• Title/Summary/Keyword: lectin

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Antitumor Effect of Asterina pectinifera Lectin on Ascitic Tumor (별불가사리 렉틴의 복수암에 대한 항암효과)

  • Shon, Yun-Hee;Jeune, Kyung-Hee;Choi, Soo-Jeong;Chung, See-Ryun
    • YAKHAK HOEJI
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    • v.42 no.4
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    • pp.388-394
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    • 1998
  • The lectin from starfish, Asterina pectinifera, was purified and tested for its potential antitumor activity. It was shown to possess considerable toxicity toward various tumor cell lines. Concentration of Asterina pectinifera lectin (APL) at 4mg/$5{\times}10^5$ cells resulted in 28% death of Ehrlich ascites tumor cell, 40% of L929, 60% of A549, and 52% of HeLa cells after 48 hours incubation. Toxicity of APL to L929, Ehrlich ascites, A549, and HeLa cells revealed a reduction in cell viability of approximately 70% at APL concentration of 8mg/$5{\times}10^5$ cells after 48 hours incubation. Administration of APL ($100{\mu}g/day$ or $300{\mu}g/day$) inhibited the growth of Ehrlich ascites cells in vivo. Mice given only Ehrlich cells survived an average of $15{\pm}1$ (S.E.) days. Mice given Ehrlich cells and $100{\mu}g\;or\;300{\mu}g$ APL had 58% and 67% survival, respectively, after 20 days. These results suggest that APL has antitumor activity.

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An Antibacterial Lectin from Lampteromyces japonicus (화경버섯의 항세균성 렉틴)

  • Yoon, Joo-Ok;Min, Tae-Jin;Yoon, Hee-Sik
    • The Korean Journal of Mycology
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    • v.23 no.1 s.72
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    • pp.46-52
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    • 1995
  • A lectin was isolated from the fruiting bodies of Lampteromyces japonicus by preparative PAGE and named LJAP (Lampteromyces japonicus antibacterial protein). LJAP was a polymeric protein of more than one hundred kDa consisting of 17-kDa subunits. The amino acid analysis revealed a high content of serine, glycine, and acidic amino acids. LJAP has an excellent antibacterial activity for Escherichia coli, JM 109, K 12, HB 101, and JW 380. By the inhibition assay of the antibacterial activity, a glycoprotein, asialofetuin was confirmed as the best inhibitor. This is the first lectin isolated and characterized its antibacterial and agglutination activities from the family Lampteromyces.

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Anti-tumor Effect of Korean Mistletoe Extract Intensified with Mistletoe Lectin against Melanoma Cells in vitro and in vivo (Lectin으로 강화한 한국산 겨우살이 추출물의 in vitro 및 in vivo에서의 피부암에 대한 항암효과)

  • Yang, Eun-Young;Yeo, Jeong-Hoon;Jin, Ji-Young;Kim, Hyun-Sung;Park, Won-Bong;Suh, Jung-Jin;Hwang, Suk-Yeon
    • Korean Journal of Pharmacognosy
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    • v.34 no.3 s.134
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    • pp.218-222
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    • 2003
  • The mistletoe lectins are major active components in the extrct of Viscum album var. coloratum. This study was performed to investigate the anti- skin cancer effect of Korean mistletoe extract intensified with mistletoe lectin (KI 2103S). B16F10 melanoma cells were allografted in C57BL/6 mice and F344 rats. The effect of KI 2103S on melanoma was measured by monitoring tumor index. The KI 2103S was injected intra-tumorally and tumor index was decreased in dose dependent manner.

A Simple and Rapid Methicillin-Resistant Staphylococcus aureus (MRSA) Screening Test Using a Mannose-Binding Lectin (MBL)-Conjugated Gold Nanoparticle Probe

  • So Yeon Yi;Jinyoung Jeong;Wang Sik Lee;Jungsun Kwon;Kyungah Yoon;Kyoungsook Park
    • Journal of Microbiology and Biotechnology
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    • v.33 no.5
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    • pp.698-705
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    • 2023
  • Rapid diagnosis of methicillin-resistant Staphylococcus aureus (MRSA) is essential for guiding clinical treatment and preventing the spread of MRSA infections. Herein, we present a simple and rapid MRSA screening test based on the aggregation effect of mannose-binding lectin (MBL)-conjugated gold nanoparticles (AuNP), called the MRSA probe. Recombinant MBL protein is a member of the lectin family and part of the innate immune system. It can recognize wall teichoic acid (WTA) on the membrane of MRSA more specifically than that of methicillin-sensitive Staphylococcus aureus (MSSA) under optimized salt conditions. Thus, the MRSA probe can selectively bind to MRSA, and the aggregation of the probes on the surface of the target bacteria can be detected and analyzed by the naked eye within 5 min. To demonstrate the suitability of the method for real-world application, we tested 40 clinical S. aureus isolates (including 20 MRSA specimens) and recorded a sensitivity of 100%. In conclusion, the MRSA probe-based screening test with its excellent sensitivity has the potential for successful application in the microbiology laboratory.

Purification and Characterization of a Lectin from Arisaema tortuosum Schott Having in-vitro Anticancer Activity against Human Cancer Cell Lines

  • Dhuna, Vikram;Bains, Jagmohan Singh;Kamboj, Sukhdev Singh;Singh, Jatinder;Shanmugavel;Saxena, Ajit Kumar
    • BMB Reports
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    • v.38 no.5
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    • pp.526-532
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    • 2005
  • A lectin with in-vitro anticancer activity against established human cancer cell lines has been purified by affinity chromatography on asialofetuin-linked amino activated silica beads from the tubers of Arisaema tortuosum, popularly known as Himalayan Cobra lily, a monocot plant from the family Araceae. The bound Arisaema tortuosum lectin (ATL) was eluted with glycine-HCl buffer, pH 2.5. ATL was effectively inhibited by asialofetuin, a complex desialylated serum glycoprotein as well as by N-acetyl-D-lactosamine, a disaccharide. It gave a single band corresponding to a subunit molecular weight of 13.5 kDa in SDS-PAGE, pH 8.8 both under reducing and non reducing conditions. When subjected to gel-filtration on Biogel P-200, it was found to have a molecular weight of 54 kDa, suggesting a homotetramer structure, in which individual polypeptides are not bound to each other with disulfide bonds. ATL is a glycoprotein with 0.9% carbohydrate content, stable up to $55^{\circ}C$ and at pH 2 to 10. The lectin had no requirement for divalent metal ions i.e. $Ca^{2+}$ and $Mn^{2+}$ for its activity. However, as reported for other monocot lectins, ATL gave multiple bands in isoelectric focusing and Native PAGE, pH 8.3. The lectin was found to inhibit in vitro proliferation of human cancer cell lines HT29, SiHa and OVCAR-5.

A Novel Mannose-binding Tuber Lectin from Typhonium divaricatum (L.) Decne (family Araceae) with Antiviral Activity Against HSV-II and Anti-proliferative Effect on Human Cancer Cell Lines

  • Luo, Yongting;Xu, Xiaochao;Liu, Jiwei;Li, Jian;Sun, Yisheng;Liu, Zhen;Liu, Jinzhi;Damme, Els Van;Balzarini, Jan;Bao, Jinku
    • BMB Reports
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    • v.40 no.3
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    • pp.358-367
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    • 2007
  • A novel mannose-binding tuber lectin with in vitro antiproliferative activity towards human cancer cell lines and antiviral activity against HSV-II was isolated from fresh tubers of a traditional Chinese medicinal herb, Typhonium divaricatum (L.) Decne by a combined procedure involving extraction, ammonium sulfate precipitation, ion exchange chromatography on DEAE-SEPHAROSE, CM-SEPHAROSE and gel-filtration on sephacryl S-200. The apparent molecular mass of the purified Typhonium divaricatum lectin (TDL) was 48 kDa. TDL exhibits hemagglutinating activity toward rabbit erythrocytes at 0.95 $\mu$g/ml, and its activity could be strongly inhibited by mannan, ovomucoid, asialofetuin and thyroglobulin. TDL showed antiproliferative activity towards some well established human cancer cell lines, e.g. Pro-01 (56.7 $\pm$ 6.8), Bre-04 (41.5 $\pm$ 4.8), and Lu-04 (11.4 $\pm$ 0.3). The anti-HSV-II activity of TDL was elucidated by testing its HSV-II infection inhibitory activity in Vero cells with $TC_50$ and $EC_50$ of 5.176 mg/ml and 3.054 $\mu$g/ml respectively. The full-length cDNA sequence of TDL was 1145 bp and contained an 813-bp open reading frame (ORF) encoding a 271 amino acid precursor of 29-kDa. Homology analysis showed that TDL had high homology with many other mannose-binding lectins. Secondary and three-dimensional structures analyses showed that TDL is heterotetramer and similar with lectins from mannose-binding lectin superfamily, especially those from family Araceae.

Glycoconjugates Properties of the Kidney in the Hibernating Chipmunks (동면 중 한국산 다람쥐 신장의 복합당질 변화)

  • Gil, Young-Gi
    • 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.

Immunoadjuvant Activity of Korean Mistletoe Lectin B-chain (한국산 겨우살이 Lectin B-chain의 면역증강 효과)

  • Her, Sun-Mi;An, Hyo-Sun;Kim, Kyu-Dae;Kim, Young-Hoon;Kim, In-Bo;Yoon, Taek-Joon;Kim, Jong-Bae
    • Korean Journal of Pharmacognosy
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    • v.42 no.3
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    • pp.246-252
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    • 2011
  • Korean mistletoe Lectin (KML-C) is composed of A and B sub-chain. B chain binds to carbohydrates on cell surface and A chain hinders translation and induces an apoptosis as a RIP (ribosome inactivating protein). KML-C has very strong biological activities, it has seriously limits to use as a cancer therapy or adjuvant because of its toxicity to normal cells. This study is therefore conducted to see if B chain of KML-C might have immunological activity, especially adjuvant activities with less toxicity. We isolated B chain from KML-C using the lactose affinity chromatography, and examined their immunoadjuvant activity. The isolated B-chain did not show any cytotoxicity against tumor cell, RAW264.7, and P388D1 while KML-C had a very strong toxicity. This non-toxic effect was observed also by in-vivo study. Both humoral and cellular immunities were observed ; the antibody titer was increased when the mice were immunized with B-chain used as adjuvant like Freund's adjuvant, indicating that B chain of mistletoe lectin alone might be used for adjuvant; it also increased DTH in cellular immunity. These results suggest that B-chain of KML-C might be used for adjuvant used for the production of antibody or vaccine with less toxicity.

Protective effect of lectin from Synadenium carinatum on Leishmania amazonensis infection in BALB/c mice

  • Afonso-Cardoso, Sandra R.;Rodrigues, Flavio H.;Gomes, Marcio A.B.;Silva, Adriano G.;Rocha, Ademir;Guimaraes, Aparecida H.B.;Candeloro, Ignes;Favoreto, Silvio;Ferreira, Marcelo S.;Souza, Maria A. de
    • Parasites, Hosts and Diseases
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    • v.45 no.4
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    • pp.255-266
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    • 2007
  • The protective effect of the Synadenium carinatum latex lectin (ScLL), and the possibility of using it as an adjuvant in murine model of vaccination against American cutaneous leishmaniasis, were evaluated. BALB/c mice were immunized with the lectin ScLL (10, 50, 100$[\mu}g$/animal) separately or in association with the soluble Leishmania amazonensis antigen (SLA). After a challenge infection with $10^6$ promastigotes, the injury progression was monitored weekly by measuring the footpad swelling for 10 weeks. ScLL appeared to be capable of conferring partial protection to the animals, being most evident when ScLL was used in concentrations of 50 and 100${\mu}g$/animal. Also the parasite load in the interior of macrophages showed significant reduction (61.7%) when compared to the control group. With regard to the cellular response, ScLL 50 and 100 ${\mu}g$/animal stimulated the delayed-type hypersensitivity (DTH) reaction significantly (P < 0.05) higher than SLA or SLA plus ScLL 10 weeks after the challenge infection. The detection of high levels of IgG2a and the expression of mRNA cytokines, such as IFN-$\gamma$, IL-12, and TNF-$\alpha$ (Th1 profiles), corroborated the protective role of this lectin against cutaneous leishmaniasis. This is the first report of the ScLL effect on leishmaniasis and shows a promising role for ScLL to be explored in other experimental models for treatment of leishmaniasis.

Histology and lectin histochemistry in the vomeronasal organ of Korean native cattle, Bos taurus coreanae

  • Jang, Sungwoong;Kim, Bohye;Kim, Joong-Sun;Moon, Changjong
    • Journal of Animal Reproduction and Biotechnology
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    • v.36 no.4
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    • pp.270-284
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    • 2021
  • The vomeronasal organ (VNO) is critical for reproduction and social behavior in ruminants, including cattle. The present study examined the structure of the VNO and its epithelial cells in neonatal and adult Korean native cattle (Hanwoo), Bos taurus coreanae, using immunohistochemistry and lectin histochemistry. Histologically, the VNO comprised two types of epithelia: medial vomeronasal sensory (VSE) and lateral vomeronasal non-sensory epithelia (VNSE). Numerous blood vessels and nerve bundles were observed within the vomeronasal cartilage encased lamina propria. Immunohistochemistry revealed high expression level of protein gene product9.5 and moderate expression level of olfactory marker protein in the neuroreceptor cells of the VSE and occasionally in some ciliated cells of the VNSE in both neonates and adults. The properties of the glycoconjugates in the VNO were investigated using 21 lectins, most of which were expressed at varied intensities in the VSE and VNSE, as well as in the lamina propria. Several lectins exhibited variations in their intensities and localization between neonatal and adult VNOs. This study is the first descriptive lectin histochemical examination of the VNO of Korean native cattle with a focus on lectin histochemistry, confirming that the VNO of Korean native cattle is differentiated during postnatal development.