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11 Ergebnisse
Albumin and Ricinus communis agglutinin decrease endothelial permeability via interactions with matrix.
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We studied the effects of albumin and the lectin Ricinus communis agglutinin (RCA) on hydraulic conductivity (Lp) of bovine pulmonary microvascular endothelial cell monolayers (BPMVEC) because of the evidence that albumin and RCA can interfere with transendothelial albumin permeability
Characteristics of albumin binding to opossum kidney cells and identification of potential receptors.
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Albumin re-absorption in the kidney proximal tubule may be pathophysiological in disease. Opossum kidney (OK) cell monolayers were used to investigate the characteristics of [125I]-labelled albumin binding at 4 degrees C. Two binding sites were identified, one with high affinity (KD 154.8 +/-7 mg/l)
Lectin binding to gp60 decreases specific albumin binding and transport in pulmonary artery endothelial monolayers.
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The effect of albumin binding to cultured bovine pulmonary artery endothelial cell (BPAEC) monolayers on the transendothelial flux of 125I-labelled bovine serum albumin (BSA) was examined to determine its possible role on albumin transcytosis. The transport of 125I-BSA tracer across BPAEC grown on
Ulex europaeus 1 lectin targets microspheres to mouse Peyer's patch M-cells in vivo.
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The interaction of latex microspheres with mouse Peyer's patch membranous M-cells was studied in a mouse gut loop model after the microspheres were coated with a variety of agents. Carboxylated microspheres (diameter 0.5 micron) were covalently coated with lectins Ulex europaeus 1, Concanavalin A,
Studies on lectins. XL. O-glycosyl derivatives of Spheron in affinity chromatography of lectins.
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Free monosaccharides can be used for direct glycosylation of Spheron, a spherical macroporous hydroxyalkyl methacrylate-ethylene dimethacrylate copolymer, in a reaction that proceeds at room temperature in dioxane medium under catalysis of dry HCl or BF3. Derivatives of L-fucose, D-galactose,
Lectins at Interfaces-An Atomic Force Microscopy and Multi-Parameter-Surface Plasmon Resonance Study.
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Lectins are a diverse class of carbohydrate binding proteins with pivotal roles in cell communication and signaling in many (patho)physiologic processes in the human body, making them promising targets in drug development, for instance, in cancer or infectious diseases. Other applications of lectins
Lectin (UEA-1) reaction of capillary endothelium with reference to permeability in autopsied cases of cerebral infarction.
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The relationship between endothelial reactivity to Ulex europaeus agglutinin-1 (UEA-1) and the permeability of the vascular wall in human autopsied cases of cerebral infarction was studied. Sections from the cerebral cortex were reacted with horseradish peroxidase UEA-1 to demonstrate the surface
Mitogenic lectins bind to the antigen receptor on human lymphocytes.
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The specificity of interactions between mitogenic and non-mitogenic lectins and disulfide-linked cell surface receptors on human lymphocytes was explored. Lysates (Nonidet-P40) of surface-radioiodinated tonsil lymphocytes and T lymphoblastoid cells (HPB-ALL) were absorbed with lectin-agarose
Recognition of the blood group H type 2 trisaccharide epitope by 28 monoclonal antibodies and three lectins.
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The patterns of cross-reaction of 30 monoclonal antibodies and three lectins were determined by ELISA with 21 ABH, Ii or Lewis related synthetic oligosaccharides coupled to bovine serum albumin. At least seven main groups of cross-reactive patterns were identified among the antibodies, plus several
Lectin cytochemistry of the lacrimal sac epithelium in experimental dacryocystitis.
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OBJECTIVE
To study the glycoconjugates in the lacrimal sac epithelium of Japanese white rabbits with experimentally induced chronic dacryocystitis.
METHODS
Chronic dacryocystitis was induced by a subcutaneous injection of albumin followed by an injection of Staphylococcus aureus into the lacrimal
Comparative study of blood group-recognizing lectins toward ABO blood group antigens on neoglycoproteins, glycoproteins and complex-type oligosaccharides.
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Binding specificities of ABO blood group-recognizing lectins toward blood group antigens on neoglycoproteins, glycoproteins and complex-type oligosaccharides were studied by lectin-blotting analysis, enzyme linked immunosorbent assay and lectin-conjugated agarose column chromatography. Human serum
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