• Journal of Life Science
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• v.14 no.3
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• pp.417-424
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• 2004

This study attempts to investigate lectin binding patterns of the glycoconjugates of the esophageal mucous cells in four teleostean speceis, i. e., Sebastes schlegeli, Halichoeres poecilopterus, Bryzoichthys lysimus and Takifugu pardalis. To investigate glycoconjugates of esophageal mucous cells, nine biotinylated lectins (DBA, SBA, PNA, BSL-l, RCA-l, sWGA, UEA-l, LCA and ConA) were applied with ABC method. Esophageal mucous cells of Sebastes schlegeli and Halichoeres poecilopterus were mixed with large, medium sized and small mucous cells. But these cells of the other species only were mixed with medium sized and small mucous cells. The lectin binding pattern of esophageal mucous cells depends on the species; Sebastes schlegeli was stained with DBA, SBA, BSL-l, RCA-l and sWGA, Halichoeres poecilopterus with DBA, SBA, PNA and sWGA, Bryzoichthys lysimus with SBA and sWGA, Takifugu pardalis with all lectins except DBA, LCA and Con A, respectively. All the mucous cells of Sebastes schlegeli were stained with DBA, SBA and sWGA, while small mucous cells with BSL-l besides these lectins. In Halichoeres poecilopterus,l the large mucous cells reacted with PNA, medium sized mucous cells with DBA, SBA and sWGA, and small mucous cells with DBA and SBA, respectively. Medium sized mucous cells of Bryzoichthys lysimus were stained with sWGA, and small mucous cells with SBA and sWGA. In Takifugu pardalis, all mucous cells reacted with SBA, PNA and RCA-l, but medium sized mucous cells with sWGA and UEA-l besides these lectins. Especially DBA and SBA lectins showed a strong binding to all mucous cells of Sebastes schlegeli. In Halichoeres poecilopterus, PNA binding were notable in large mucous cells, and SBA binding in medium sized and small cells, respectively. However, SBA, PNA, sWGA and UEA-l lectins of Takifugu pardalis showed a strong binding to medium sized mucous cells, but RCA-l binding which small mucous cells were notable.

• Applied Microscopy
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• v.32 no.2
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• pp.163-170
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• 2002

Experimatal maxillary sinusitis was induced in New Zealand white rabbits by blocking the maxillary sinus ostium. The distribution of lectin receptors was explored in the mucosa with induced maxillary sinusitis using colloidal gold label complex with lectin WGA purified from wheat germ (Triticum vulgaris). The lectin WGA gold complex, shown to recognize GlcNac (N-acetylglucosamine) and NeuNAc (N-acetylneuraminic acid) regions, was applied to detect binding sites in Lowicryl HM 20 sections and viewed under the electron microscope. An increased height of the cylindric cells, ciliary loss and hyperplasia of the secretory cells were observed. Examination of normal sinus mucosa labeled with gold-labeled lectins showed the distribution of sialoglycoconjugates to be mainly in the ciliary layer and the granules in the secretory cells. Inflamed mucosa had increased labeling intensity of gold-labeled WGA in the cilia and the secretory granules. These results indicate that lectin WGA receptors are located in the cilia and secretory granules. Specific changes in the lectin binding pattern were apparent in the inflamed mucosa in the experimentally induced acute sinusitis, in comparison with normal mucosa, conceivably as a part of host defense reactions.

• YAKHAK HOEJI
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• v.45 no.3
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• pp.302-309
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• 2001

Wheat germ agglutinin (WGA) pectin, which binds to human melanoma cell line, was conjugated with Praecoxin A using 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide as a cross-linking agent. Physical mixture (PM) of WGA and Praecoxin A was also prepared by using a non-specific binding property of Praecoxin A to WGA. The WGA:Praecoxin A ratio in the conjugate and PM was approximately 1:18 and 1:20, respectively. The results of hemagglutination assay and enzyme-linked lectin assay indicated that the conjugate and PM maintained the lectin-like properties of the WGA. The binding ratio of conjugate was about 70% during 4-24 hr, but the most of Praecoxin A was released within 24 hr in the case of PM. These results lead to the conclusion that the conjugate is potentially useful for the formulation of injection that requires targeting for melanoma as well as sustained release at the site.

• Applied Microscopy
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• v.30 no.1
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• pp.101-111
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• 2000

In this study, the distribution of lectin receptors in Paragonimus westermani tissue was explored using colloidal gold label complexed with lectin WGA purified from wheat germ (Triticum vulgare). The lectin WGA gold complex, shown to recognize GlcNAc (N-acetylgalactosamine) and NeuNAc (N-acetylneuraminic acid) regions, was applied to detect binding sites in Lowicryl HM 20 sections viewed under electron microscope. Labeled sections of the metacercaria revealed gold particles specifically distributed on the tegumental syncytium and lamella of the excretory canal. Labeling of young adult tissue was then quantified and compared to that of adult worm tissue. Adult worm tissue sections resulted in specific gold particle distribution on the lamella of caecal epithelium and excretory canal. These results indicate that lectin WGA receptors are located in the tegumental syncytium and lamella of the excretory canal of the metacercariae, and in the lamella of the caecum and excretory canal of the young adult and adult. Therefore, the GlcNAc and NeuNAc regions in the tegumental syncytium appear to be functionally associated with cell-recognition and protection from the immune system of the host, and linked with membrane transport and absorption of nutrients in the lamella of the excretaory canal and caecal epithelia.

• Journal of Life Science
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• v.18 no.11
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• pp.1543-1550
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• 2008

We studied the effects of smoking, which is one of indoor-environmental pollutants and related to various cancers, on glycoconjugates of rat sebaceous glands with the lectin histochemistry. To investigate the effects of smoking on glycoconjugates, male Sprague-Dawley rats were exposed to tabacco smoke for 10 minutes per day in an inhalation chamber for 1, 2, 3, and 5 days with active and passive exposure. For the structure of sebaceous glands we used PAS reaction, and for the glycoconjugates binding pattern 9 biotinylated lectins (DBA, SBA, PNA, BSL-1, WGA, RCA-1, UEA-1, Con A, and LCA) were used. Some remarkable changes, such as the decrease in the size of sebaceous glandular acini, the destruction of upper portion of sebaceous glands, vacuolation of central portion of sebocytes, and the immature sebaceous glandular acini were seen in the smoke-exposed rats. In the control rats, basal cells were stained with BSL-1, PNA and WGA, but the stronger reaction was founded in BSL-1 binding. Also, sebocytes were stained with PNA, WGA, Con A, BSL-1 and SBA, but stronger reactions were founded in PNA and Con A stainings. Specific changes in the lectin binding patterns were also observed in the smoke-exposed rats. In the basal cells of exposed rats, PNA binding increased, BSL-1 decreased but returned to control level, and WGA disappeared. Plus, immature glandular acini, which were not found in the control rats, were stained PNA, Con A and BSL-1, but the stronger reaction were founded in PNA and Con A binding. In conclusion, it was assumed that the tabacco smoke seriously effected on the structure and glycoconjugates metabolism of sebaceous glands.

• Applied Microscopy
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• v.31 no.1
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• pp.49-57
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• 2001

In this study, the distribution of lectin receptors in culutured fibroblast was explored using colloidal gold label complexed with lectin WGA purified from wheat germ (Triticum vulgare). The lectin WGA gold complex, shown to recognize GlcNAc (N-acetylgalactosamine) and NeuNAc (N-acetylneuraminic acid) regions, was applied to detect binding sites in Lowicryl HM 20 sections viewed under electron microscope Labeled sections of the culutured fibroblast revealed gold particles specifically distributed on the cytoplasm and cell surface of the fibroblast. Labeling of 24 hours culutured fibroblast was then quantified and compared to that of 72 hours culutured fibroblast. 24 hours culutured fibroblast sections resulted in specific gold particle distribution on the cytoplasmic vesicle of the culutured fibroblast. These results indicate that lectin WGA receptors are located in the cytoplasmic vesicle and cell surface of the 24 hours culutured fibroblast, and on the cell surface of the 72 hours culutured fibroblast. Therefore, the GlcNAc and NeuNAc regions on the cell surface appear to be functionally associated with cell-recognition and protection from other cell of the tissue, and linked with secretion and exocytosis of the fibroblast cytoplasm.

• Journal of Life Science
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• v.18 no.9
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• pp.1239-1243
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• 2008

Though relatively little is known of the physiology involved, there is reduced kidney activity during hibernation. In this experimental study, male Korean chipmunks (Tamias sibiricus barberi) were maintained in cold conditions ($6^{\circ}C$) for 9 months, in an attempt to mimic conditions occurring during seasonal hibernation. The examination was made to determine changes of glycoconjugates on the kidney after hibernation by lectin histochemistry. The changes of lectin affinities in the kidney categorize into three groups: a) increase ones only in the early hibernation stage b) increase ones during hibernation and c) decrease ones during hibernation. The transient increase of Con A affinity in the proximal convoluted tubules were demonstrated only in the early cold-treated stage, and PNA and Con A in the distal convoluted tubules and DBA and sWGA in the collecting tubules. SBA affinity tended to increase with hibernation in the proximal convoluted tubules, but sWGA affinities were significantly decreased in the all tubule examined with hibernation. The present results suggest that the glycosylation pattern of the kidney undergoes profound changes during hibernation, and is probably associated with transiently reduced renal function.

• Korean Journal of Veterinary Research
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• v.52 no.1
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• pp.1-8
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• 2012

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.

• Tuberculosis and Respiratory Diseases
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• v.41 no.3
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• pp.248-261
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• 1994

Background: Lectins are proteins or glycoproteins of non-immune origin that recognize a specific sequence of sugar residues. The availability of a large number of lectins has provided the capacity to identify selectively glycoconjugates possessing distinctive chemical structure in diverse sites of highly specialized biological activity. The purpose of the present study was to investigate the lectin binding patterns of various components in human pulmonary tubercles. Method: Biopsy specimens of tuberculous lung were obtained from male adult patients who underwent a surgical resection for severe pulmonary tuberculosis. The specimens were processed and stained with 13 kinds of biotinylated lectins according to some modification of Hsu and Raine's methods. Results: 1) In the caseous necrotic lesions, BS $I-B_4$ showed negative reaction and BS I were also negative except some irregularly-shaped cells located in the marginal zone. All other lectins, however, showed a positive reaction with various binding patterns. 2) The epithelioid cells were broadly divided into three groups according to the reaction patterns in the cytoplasms and cell membranes. 3) WGA, ECL, PHA-L, PHA-E and LCA showed strong staining in the lymphocytes. 4) SBA showed a different binding patterns between the endothelial layers located in the region beyond the fibrous layers and those located within the fibrous layers. 5) PNA showed a positive reaction in the outer 1/3 to 1/2 of the fibrous layer, but showed no staining in the inner 1/2 to 2/3 of the fibrous layers. Conclusion: The present lectin histochemical study provided a useful information to assess the characterization and distribution of various glycoconjugates in each constituent of human pulmonary tubercles. The results demonstrate structural differences in the glycoconjugate composition of various components of the tubercles and reveal changes in glycosylation in the components during soft tubercle formation. This study provides a new data useful for the studies on the pathogenesis and pathology of human pulmonary tubercles.

• Development and Reproduction
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• v.5 no.2
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• pp.167-173
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• 2001

To characterize the difference in glycoconjugates of mouse epididymis, lectin labeling of the tissue section was conducted using Ulex europaeus agglutinin I(UEA I), succinylated wheat germ agglutinin(sWGA), and Griffonia simplicifolia lectin-I(GSL-I). UEA I which binds to outer $\alpha$-L-fucose residue that is a terminal sugar of the side chain branched from oligosaccharide chain gave the labeling in the proximal caput epithelia exclusively. Lumen was commonly labeled in all of the organ. It suggested that the glycoconjugates bearing outer $\alpha$ -L-fucose residue were largely expressed in the initial segments ot epididymis and subjected to secretion. GSL-I which binds to terminal $\alpha$ -D-galactosyl residue of glycoconjugates gave the labeling in the cytoplasm of clear cells and basal cells, and cilia in corpus and cauda regions but not in the caput region. There was no vast difference in labeling pattern by sWGA which binds to N-acetyl-glucosamine residue among the epididymal regions. Clear cells in corpus and cauda epithelia showed more intense labeling by sWGA compared to principal cells, suggesting the functional specialization of this type of cells. The labeling intensities of luminal content by UEA I and sWGA decreased in cauda region compared to corpus region suggesting the presence of enzymatic activities responsible for processing the $\alpha$-L-fucose and N-acetyl-glucosamine residues from secreted glycoconjugates. In summary, the difference in glycoconjugates bearing the $\alpha$-L-fucose, $\alpha$-D-galactose, and N-acetyl-glucosamine residues according to the type of epithelial cells and epididymal segments suggests functional specialization and different roles of each segment in the processing of sperm surface antigens during the epididymal transit.