The present study was carried out to investigate the glycoconjugate properties of the nasal mucosa in the rat after inhalation of formaldehyde. Sprague-Dawley male rats were inhalated 30 ppm formaldehyde for 3 times with 3 hours exposure. The olfactory and respiratory mucosa in the nasal mucosa were taken from the animals on 3, 6,9 days and 2, 3, 4, 5 weeks after inhalation of formaldehyde. The properties of glycoconjugate of the olfactory and respiratory mucosa were investigated using nine biotinylated lectins (PSA, UEA I, PHA-L, BSL I, PNA, MAL I, DBA, BSL II or sWGA). In experimental groups, the degenerative changes of the olfactory epithelium were observed until 3 weeks after inhalation of formaldehyde, but the respiratory epithelium was no change. In control group, the olfactory cells in the olfactory epithelium reacted with PSA, UEA I, PNA, DBA, BSL II, sWGA, and the supporting cells reacted with PSA, PHA-L, PNA, MAL I, DBA, BSL II, sWGA, and Bowman's glands reacted with all the lectins. In experimental groups, the olfactory cells reacted with UEA I, DBA, and the supporting cells reacted with PHA-L, MAL I, DBA, UEA I, and the positive reaction of Bowman's glands was increased. In control group, the goblet cells in the respiratory epithelium reacted with UEA I, MAL I, and the ciliated columnar cells reacted with PSA, UEA I, PHA-L, BSL I, DBA, BSL II, sWGA, and the septal nasal glands reacted with all the lectins except UEA I. In experimental groups, the goblet cells reacted with UEA I, MAL I and PNA. Conclusively, the olfactory mucosa was shown a lot of changes in the properties of glycoconjugates following inhalation of formaldehyde, but respiratory mucosa was shown feeble change. These results suggest that there were different sugar residues of glycoconjugate in the olfactory and respiratory mucosa following inhalation of formaldehyde, respectively.
Animals ; Formaldehyde ; Glycoconjugates ; Goblet Cells ; Humans ; Inhalation ; Lectins ; Male ; Nasal Mucosa ; Olfactory Mucosa ; Phytohemagglutinins ; Rats ; Respiratory Mucosa ; Wheat Germ Agglutinins

Lectins are glycoproteins that specifically bind carbohydrate structures and may participate in the biodefense mechanisms of fish. In this study, the binding of three lectins, Dolichos biflorus agglutinin (DBA), soybean agglutinin (SBA), Bandeiraea simplicifolia BS-1 (isolectin B4), Triticum vulgaris (WGA), Arachis hypogaea (PNA) and Ulex europaeus (UEA-I) were studied in the gill, liver, intestine, kidney, heart, and spleen of the flat fish Paralichthys olivaceus. DBA was detected in intestinal mucous cells, as well as in gill epithelial and mucous cells. It was weakly detected in renal tubule epithelial cells and in bile duct epithelial cells. The strong SBA staining was seen in the intestinal club cells, in bile duct epithelial cells and renal tubule epithelial cells. There were intense positive reactions for isolectin B4 in gill epithelial and mucous cells, and the strong isolectin B4 staining was seen in epithelial cells of the bile duct and intestine. The strong WGA staining was seen in the gill mucosal cells, sinusoid, renal tubule epithelial cells and mucosal cells of the intestine. UEA-I was detected in the gill epithelial and mucosal cells, bile duct epithelial cells and renal tubular epithelial cells. These results suggest that the six lectins examined were localized in the covering epithelia of the various organs of the flat fish and they may participate in the biodefense mechanism of the intra body surface in which is exposed to various antigens.
Animals ; Epithelial Cells/metabolism ; Flatfishes/*metabolism ; Histocytochemistry/veterinary ; Lectins/*metabolism ; Mucus/metabolism ; Peanut Agglutinin/metabolism ; Plant Lectins/metabolism ; Soybean Proteins/metabolism ; Wheat Germ Agglutinins/metabolism

In this study, wheat germ agglutinin (WGA), tomato lectin (TL) and asparagus pea lectin (AL) were covalently coupled to conventional poly lactic-co-glycolic acid (PLGA) nanoparticles using a carbodiimide method to take the bioadhesive properties. The influences of the amounts of activating agents and lectins, as well as the activating time and incubating time on the effect of lectin conjugating were investigated to optimize the preparation conditions. The mean diameters of the performed nanoparticles with or without lectin conjugation ranged from (140.7 +/- 5.7) nm to (245.6 +/- 18.3) nm. The yields of lectin conjugating and the lectin surface concentrations on nanoparticles were determined by Lowry's methods, and were calculated to be (18.97 +/- 2.9)% - (20.15 +/- 2.4)% and (9.46 +/- 1.45)--(10.05 +/- 1.19) microg x mg(-1), respectively. The in vitro bioadhesive activities of nanoparticles were evaluated by pig gastric mucin (PM) binding experiments. After incubation at room temperature for 60 min, the equilibria of binding between nanoparticles and PM reached. The percentages of the bulk PM which had interacted with different lectin-conjugated PLGA nanoparticles were 15.5%, 12.1% and 11.8%, respectively. The conjugation of lectin enhanced the interaction about 2.4 - 3.2 fold compared with that of the non-conjugated one. A mathematical model was used based on the Langmuir equation, and the rate constants of interaction (k) were calculated to be 2.373 x 10(-3), 1.536 x 10(-3) and 1.714 x 10(-3) (microg x min/mL)(-1), respectively. These interactions could be competitively inhibited by their corresponding sugars of lectins. The results suggested that lectin-conjugated PLGA nanoparticles greatly promoted the interaction with PM in vitro compared with the conventional PLGA nanoparticles, thus would improve the bioadhesion on gastrointestinal mucosa after oral administration resulting in a prolonged residence time in the gastrointestinal tract.
Adhesiveness ; Drug Carriers ; Drug Compounding ; Drug Delivery Systems ; Gastric Mucins ; metabolism ; Lactic Acid ; chemistry ; metabolism ; Nanoparticles ; Plant Lectins ; chemistry ; metabolism ; Polyglycolic Acid ; chemistry ; metabolism ; Protein Binding ; Wheat Germ Agglutinins ; chemistry ; metabolism

Viscum plants,the evergreen perennial parasitic shrubs or subshrubs,are mainly distributed in tropical and subtropical regions. There are about 70 Viscum species around the world,including 11 species and one variety in China. Mistletoe lectins are typeⅡ ribosome-inactivating proteins( RIPs) extracted from Viscum plants with anticancer and immunoregulatory activities. Many studies have focused on the mistletoe lectins isolated from V. album in Europe and V. album var. coloratum distributed in South Korea,respectively,and several preparations,such as Iscucin Ⓡ,were developed and clinically applied for cancer treatment. Although Viscum plants are widely distributed in China,only a few studies of mistletoe lectins have been reported. The recent progress of mistletoe lectins was reviewed from extraction,purification,quantitative/qualitative detection,molecular structure,pharmacological activities,toxicities,and clinical application,aiming at providing a reference for in-depth research and utilization of mistletoe lectins produced in China.
Humans ; Lectins ; Plant Extracts ; Plant Lectins ; Plant Proteins/genetics* ; Toxins, Biological ; Viscum

Histochemical patterns of lectin binding during development of the rat vomeronasal organ (VNO) were studied to determine whether glycoconjugates are differently expressed after birth. Three types of lectins, Dolichos biflorus agglutinin (DBA), wheat germ agglutinin (WGA), and Ulex europaeus agglutinin I (UEA-I), were studied histochemically in the rat VNO at various stages post-birth: postnatal days 1 and 7, the preweaning period (4 weeks after birth), and at sexual maturity (8 weeks after birth). The free border of the vomeronasal sensory epithelium was positive for both WGA and UEA-I in rats of all ages; whereas, VNO receptor cells and supporting cells were positive only for both WGA and UEA-I from 4 weeks after birth. DBA reactivity was detected in the free border but less so in receptor cells and supporting cells. WGA and UEA-I, but not DBA, showed similar patterns in various ages. In the Jacobson's gland, WGA, UEA-I and DBA were detected in some acini from 4 weeks after birth but not at postnatal days 1 or 7. Collectively, reactivity for three lectins, WGA, UEA-I and DBA, increased in receptor cells and gland acini during postnatal development, possibly contributing to the enhanced chemoreception in rats.
Animals ; Dolichos ; Epithelium ; Glycoconjugates ; Lectins ; Parturition ; Plant Lectins ; Rats ; Triticum ; Ulex ; Vomeronasal Organ

OBJECTIVE: Lectins are cell-agglutinating and sugar specific proteins or glycoproteins of non-immune origin that precipitate glycoconjugates having saccharides of appropriate complementarity. Because of these properties, plant lectins have been used to help characterize the carbohydrate moieties of glycoproteins in the zona pellucida (ZP) of several mammalian species including pigs. Treatment of oocytes with various lectins blocks sperm binding to the ZP in various mammalian species. This study was undertaken to examine the distribution of sugar residues in the ZP of pig oocytes matured in vitro and the ability of spermatozoa to bind to ZP and in vitro penetration in oocytes treated with fluorescein isothiocyanate (FITC)-labelled lectins. MATERIALS AND METHODS: The lectins of Banderiaea simplicifolia (BS-II, bind to beta-D-Nacetylglucosamine), Canavalin ensiformis (Con A, bind to alpha-D-Mannose), Lens culinaris (LCA, bind to alpha-D-Mannose), Ricinus communis (RCA-I, bind to beta-D-Galactose) and Ulex europaeus (UEA-I, bind to alpha-L-Fucose) were examined for spermatozoa penetration, binding capacity to ZP and distribution of lectins. RESULTS: The penetration rates were significantry (p<0.05) higher in control oocytes (63%) than those treated with all lectins, but penetration rates (40~49%) were simililar in group treated with lectins. The incidence of monospermy was similar in oocytes untreated and UEA-I, but it was higher in oocytes treated with BS-II, Con A, RCA-I and LCA. The porcine oocytes cultured for 48 h in TC-199 medium were freed from cumulus cells and treated for 30 min with fluorescein isothiocyanate-labelled lectins. When examined under fluorescein illumination, higher (p<0.001) proportions of oocytes showed fluorescein of zona pellucida after treatment with Con A (93%), LCA (93%) and RCA-I (100%) than BS-II (37%) and UEA-I (50%). All of the oocytes treated with RCA-I exhibited strong fluorescein in the outer region of the zona pellucida while those treated with LCA exhibited strong fluorescein throughout the zona pellucida. BS-II bounded mainly to the outer region and UEA-I bounded mainly to the inner region of the zona pellucida, with either strong or weak fluorescein. At 120 min after insemination in vitro, fewer spermatozoa were bound to the zona pellucida of the oocytes treated with BS-II, Con-A and RCA-I. Of the lectins, Con A most inhibited sperm binding. CONCLUSIONS: These results suggest that beta-D-Galactose residues in the porcine zona pellucida may act as primary sperm receptors and inducers of the sperm acrosome reaction and these sugar residues may be involved in the block to polyspermy.
Acrosome Reaction ; Cumulus Cells ; Fluorescein ; Glycoconjugates ; Glycoproteins ; Herpes Zoster* ; Incidence ; Insemination ; Lectins* ; Lens Plant ; Lighting ; Oocytes ; Plant Lectins ; Ricinus ; Sperm-Ovum Interactions ; Spermatozoa ; Swine ; Ulex ; Zona Pellucida*

A lectin from the haemolymph clam was purified by molecular sieving on sephadex- G75 column. The products have a high purity. The purity of lectin was assessed by SDS polyacrylamide gel. Two doublets band of apparent molecular weights of respectively about 14,000-17,000 and 20,000-23,000 Dalton were revealed upon staining with Coomassie blue. Optimum-pH of the lectin from the clams is pH 6,5-7,0 and 8,5-9,0. The lectins of the clams had very different specificity for hydratecarbons and glucoproteins
isolation & purification ; Lectins ; medicine

Lectin (APA) was purified from jequirity bean (Abrus precatorius) by affinity chromatography on insoluble ovomucoid. Lectin (APA) and conjugate Lectin-biotin have been used in ELLA technique (Enzyme Linked Lectinosorbent Assay) to detect some pathogenic bacteria. Based on its specific bioavailability to the poD-Gal sugar compounds in cell membrane, lectin (APA) was capable of differentiating B. anthracis and B. cereus from S. flexneri, S. sonnei, C. diphteria, and Salmonella and Staphylococcus aureus.
Lectins ; Abrus ; Diagnosis ; Bacteria

A study was conducted on biological active element lactin and clean lactin-biotin from Abrus precatorius in Hung Yen province. Result: clean lactin production from abrus precatorius and combination of Lectin (APA)-biotin were used to make ELISA to realize some disease-caused bacteria. Clean lectin (APA) related specific with original sugar β- D- Gal so it is able to realize B. anthracis bacterium and B. Cereus. Lectin (APA) does not connect with S. flexneri, S. sonnei, C.diphteriae and Salmonella bacteria. The findings of trial bring the new research approach in applying lectin in immunology production to contribute in diagnosis accurately bacterium strain cause disease.
Viruses ; Lectins ; Abrus

BACKGROUND: It is currently thought that tissue valve degeneration is related to an animal's immune response, which is mainly due to cell surface alpha-Gal epitopes. Cell surface alpha-Gal epitopes are known to be degraded by the enzyme called green coffee bean alpha-galactosidase. It is also well known that alpha-Gal epitopes are immunologically stained by Griffonia Simplicifolia isolectin type B4. We know that many commercially available tissue valves are made of aortic valves and pericardial tissue of pig. So, we investigated whether alpha-Gal epitopes of the aortic valve and pericardial tissue of a pig can be removed by green coffee bean alpha-galactosidase, and we did so by comparing immunologic staining of the tissues before and after the enzyme treatment. MATERIAL AND METHOD: After treating fresh porcine aortic valve and pericardial tissue with green coffee bean alpha-galactosidase at concentrations of 0.5 unit/mL, 1.0 unit/mL, 2.0 unit/mL, respectively, under the condition of pH 6.5, temperature 4degrees C and 24 hours of incubation, each sample was stained with Griffonia Simplicifolia isolectin type B4 immunofluorescent labeling. We then examined whether the alpha-Gal epitopes were reduced or abolished in each consecutive concentration of green coffee bean alpha-galactosidase by comparing the degree of the Griffonia Simplicifolia isolectin B4 staining in each sample. RESULT: In the pig aortic valve tissue, a 1.0 unit/mL concentration of green coffee bean alpha-galactosidase at pH 6.5, 4degrees C and reaction for 24 hours was enough for complete removal of alpha-Gal epitopes from the cell surface on the immunostaining with Griffonia Simplicifolia isolectin B4. On the other hand, more alpha-Gal epitopes were present in the pig pericardial tissue on Griffonia Simplicifolia isolectin B4 staining before the enzyme treatment, and 1.0 unit/mL of galactosidase was not sufficient for complete removal of alpha-Gal from the tissue. 2.0 units/mL of green coffee bean alpha-galactosidase was needed to completely remove the alpha-Gal epitopes from the pericardial tissue on immunostaining. CONCLUSION: The alpha-Gal epitopes of the pig's aortic valve and pericardial tissue were successfully stained with Griffonia Simplicifolia isolectin B4. We could remove nearly all the alpha-Gal epitopes using green coffee bean alpha-galactosidase at the concentration of 1.0 unit/mL in the aortic valve of pig, and 2.0 unit/mL was need to nearly completely remove all the alpha-Gal epitopes in the pericardial tissue of pig under the condition of pH 6.5, 4degrees C and 24 hours of reaction time. In the near future, removal of alpha-Gal epitopes in the pig's aortic valve and pericardial tissue will become a powerful tool for the improvement of the tissue valve durability. It needs to be determined if alpha-galactosidase treated pig tissue is immune to human anti-Gal antibody or anti-Gal monoclonal antibodies.
alpha-Galactosidase ; Aortic Valve ; Coffee ; Epitopes ; Galactosidases ; Griffonia ; Hand ; Humans ; Hydrogen-Ion Concentration ; Lectins ; Pericardium ; Plant Lectins ; Reaction Time ; Tissue Transplantation