Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0019621 (Langerhans cell histiocytosis)
 3,250 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Concanavalin A (Con A) and agglutinins from the pea (PSA), lentil (LCH), and fava bean (VFA) constitute a group of D-mannose/D-glucose binding legume lectins. In addition to their sugar binding specificity, these lectins also contain sites that bind hydrophobic ligands. The present study explores a class of nonpolar binding sites reportedly present adjacent to the carbohydrate binding site in PSA, LCH, and VFA. A series of 2-O- and 3-O-substituted nitrobenzoyl and nitrobenzyl derivatives of methyl alpha-D-glucopyranoside and methyl alpha-D-mannopyranoside were synthesized. Evaluation of their binding to Con A, PSA, LCH, and VFA was carried out by the technique of hapten inhibition of precipitation reaction. The hapten inhibition assay results reveal that the presence of a methyl or methylene group at the O-2 or O-3 position of the sugar is essential for hydrophobic interaction with PSA, LCH, and VFA. The substitution of methyl by nitrobenzyl leads to enhanced binding (1.7-16.7 times for the 2-O-substituted compounds and 7.9-40.5 times for the 3-O-substituted compounds) with the m-nitrobenzyl group contributing to maximum binding. A hydrophobic interaction is also involved between Con A and 2-O-nitrobenzyl derivatives, resulting in enhanced binding, but the corresponding 3-O-isomers bind poorly due probably to steric reasons. These results may be rationalized on the basis of the recently published X-ray data of Con A and VFA. The nitrobenzyl derivatives, after transformation to their azido analogs, have potential applications in the photoaffinity labeling of these lectins.
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PMID:Synthesis of high-affinity, hydrophobic monosaccharide derivatives and study of their interaction with concanavalin A, the pea, the lentil, and fava bean lectins. 144 65

Seven tetramethylrhodamine B isothiocyanate- (TRITC) labeled lectins: lens culinaris (LCH), ulex europeus-1 (UEA-1), lycopersicon esculentum (LEA), wheat germ agglutinin (WGA), dolichos biflorus (DBA), soybean agglutinin (SBA) and erythrina cristagalli (ECA) were applied on cultured human megakaryocytes (Megs) detected by immunofluorescence. All stages of Megs (from lymphocyte-like Megs to mature Megs) and platelets were labeled by LCH, LEA, UEA-1 and WGA. ECA binds to platelets but only to some Megs. DBA did not bind to platelets but did bind to some Megs, irrespective of stage. SBA binds to all stages of Megs, but did not bind to platelets. These results indicate the presence of mannose, glucose (LCH), sialic acid (WGA), and glucosamine (UEA-1, LEA, WGA) on the surface of all cells of the Meg lineage, a variable presence of galactosamine (DBA, SBA, ECA), and a discrepancy in the presence of some galactosamine compounds between platelets and Megs (DBA, SBA).
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PMID:Carbohydrate composition of human megakaryocyte membranes in culture: identification using binding of seven lectins. 206 23

FITC-Con A staining as a rapid diagnostic method for tumor cells was applied to the tumors smeared on glass slide and section specimens to evaluate the reactivity with FITC-Con A. Good staining results were obtained in smear specimens with clear fluorescence on the membrane of tumor cells. Con A and LCH lectins bound well with tumor cells to produce strong fluorescence in comparison with PEA and DBA. It indicates that tumor cells expressed dominantly the receptors of alpha-D-glucose and alpha-D-mannose sugar chain on the membrane of tumor cells. From these results it was concluded that FITC-Con A staining method applied to smear specimens is more advantageous in the rapidity and the simplicity for tumor cell diagnosis than section specimen method.
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PMID:[Rapid diagnosis of experimental tumor by FITC-Con A lectin--a comparative study of smear and section specimens]. 245 71

Profiles of concanavalin A (Con A) and lentil agglutinin (LCH) affinity immunoelectrophoresis were compared for serum alpha-fetoprotein (AFP) from patients with yolk sac tumors and carcinomas of the gastrointestinal tract, in order to find some correlations between peaks of AFP subfractions detectable by two different lectins, and to investigate whether or not it is possible to prove that the binding of AFP to LCH is weakened to some extent if a fucosylated sugar chain has, in addition, a bisect N-acetylglucosamine (GlcNAc) attached to the beta-linked mannose. The results obtained with our improved techniques tend to indicate that a Con A-reactive AFP subfraction (peak a) corresponds to an LCH strongly reactive AFP (peak A), while a Con A-nonreactive AFP (peak b) corresponds to an LCH weakly reactive AFP (peak B). the authors consider the present data sufficient to support the above explanation.
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PMID:Analysis of lectin affinity immunoelectrophoretic profiles of serum alpha-fetoprotein from patients with yolk sac tumors and carcinomas of the gastrointestinal tract: correlations with molecular structures. 248 Jun 30

The binding of 10 different lectins to the surface of microfilariae of Wuchereria bancrofti has been investigated. Wheat germ agglutinin (WGA) and Helix pomatia lectin (HPA) bound specifically to the sheathed microfilariae indicating the presence of N-acetyl-D-glucosamine and N-acetyl-D-galactosamine respectively on the surface. Exsheathed microfilariae did not react with any of the lectins. Treatment of sheathed microfilariae with proteases resulted in increased binding of WGA and HPA. Such treated microfilariae showed a weak binding of Concanavalin A (Con A), and lectins of lentil (LCH) and of Limulus polyphemus (LPA). Sheathed microfilariae incubated with sera of people living in endemic zones of filariasis but with no apparent evidence of infection (endemic normals), or with sera of chronic elephantiasis patients, or with their respective gamma globulin fractions, bound Con A and LCH. These lectins bound weakly to exsheathed microfilariae under the same conditions. Binding was due to the mannose components of the specific immunoglobulins of the sera which coated the microfilariae. However, microfilariae when incubated with sera or their globulin fractions from non-endemic normals (NEN), or from microfilarial carriers, did not bind Con A and LCH, suggesting that specific immunoglobulins were neither present in NEN sera nor in significant amounts in sera of microfilarial carriers.
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PMID:Lectin-binding characteristics of Wuchereria bancrofti microfilariae. 288 37

The carbohydrate compounds of the mucus of flask cells in the kidney of claw-frogs (Xenopus laevis) were analysed through lectin binding studies. After removing epoxy resin semithin sections were incubated with 7 lectins (WGA, RCA I, PNA, LCH, UEA, LPA) marked by horseradish peroxidase and 2 unmarked lectins (VAA, Con A). The glycosaminoglycans in the canalicular lumen of flask cells showed a strong reaction with WGA and RCA, whereas the binding of PHA, Con A, and LCH was weaker. No reaction was observed with PNA, UEA, LPA, and VAA. The mucus of the flask cells seems to be rich in N-acetyl-glycosamine and -galactosamine. It contains also mannose, glucose, and galactose, but seems to have no fucose or N-acetyl-sialic acid residues.
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PMID:Lectin binding on carbohydrate compounds of the flask cells in the claw-frog kidney. 314 43

The carbohydrate moieties of microfilariae (Mf) and infective larvae (L3) have been investigated by lectin-binding technique. Mf derived from three sources, namely, uteri (in utero), released in vitro from adults and from blood of rodents infected with Litomosoides carinii were examined by using fluoresceinated lectins. Wheat germ agglutinin (WGA) bound to these Mf and the binding was inhibited by N-acetyl glucosamine. In addition to WGA, Concanavalin A (Con A) and lentil lectin (LCH) bound to in vitro-released and in utero-derived Mf showing the presence of mannose moieties on their surface. In utero-derived Mf also showed binding with the agglutinins of Limulus polyphemus (LPA), peanut (PNA), Ricinus communis (RCA), Helix pomatia (HPA), Soyabean (SBA) and Dolichos biflorus (DBA) but not to that of Ulex europaeus (UEA) indicating the presence of additional carbohydrate molecules like sialic acid, galactose and N-acetyl galactosamine on their sheath. None of the lectins bound to the cuticle of exsheathed Mf. Treatment of blood-derived and in vitro-released Mf with certain proteases exposed additional binding sites for SBA, HPA, Con A and LCH. In case of L3, only PNA bound to the larvae isolated from infective mites Bdellonyssus bacoti, and the binding was inhibited by D-galactose. No such binding of the lectins was seen to the larvae that migrated to the pleural cavity of jirds indicating that there is considerable change on the parasite surface during their migration in the vertebrate host. Sheathed Mf and mite-derived L3 when incubated with immune rat sera, bind Con A and LCH lectins possibly due to the mannose components of the specific immunoglobulins that coat onto the Mf and L3.
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PMID:Litomosoides carinii: characterization of surface carbohydrates of microfilariae and infective larvae. 360 35

Binding patterns of fluorescein isothiocyanate (FITC)- and gold-conjugated lectins to extracellularly melanized sheathed and exsheathed microfilariae of subperiodic Brugia malayi, isolated from and in situ in the abdominal hemocoel of Anopheles quadrimaculatus 72-hr postinfection, were examined. Five FITC-conjugated lectins [Helix pomatia agglutinin (HPA), Arachis hypogaea (peanut agglutinin-PNA), Triticum vulgaris (wheat germ agglutinin-WGA), Lens culinaris (lentil-LCH), and Concanavalin A (Con A)] with specificities for different carbohydrate moieties were tested for binding to isolated melanized microfilariae and observed with transmitted light and fluorescence microscopy. All five FITC-lectins bound strongly to the acellular material accompanying the melanin deposits on the surface of isolated melanized microfilariae. Significant inhibition of FITC-lectin binding occurred when lectins were preincubated with their complementary carbohydrates before testing. H. pomatia agglutinin binding was totally inhibited by N-acetyl-D-glucosamine and N-acetyl-D-galactosamine. Other lectins were partially inhibited, such as PNA by galactose and lactose; WGA by N-acetylneuraminic acid; LCH by N-acetyl-D-glucosamine, mannose, glucose, and methyl alpha-D-mannopyranoside; and Con A by mannose and methyl alpha-D-mannopyranoside. Three gold-conjugated lectins (HPA, PNA, and Con A), examined by using transmission electron microscopy, bound to the outer surface of the acellular material associated with the melanin deposits on isolated melanized microfilarial sheaths and melanized microfilariae and to the remnants of lysed hemocytes found in the proximity of the melanized deposits. Con A in the presence of gold-labeled horseradish peroxidase, examined by using transmission electron microscopy, showed random binding within the melanized capsule formed around the microfilarial sheath in situ. These results indicate that the acellular material accompanying melanin deposits on melanized microfilarial sheaths and sheathed and exsheathed microfilariae contain several glycoconjugates with exposed carbohydrate moieties and are possibly glycoproteins. These glycoproteins could be the by-products of the activation of the prophenoloxidase by the microfilariae.
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PMID:Lectin binding to extracellularly melanized microfilariae of Brugia malayi from the hemocoel of Anopheles quadrimaculatus. 856 82

The diagnosis of pulmonary Langerhans cell histiocytosis might be refined by demonstrating reliability of a new cell marker, i.e., Langerin (CD207), used on bronchoalveolar lavage fluid. For this purpose, we collected material from patients with this disease and also with sarcoidosis and idiopathic pulmonary fibrosis as controls. In addition to the immunocytochemical detection of Langerin, we examined the expression profiles of CD1a and the macrophage tandem-repeat mannose receptor (CD206). To test accessibility of Langerin, a C-type lectin, for mannosides, we employed reverse lectin histochemistry using mannose-containing neoglycoproteins. The analysis revealed a significantly increased percentage of CD1a- and Langerin-positive cells in pulmonary Langerhans cell histiocytosis in comparison with both other studied diseases. No expression of the 175-kDa mannose-binding lectin (CD206) in Langerhans cells was observed. Evidently, binding sites on the cells were not accessible for the mannose-containing neoglycoligand. These results provide evidence for the usefulness of Langerin-directed immuno- and glycohistochemical monitoring of bronchoalveolar lavage fluid in the diagnosis of pulmonary Langerhans cell histiocytosis.
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PMID:Diagnostic relevance of Langerin detection in cells from bronchoalveolar lavage of patients with pulmonary Langerhans cell histiocytosis, sarcoidosis and idiopathic pulmonary fibrosis. 1472 67

A 28-year-old man with a history of Hodgkin lymphoma that was intensely [F-18]fluoro-2-deoxy-D-glucose-avid at diagnosis had achieved complete remission following appropriate therapy. On surveillance positron emission tomography/computed tomography (CT), new, intensely [F-18]fluoro-2-deoxy-D-glucose-avid lesions (lytic on CT) were seen within the vertebral body of C7, left scapula, and right glenoid. The findings of a biopsy revealed these lesions to be Langerhans cell histiocytosis. Langerhans cell histiocytosis arising in the context of lymphoma is a well-documented phenomenon, and its appearance on positron emission tomography/CT cannot be conclusively distinguished from lymphoma recurrence. This manuscript emphasizes the necessity of biopsy to ensure correct diagnosis and subsequent correct therapy.
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PMID:False-positive PET/CT for lymphoma recurrence secondary to Langerhans cell histiocytosis. 2171 31


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