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)

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

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

Tear samples were collected from 46 healthy volunteers evenly distributed according to sex and age (mean age 43.5 years). Samples were denatured in a Tris-HCl sample buffer containing 2-mercaptoethanol and SDS, and applied to a gradient SDS-polyacrylamide gel for electrophoresis. The proteinaceous material was transferred to nitrocellulose by a semi-dry blotting technique, and the glycoprotein content subsequently visualized by incubation with four lectins (WGA, PHA, PSA and SBA) and staining with avidin horseradish-peroxidase. Glycoprotein bands were generally found to be significantly less frequent in persons under the age of 30 years. Apart from this the technique gave a uniform picture of the glycoprotein profile, with only modest differences according to age and/or sex. The technique may therefore be suitable for the detection of differences in the glycoprotein composition indicative of disease.
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PMID:The normal human tear glycoprotein profile detected with lectin probes. 193 80

Thirty-one canine adenocarcinomas of prostatic origin were examined immunohistochemically with antibodies generated against three prostate-specific antigens by using a peroxidase-antiperoxidase technique. Primary antibodies included two generated with human prostatic antigens (PSA, PSAP) and one generated with a canine prostatic antigen (CPSP). Eight of 31 adenocarcinomas were positive with CPSP, two were positive with PSA, and three were PSAP positive. Normal and hyperplastic canine prostatic epithelium was strongly positive with all three markers. These results contrast with those in human studies in which PSA and PSAP stain normal and neoplastic epithelium with comparable intensity in all but the most anaplastic tumors.
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PMID:Adenocarcinoma of the canine prostate: immunohistochemical examination for secretory antigens. 244 55

Bouin-fixed and paraffin-embedded sections from the dorsal skin of Bufo bufo and Xenopus Laevis were subjected to lectin histochemistry. A panel of biotinylated lectins (Con-A, PSA, LCA, UEA-I, DBA, SBA, SJA, RCA-I, BSL-I, WGA, s-WGA, PHA-E and PHA-L) and an avidin-biotin-peroxidase complex (ABC) showed a species-specific compartmentalization of saccharides to certain parts of the epidermis and glandular domains. Some marked histochemical differences between the two examined species adapted to fully aquatic (X. laevis) or semiterrestrial (B. bufo) environments may be relevant of a relationship existing between habitat selection and the glycosaminoglycans content of the skin. In addition the technique used in this paper may be applicable for further studies of the carbohydrate composition in various tissues of lower vertebrates.
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PMID:Comparative lectin-binding patterns in the epidermis and dermal glands of Bufo bufo (L.) and Xenopus laevis (Daudin). 251 85

We studied the subcellular localization of glycoconjugates recognized by the garden pea and lentil lectins (Pisum sativum, PSA; Lens culinaris, LCA) in mature absorptive cells of duodenum and jejunum of fasted rats. PSA and LCA are mannose-, glucose-, and N-acetyl-glucosamine-recognizing lectins that bind with high affinity to fucosylated core regions of N-glycosidically linked glycans. The binding reactions were cytochemically demonstrated in a pre-embedment incubation system using peroxidase-labeled lectins. Both pea and lentil lectins bound with constituents of nuclear envelope and endoplasmic reticulum, cisternae of the Golgi apparatus, several Golgi-associated vesicles, lysosomes, and portions of the plasma membrane. PSA and LCA label was non-homogeneous in the endoplasmic reticulum; in the Golgi apparatus the reactions were most intense in the cis and medial cisternae of the stacks. For inhibition of the intense reactions apparent in the Golgi apparatus, in lysosomes, and at the plasma membrane, considerably higher concentrations of competitive sugars were necessary than for abolition of the endoplasmic reticulum label. This indicates that endoplasmic reticulum glycoconjugates bind at low affinities with pea and lentil lectins, and that high-affinity PSA/LCA-binding glycoconjugates, which may correspond to corefucosylated N-linked glycans, predominate in cis and medial Golgi cisternae, lysosomes, and at the plasma membrane.
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PMID:Affinity cytochemical differentiation of glycoconjugates of small intestinal absorptive cells using Pisum sativum and Lens culinaris lectins. 254 94

Receptors of 12 lectins in 25 cases of human hepatocellular carcinomas (HCC) were histochemically investigated by avidin-biotin-peroxidase complex (ABC) method. Liver tissues of five cirrhotic patients and five normal subjects were used as controls. SJA receptor was absent both in HCC and controls, while LCA and PSA receptors were present in all tissues studied here. Receptors of DBA, PHA, PNA, UEAI and SBA which did not bind to normal, cirrhotic and pericarcinomatous liver tissues had the positive rates of 4%, 44%, 16%, 4% and 12% in HCC, respectively. Four lectins which strongly bound to the non-cancer liver tissues had their receptors in 96% (ConA, WGA, RCAI) and 36% (BSAI) of HCC. The pretreatment of tissue sections with neuraminidase abolished most of WGA receptors and exposed some PNA binding sites. There were many differences in lectin distribution between HCC and noncancer liver tissues. The changes of glycoconjugates in HCC were discussed.
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PMID:Changes of glycoconjugates in human hepatocellular carcinoma. 254 84

The tissues consisted of adenocarcinoma of the prostate were examined by immunohistochemical study with monoclonal antibody (43-21-1-1) against gamma-seminoprotein (gamma Sm)2). The degree of staining regarding any correlation with the histological grade was evaluated. The prostatic tissues were obtained by transurethral resection or by fine needle biopsy from untreated 38 patients. The avidin-biotin peroxidase complex technique was used to stain on 3 microns-sections of 10% formalin fixed, paraffin embedded tissue. In addition, immunohistochemical staining with the commercialized antibodies to prostate-specific antigen (PSA; polyclonal, DAKO) and to prostatic acid phosphatase (PAP; polyclonal, DAKO) was done simultaneously for a comparative study. The degree of immunoperoxidase stain was classified into two categories, namely location and pattern, and was graded from 0 to 3, respectively. The product of the degree of location and the degree of pattern was noted as the total score. The mean of score was calculated in each histological grade. Then the means of total scores were compared and evaluated as having any statistical difference by Student's t test among 3 histological grades as well as among 3 primary antibodies used in this study. When the monoclonal antibody to gamma-Sm was used for immunoperoxidase staining, the means of total scores and the rates of negative reactions (% Negative) in 3 histological grades were 6.8 +/- 1.8 (M +/- SD) and 0% in well (N = 9), 4.4 +/- 2.4 and 14% in moderately (N = 22), and 1.8 +/- 2.3 and 54% in poorly differentiated lesions (N = 11), respectively. There were statistically significant differences (P < 0.05) among 3 histological grades.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:[Immunohistochemical study of monoclonal antibody against gamma-seminoprotein in the prostatic tissues. A significant correlation between the degree of staining and the histological grade of adenocarcinoma of the prostate]. 768 1

The distribution of six lectin receptors, WGA, RCA-1, LCA, PSA, PNA and SBA in 111 human gliomas, 8 human normal brain tissues and 11 reactive hyperplasia of astrocytes was observed by means of avidin-biotin-peroxidase technique. Their grays were also quantified with the image analysis instrument. The results showed that WGA and RCA-1 might be used as markers for distinguishing well-differentiated astrocytomas from the reactive hyperplasia of astrocytes especially the reactivity of astrocytes had a specific feature with RCA-1. The difference in quantities of WGA, RCA-1, LCA, PSA receptors between astrocytomas, ependymomas and oligodendrogliomas, medulloblastomas might conduce to the diagnosis and classification. For astrocytomas, it was also showed that a quantity of LCA and PSA receptors was correlated with the degree of cell differentiation. Therefore, they can be used as valuable markers of the differentiation of astrocytomas.
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PMID:Labeling and quantitative analysis of six lectin receptors of intracranial gliomas. 771 37

The staining patterns of 24 biotinylated lectins were analyzed in serial sections of the mandible of 13- to 21-day-old rat embryos by means of the avidin-biotin-peroxidase method. A ubiquitous distribution of binding sites was demonstrated after incubation with Con A (Canavalia ensiformis), DSL (Datura stramonium; except bone matrix), and WGA (Triticum vulgare). ECL (Erythrina cristagalli), GSL I (Griffonia simplicifolia), SJA (Saphora japonica), VVL (Vicia villosa), DBA (Dolichus biflorus), UEA I (Ulex europeus), and LTA (Lotus tetragonobolus) were constantly negative. In early stages of development, GSL II (Griffonia simplicifolia II) was a selective marker of prechondral blastema. In contrast, PNA (Arachis hypogaea) did not stain condensing mesenchyme. During chondrogenesis of Meckels's cartilage a general decrease of lectin binding was observed. Mature cartilage matrix was constantly negative. Chondrocytes were marked by the lectins PSA (Pisum sativum), WGA, PHA-E, and PHA-L (Phaseolus vulgaris E and L). A strong GSL II binding was restricted to the mesial-superior region of the perichondrium. In later stages, several lectins revealed significant differences between preskeletal ("central") areas and the remaining ("peripheral") mesenchyme. A clear binding reaction was noted in central regions by applying LEA (Lycopersicon esculentum) and STL (Solanum tuberosum), while the peripheral tissue was only faintly stained. Developing bone was specifically marked by succinylated WGA (sWGA). The lectins LCA (Lens culinaris) and RCA (Ricinus communis) bound to fibers and extracellular matrix of the connective tissue. Jacalin (Artocarpus integrifolia) and SBA (Glycine max) binding sites were found in macrophages. Affinity of VAA (Viscum album) increased parallel with maturation of endothelial cells. Specific lectin-binding patterns revealed no correlation with the distribution of glycosaminoglycans. The results demonstrate a general reduction of oligosaccharide structures during development of Meckel's cartilage. From our observations we conclude that intralaminar glucose and/or mannose sequences as well as terminal sialic acid molecules are ubiquitously distributed, while terminal alpha-fucose was constantly negative. Lectin-binding patterns of macrophages may reflect the presence of specifically linked terminal galactose. Our findings indicate that oligosaccharides terminating in N-acetylglucosamine are bone-specific. The significance of the restricted staining of the perichondrium by GSL II remains to be elucidated.
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PMID:Characterization of glycoconjugate expression during development of Meckel's cartilage in the rat. 771 33


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