• BMB Reports
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• v.38 no.2
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• pp.128-150
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• 2005

Invertebrate animals, which lack adaptive immune systems, have developed other systems of biological host defense, so called innate immunity, that respond to common antigens on the cell surfaces of potential pathogens. During the past two decades, the molecular structures and functions of various defense components that participated in innate immune systems have been established in Arthropoda, such as, insects, the horseshoe crab, freshwater crayfish, and the protochordata ascidian. These defense molecules include phenoloxidases, clotting factors, complement factors, lectins, protease inhibitors, antimicrobial peptides, Toll receptors, and other humoral factors found mainly in hemolymph plasma and hemocytes. These components, which together compose the innate immune system, defend invertebrate from invading bacterial, fungal, and viral pathogens. This review describes the present status of our knowledge concerning such defensive molecules in invertebrates.

• Macromolecular Research
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• v.17 no.4
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• pp.232-239
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• 2009

This paper describes the simple nanopatterning of proteins on polyelectrolyte surfaces using microcontact printing with a nanopatternable, hydrophilic composite nanomold. The composite nanomold was easily fabricated by blending two UV-curable materials composed of Norland Optical Adhesives(NOA) 63 and poly(ethylene glycol) dimethacrylate(PEG-DMA). NOA 63 provided stable nanostructure formation and PEG-DMA induced high wettability of proteins in the nanomold. Using the composite mold and functionalized surface with polyelectrolytes, the fluorescent, isothiocyanate-tagged, bovine serum albumin(FITC-BSA) was successfully patterned with 8 nm height and 500 nm width. To confirm the feasibility of the protein assay on a nanoscale, a glycoprotein-lectin assay was successfully demonstrated as a model system. As expected, the lectins correctly recognized the nano-patterned glycoproteins such as chicken ovalbumin. The simple preparation of composite nanomold and functionalized surface with a universal platform can be applied to various biomolecules such as DNA, proteins, carbohydrates, and other biomolecules on a nanoscale.

• Korean Journal of Pharmacognosy
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• v.42 no.1
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• pp.68-75
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• 2011

A new lectin was purified from Bombyx mori (BML) by physiological saline extraction, ammonium sulfate precipitants, anion exchange column chromatography on DEAE Sephadex A-50 and gel filtration column chromatography on Sephadex G-200. BML agglutinated trypsinized and glutaraldehyde-fixed erythrocytes, and was observed the most high activity with rabbit, chicken erythrocytes and rat splenic lymphocytes. Agglutinability was markedly affected at highly acidic pH, but was relatively stable with high temperature. The effect of metal ions was observed and BML was affected by bivalaent cations, especially depending on $Ca^{2+}$, $Fe^{2+}$, $Mn^{2+}$, whereas, inhibited by $Mg^{2+}$. Agglutination was strongly inhibited by heparin and glucuronic acid. BML was proved to be a glycoprotein which contains 17.16% of sugars. By mass spectrometry analysis, we found 2 bands that were considered as lectin subunits.

• Korean Journal of Veterinary Research
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• v.44 no.1
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• pp.83-88
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• 2004

Galectin family, endogenous ${\beta}$-galactoside-binding animal lectins, is known for the role in cell differentiation, morphogenesis, apoptosis and tumorigenesis. Galectin-3, one of family member, has been studied for its role in cell differentiation and tumor metastasis, and for its expression on epithelial cells of colon and mast cells but not in brain. Several reports, however, suggest its expression in brain including as a prion binding protein. In this report we explored possibility of galectin-3 expression in brain tissue. With Western blot and RT-PCR with rat brain tissues, we could detect galectin-3 that was not shown by conventional immunohistochemistry. Our results indicated galectin-3 was expressed in brain, and substantiate the previous report on galecin-3 as a prion-related protein in brain.

• Mass Spectrometry Letters
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• v.7 no.3
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• pp.74-78
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• 2016

Targeted glycoproteomics is an effective way to discover disease-associated glycoproteins in proteomics and serial affinity chromatography (SAC) using lectin and glycan-targeting antibodies shows glycan diversity on the captured glycoproteins. This study suggests a way to determine glycan heterogeneity and structural analysis on the post-translationally modified proteins through serial affinity column set (SACS) using four Lycopersicon esculentum lectin (LEL) columns. The great advantage of this method is that it differentiates between glycoproteins on the basis of their binding affinity. Through this study, some proteins were identified to have glycoforms with different affinity on a single glycoprotein. It will be particularly useful in determining biomarkers in which the disease-specific feature is a unique glycan, or a group of glycans.

• Food Science of Animal Resources
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• v.21 no.3
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• pp.246-255
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• 2001

Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) of muscles extracted with distilled water, saline solution, SDS or Trition X-100 showed simular protein patterns between Hanwoo and Holstein meat, indicating that SDS-PAGE technique may not be useful for the identification between Hanwoo and Holstein meat. Lectine blot analysis of muscle extracted with distilled water demonstrated that Hanwoo and Holstein meat had similar affinities for concanavalin A (Con A), ricinus communis agglutinin (RCA-120), ulex europaeus agglutinin (UEA-1) or peanut agglutinin (PNA) lectins. However, approximately 32.1 kDa component of Hanwoo meat showed high affinity for dolichos biflorus agglutinin (DBA) lectin. On the contrary, high molecular weight components of Holstein meat had the specific affinity for wheat germ agglutinin (WGA) lectin. Hanwoo meat-specific components were observed by lectin staining of heat-denatured meat at 100$^{\circ}C$ for 30 sec. Also, the component of heat-denatured meat at 100$^{\circ}C$ for 30 sec, which was slightly smaller than Hanwoo meat-specific component, was concentrated specifically in Holstein meat.

• Journal of Microbiology and Biotechnology
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• v.11 no.1
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• pp.35-39
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• 2001

A simple method for studying the lectin-like interactions between Helicobacter pylori and cultured human epithelial cell lines was developed using an enzyme-linked, biotin-streptavidin bacterial-adhesion assay. The present study suggests that this method is suitable for evaluating the participation of lectin interactions in the adhesion of H. pylori to cultured HeLa S3 and Kato III cells, both fixed and glycosidase-treated cells, as well as assessing glycoconjugated binding inhibition studies. The time-course and dose-dependent kinetics of the biotin-labeled H. pylori adhesion th the formaldehyde-fixed Hela S3 and Kato III cell lines exhibited saturation. In addition, the binding of the biotin-labeled H. pylori to the formaldehyde-fixed cultured cells was partially blocked by pre-incubation with glycoconjugates and polyclonal antibodies against a heparan sulfate binding protein from H. pylori.

• Biotechnology and Bioprocess Engineering:BBE
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• v.3 no.1
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• pp.40-43
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• 1998

The glycosylation pattern of Erythropoietin (EPO), produced by recombinant CHO cells, was studied using the simple and rapid technique of 'Lectin-blotting'. In this experiment we used three different kinds of lectins, MAA(Maackia amurensis agglutinine), RCA(Ricinus communis agglutinine), and DSA(Datura stramonium agglutinine), which bind to the terminal sialic acid, galactose, and the N-acetyllactosamine chain respectively. The lectin-blotting technique was used to analyze the carbohydrate structure of EPO produced in the presence of two physiologically active chemical compounds, ammonium and chloroquine. The effect of the ammonium ion on the glycosylation of EPO was studied because it accumulated in the medium mainly as a by-product of glutamine matabolism. Ammonium chloride significantly inhibited the sialylation of the terminal galactose residue at concentrations of 8mM or more. Chloroquine, a potent inhibitor of glycosylation, inhibited terminal sialylation at concentrations of 100 and 200 $\mu$M, and at a concentration of 300 $\mu$M, also inhibited Nacetyllactosamine chain synthesis.

• Biomolecules & Therapeutics
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• v.2 no.2
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• pp.126-130
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• 1994

Water-soluble pectins isolated from Trichosanthes Rhizoma and Taraxii Herba and their deproteinized polysaccharides were purified through DEAE cellulose column and were applied to immunopotentiating and antitumor studies to clarify the nature of their activities of our previous reports. As the results of works, the lectins and deproteinized polysaccharides increased the number of circulating leukocytes and total peritoneal cells. And they markedly elevated the lowered production of antibody and reactivity of T Iymphocyte in tumor-bearing mice, which were rapidly recovered by discontinuance of sample treatments. They also decreased the growth of Sarcoma 180 solid tumor in mice.

• Proceedings of the PSK Conference
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• 2003.10b
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• pp.204.2-204.2
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• 2003

The aqueous extract of European mistletoe (Viscum album, L.) has been used in cancer therapy. The purified mistletoe lectins, main components of mistletoe, have demonstrated cytotoxic and immune-system-stimulating activities. Korean mistletoe (Viscum album L. coloratum), a subspecies of European mistletoe, has also been reported to possess anticancer and immunological activities. A galactose- and N-acetyl-D-galactosamine- specific lectin (Viscum album L. coloratum agglutinin, VCA) with Mr 60 kDa was isolated from Korean mistletoe. (omitted)