chains. Using a lectin panel (WGA, GSI-A4, GSI-B4, PSA UEA-I, PNA, Con-A, DBA, LCA, BPA, SBA), we demonstrated that, during previtellogenesis, the pattern of distribution of DBA binding sites over the follicular epithelium dramatically changes. In fact, binding sites first appear in follicular epithelium at the time that small cells begin to differentiate; in such follicles, labeling is evident on the cell surfaces of small and intermediate cells. Later on, as the differentiation progresses, the binding sites also become evident on the cell surface of pyriform cells. Once differentiated, the pattern of the distribution of DBA binding sites over the follicular epithelium does not change. By contrast, during the phase of intermediate and pyriform cell regression, DBA binding sites gradually decrease, so that the monolayered follicular epithelium of vitellogenic follicles, constituted only by small cells, shows no binding sites for DBA. It is noteworthy that binding sites for DBA are present on small cells located in contact with the oocyte membrane, but not on those located under the basal lamina or among pyriform cells, and therefore not engaged in the differentiation into pyriform cells. This finding demonstrates that, in squamates, the pattern of distribution of alpha-N-GalNAc containing glycoproteins significantly changes during previtellogenesis, and that these modifications are probably related to the differentiation of small stem cells into highly specialized pyriforms.
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PMID:Surface glycoproteins bearing alpha-GalNAc terminated chains accompany pyriform cell differentiation in lizards. 1174 25

Renal proximal straight tubules (PST) of the female mouse contain periodic acid Schiff-positive lysosome granules. An excellent example of this is found in the kidneys of female DBA/2Cr mice. In the present study, lectin-histochemistry showed that lectin-positive granules occur in the PST of DBA/2Cr mice. Out of twenty-one lectins studied, the granules bound WGA, s-WGA, LEL, STL, DSL, GSL-II, VVL, RCA-I, ECL, PSA, LCA and PHA-E. Such granules were also observed in the proximal convoluted tubules (PCT). In addition, heterogeneous binding to the SBA or DBA was observed in the PST. Lectin-cytochemistry for s-WGA, STL, VVL, RCA-I, ECL and PSA, showed that: 1) lysosomes bind a higher level of s-WGA or STL than VVL, RCA-I, ECL or PSA; 2) PSA binding is similar in PST and PCT; 3) there are many PCT lysosomes that are negative for s-WGA, STL, VVL, RCA-I, and ECL lectin binding; and 4) s-WGA binding is highly specific to the lysosomes of the PST. Based on the binding specificities of each lectin, it was suggested that the mannose content of PST and PCT lysosomes is similar, and that PST lysosomes have a high level of N-acetylglucosamine, N-acetylgalactosamine, galactose or galactosyl (beta 1, 4) N-acetylglucosamine.
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PMID:Lectin-histochemical and -cytochemical study of periodic acid Schiff-positive lysosome granules as a histological feature of the female mouse kidney. 1237 Nov 28

The lectin-binding characteristics of the epithelial lining of the thoracic air sacs of the chicken were determined. Con A, LCA and PSA bound to the apical membrane as well as to the cytoplasm distal to the nucleus of the surface epithelium, indicated the presence of a-linked mannose as well as N-acetylchitobiose-linked alpha-fucose residues in the glycoproteins. GSL I bound to the apical membrane and cytoplasm distal to the nucleus, but not to the cilia of the epithelium, where-as MPL, DBA and RCA120 bound to the apical membrane, cilia and cytoplasm, indicated the presence of a-linked N-acetylgalactosamine residues. However, neither SJA or SBA showed any binding, indicating the absence of beta anomers of galactosyl (beta1.3)N-acetylgalactosamine and beta-linked N-acetylgalactosamine residues. UEA I bound to the apical membrane and cilia, as well as to the cytoplasm of a few cells, indicated the presence of alpha-linked fucose residues. PNA bound to the apical membrane of some, but not all, surface epithelium cells, indicated the presence of galactosyl (beta1.3)N-acetylgalactosamine residues. WGA bound to the apical membrane and cilia, as well as to the cytoplasm of a few cells, indicated the presence of neuraminic acid residues.
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PMID:A lectin histochemical study of the thoracic respiratory air sacs of the fowl. 1613 35


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