Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.11.1.7 (peroxidase)
 65,474 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In the present study carbohydrate residues in taste buds (TBs) and adjacent epithelial formations of a teleostean fish, a frog and the rabbit were detected by means of lectin histochemistry. Biotinylated lectins from Pisum sativum (PSA), Arachis hypogaea (PNA), Dolichos biflorus (DBA), Triticum vulgaris (WGA and succinylated WGA), Glycine max (SBA) and Ulex europaeus (UEA I) have been applied. The lectins were bound to an avidin-biotin-peroxidase-complex (ABC) and visualized by diaminobenzidine/H2O2. Most intensive reactivity was observed at the taste disc cells of the frog with DBA, S-WGA and SBA. PNA did not bind to the TBs of any of the animals tested. As shown in SBA preparations, sialic acid is present in a nonacylated and an acylated form in the mucosa of the frog's tongue. The TBs of the fish possess all the sugars we looked for except for the disaccharide D-galactose-(1-3)-beta-D-N-acetyl-galactosamine (Gal/GalNAc) and sialic acid. The TBs of the rabbit contain GalNAc, as detected with DBA, but not with SBA; and fucose (Fuc), mannose (Man) and N-acetyl-glucosamine (GlcNAc). As revealed by preincubation of the tissue sections with neuraminidase in TB cells of the rabbit, sialic acid masks Gal/GalNAc and GalNAc. These lectin-binding characteristics show that in the TBs of some selected representatives which belong to different vertebrate classes exist different mucous substances. These substances possess different binding characteristics to specific sugars, and this is possibly of particular interest to chemoreception phenomena.
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PMID:Lectin histochemistry on mucous substances of the taste buds and adjacent epithelia of different vertebrates. 325 18

Formalin fixed, paraffin embedded tissue from 100 consecutive cases of breast carcinoma were studied for binding with Helix pomatia (HPA) and Ulex Europeus (UEA1) lectins. Serial sections were pretreated with trypsin or neuraminidase to determine the effect of these enzymes on lectin binding. The lectins were visualized by the peroxidase antiperoxidase technique and the cell staining proportion assessed in a semi-quantitative manner under the light microscope. Correlating staining with prognostic factors and patient follow-up details showed that UEA1 related to disease-free interval and survival, and HPA to lymph node stage, time to loco regional recurrence and to survival. Relationships with both lectins were abolished by pretreatment with neuraminidase. The study demonstrates that a simple assessment of lectin binding can provide prognostic information in breast cancer. This may be useful particularly when conservational surgical practice restricts the amount of nodal tissue for staging.
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PMID:Helix pomatia and Ulex europeus lectin binding in human breast carcinoma. 330 30

The lectin-binding patterns of primary malignant melanoma, nevocellular nevus, and Spitz nevus were studied on formalin-fixed, paraffin-embedded sections using a series of biotinylated lectins--concanavalin A (ConA), Ricinus communis agglutinin-1 (RCA1), dolichos biflorus agglutinin (DBA), soybean agglutinin (SBA), maclura pomifera agglutinin (MPA), peanut agglutinin (PNA), wheat germ agglutinin (WGA), and Ulex europeus agglutinin-1(UEA1)--and employing the avidin-biotin-peroxidase complex method. In nevocellular and Spitz nevi, all of the nevus cells were positively stained with ConA and RCA1. No positive staining was observed, however, with the other lectins and no change in binding patterns occurred following neuraminidase pretreatment. In malignant melanoma, all of the melanoma cells were positively stained with ConA and RCA1, and some were also stained with MPA, PNA, and WGA. In addition, DBA, SBA, MPA, PNA, and WGA labeled all of the melanoma cells after neuraminidase pretreatment. No positive staining was observed with UEA1 despite neuraminidase pretreatment. The present results showed that malignant melanoma and nevocellular and Spitz nevi have different lectin-binding patterns and different responses to neuraminidase pretreatment. We, therefore, believe that the lectin staining on paraffin-embedded sections can be a useful probe for the differentiation of these diseases.
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PMID:Differing lectin-binding patterns of malignant melanoma and nevocellular and Spitz nevi. 331 32

Expression of glycoconjugates during transfilter-induced differentiation of metanephric mesenchyme was studied by using fluorochrome- and peroxidase-coupled lectins. All cells in the uninduced metanephric mesenchyme expressed mannose, beta-D-galactose (beta-Gal), N-acetylglucosamine (GlucNAc), and terminal sialic acids. Additionally, solitary cells showed terminal alpha-D-galactose alpha-D-galactose (alpha-Gal) typical of mouse endothelial cells. During culture, undifferentiated mesenchymal cells seemed to disappear from induced explants, and many of the stromal cells between the evolving tubules presented terminal alpha-Gal residues. Similar positivity could be revealed in monolayer cultures of induced mesenchymes. A number of tubules in induced explants displayed alpha-L-fucosyl (Fuc) residues, characteristic of mature proximal tubules. Some terminal Ga1NAc residues, recognized only by Dolichos biflorus agglutinin, emerged in a few tubular cells after prolonged culture. The early tubules and glomerular bodies displayed a basement membrane presenting both terminal Ga1-(beta 1-3)-Ga1NAc and Ga1NAc residues. These positivities disappeared later from many tubular structures and glomerular bodies but persisted in tubules expressing proximal tubular differentiation. The glomerular bodies displayed only one cell type, reminiscent of maturing podocytes, presenting terminal Ga1-(beta 1-3)-Ga1NAc and Ga1NAc residues. Later these saccharide residues became covered by sialylation, as they could then be revealed only after treatment with neuraminidase. The results indicate that the segment-specific expression of saccharide residues during differentiation of nephron in vitro resembles the sequence seen in vivo. This study also suggests that the basement membranes surrounding the nephron show a stepwise, segment-specific maturation. Despite the presence of endothelial cells in the metanephric explants, only avascular glomeruli evolved in this differentiation model.
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PMID:Expression of cellular glycoconjugates in transfilter-induced metanephric mesenchyme. 335 61

The three Hodgkin disease-derived cell lines L 428, L 540, and L 591 were characterized in their carbohydrate epitope composition by a panel of lectins. Nine other human cell lines were tested in comparison to the Hodgkin (H) and Sternberg Reed (SR) cells: promyelocytic (HL 60), lymphoblastoid, myeloma, histiocytic lymphoma (U 937), and other non-Hodgkin lymphoma cell lines. Twenty-four different fluoresceinated lectins bound to the Hodgkin and other cell lines in different percentages of positive cells and with varying intensities. Lotus lectin and a monoclonal anti-Lewis blood group X antibody showed very similar binding patterns (L 428, L 540, HL 60, U 937). Soybean agglutinin stained only L 428 and L 540, although nearly all were positive after neuraminidase treatment. Cell lysis of the three H cell lines resulted in a very similar electrophoretic mobility pattern of proteins. In addition, staining of transblotted glycoproteins with biotinylated concanavalin A by avidin peroxidase reaction revealed corresponding bands. Differences were seen with Lotus staining. In summary, the origin of H cells is still unknown, but there is obviously some relationship in the glycoconjugate profile to the myelohistiocytic lineage.
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PMID:Lectin binding pattern of Hodgkin disease-derived cell lines in comparison to other human cell lines. 348 48

Uterine secretions are of fundamental importance in reproductive processes. Uterine activity is related to the hormonal status of the animal, and peroxidase is a major estrogen-regulated glycoprotein in the uterine fluid. Estrogen-induced peroxidase (EIP) can be separated into several isoelectric variants. SDS-PAGE electrophoresis suggested that EIP has a molecular weight of approximately 70kd. The observed pattern of EIP isoforms appears to result from differential glycosylation of a single protein species because neuraminidase treatment resulted in a gradual shift of EIP to the more basic isoelectric variants prior to abolishing enzymatic activity. Antibody raised against one of the major isoelectric variants of EIP demonstrated uterine epithelial cells by immunofluorescence indicating an epithelial cell localization for the enzyme. Radioactive bands comigrating with major EIP isozymes were detected in uterine fluid by in vivo labeling after estrogen treatment. The results of these studies support the hypothesis that EIP is a major estrogen-regulated secretory protein of the uterine epithelium.
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PMID:Peroxidases induced in rat uterus by estrogen administration. I. Synthesis, secretion and immunofluorescent demonstration of fluid enzymes. 353 26

Lectin-histochemical studies were performed on formalin-fixed, paraffin-embedded tissues from ten mammalian species to demonstrate the pattern of carbohydrate residues in vascular endothelium. Ten different biotinylated lectins were used as probes and avidin-biotin-peroxidase complex (ABC) was used as visualant. Ricinus communis agglutinin-I (RCA-I) and wheat germ agglutinin (WGA) stained vascular endothelium in all species. Peanut agglutinin (PNA) stained vascular endothelium in all species only after preincubation with neuraminidase. Bandeirea simplicifolia agglutinin-I (BS-I) stained vascular endothelium in all species but human, while Ulex europeus agglutinin-I (UEA-I) stained only human endothelium. Individual differences in staining of human vascular endothelium were noted with BS-I and succinylated-WGA (SWGA). Similarly, individual differences in staining of animal vascular endothelium were noted with soybean agglutinin (SBA) after preincubation with neuraminidase. Finally, Concanavalia ensiformis agglutinin (Con A), Dolichos biflorus agglutinin (DBA) and Lens culinaris agglutinin (LCA) did not stain vascular endothelium in any of the species studied.
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PMID:Lectin histochemistry of mammalian endothelium. 361 Jun 72

The binding to morphologically normal human retina of eleven biotin- or peroxidase-coupled lectins with different carbohydrate specificities was studied. Eight formalin-fixed and paraffin-embedded eyes were examined. Photoreceptor cells bound Lens culinaris (LCA), wheat germ (WGA), peanut (PNA) and Ricinus communis (RCAI) agglutinins, and concanavalin A (ConA). The outer segment region was labeled more strongly that the inner segment region, and PNA labeled only cones. All these lectins except PNA bound to both plexiform layers, and all but PNA and RCAI to the nuclear layers. Pretreatment with neuraminidase to remove sialic acid resulted in increased binding of RCAI and PNA, which now labeled both rods and cones, and in decreased binding of WGA. Bandeiraea simplicifolia (BSAI), Dolichos biflorus (DBA), soybean (SBA), Ulex europaeus (UEAI), and Lotus tetragonolobus (LTA) agglutinins, as well as pokeweek mitogen (PWM) reacted only with retinal vascular endothelial cells, which were also labeled with the other lectins. The results indicate that alpha-mannose, alpha-glucose, beta-galactose, N-acetyl-D-glucosamine and N-acetylneuraminic acid are present in glycoconjugates of human neuroretina.
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PMID:A lectin cytochemical study of glycoconjugates in the human retina. 362 2

We examined the glycoprotein composition of intestinal goblet cells in jejunal and colonic biopsies obtained from pigs on different diets. Paraffin sections were stained both chemically and with the following horseradish-peroxidase conjugated lectins: Canavalia ensiformis (Con-A), Limulus polyphemus (LPA), Lotus tetragonolobus (LTA), Arachis hypogaea (PNA), Ricinus communis (RCA1), Glycine max (SBA) and Triticum vulgaris (WGA). Using chemical staining procedures, only small quantitative differences were noted between the two organs. With respect to lectin staining, the mucus of the jejunum was characterized by the absence of Con-A binding sites, and colonic mucus consistently exhibited an absence of SBA affinity. After dietary modifications, O-acetyl sialic acid reactivity was lowered in the jejunum but was enhanced in the colon. In the jejunum, the glycoproteins became neuraminidase susceptible, whereas the colon became characterized by the absence of neutral mucins. The affinity for the tested lectins after the different diets was variable, but the most striking effects were observed after the fibreless diet (milk alone). Our data suggest the existence of marked regional variations in goblet-cell mucus and indicate significant differences between the glycoprotein components of the jejunal and colonic mucosa. Furthermore, the biosynthesis of mucins in both regions was altered by even only short-term feeding modifications.
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PMID:Histochemical characterization of glycoproteins present in jejunal and colonic goblet cells of pigs on different diets. A biopsy study using chemical methods and peroxidase-labelled lectins. 362

In the secretory epithelium of the chicken mandibular gland, glycoconjugates have been studied by means of histochemical methods of light and electron microscopy. In light microscopy, a series of histochemical procedures have been employed which included lectin--peroxidase--diaminobenzidine methods and a digestion technique with neuraminidase or alpha-amylase. In electron microscopy, a battery of methods were used that corresponded to those employed in light microscopy. In the secretory cells of the chicken mandibular gland, vicinal diol- and sulphate-containing glycoconjugates with sialic acid, alpha-D-mannose, alpha-D-glucose and beta-D-galactose residues were visualized and the possible histophysiological significances of such glycoconjugates were discussed with special reference to the functions of the salivary gland.
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PMID:Glycoconjugates in the secretory epithelium of the chicken mandibular gland. 373 63


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