• Title/Summary/Keyword: animal lectins

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Animal lectins: potential receptors for ginseng polysaccharides

  • Loh, So Hee;Park, Jin-Yeon;Cho, Eun Hee;Nah, Seung-Yeol;Kang, Young-Sun
    • Journal of Ginseng Research
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    • v.41 no.1
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    • pp.1-9
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    • 2017
  • Panax ginseng Meyer, belonging to the genus Panax of the family Araliaceae, is known for its human immune system-related effects, such as immune-boosting effects. Ginseng polysaccharides (GPs) are the responsible ingredient of ginseng in immunomodulation, and are classified as acidic and neutral GPs. Although GPs participate in various immune reactions including the stimulation of immune cells and production of cytokines, the precise function of GPs together with its potential receptor(s) and their signal transduction pathways have remained largely unknown. Animal lectins are carbohydrate-binding proteins that are highly specific for sugar moieties. Among many different biological functions in vivo, animal lectins especially play important roles in the immune system by recognizing carbohydrates that are found exclusively on pathogens or that are inaccessible on host cells. This review summarizes the immunological activities of GPs and the diverse roles of animal lectins in the immune system, suggesting the possibility of animal lectins as the potential receptor candidates of GPs and giving insights into the development of GPs as therapeutic biomaterials for many immunological diseases.

Studies on Lectins from Marine Animal Chlorostoma argyrostoma turbinatum (해양동물 구멍밤고둥의 렉틴 성분 연구)

  • Chung, See-Ryun;Choi, Il-Shik;Jeune, Kyung-Hee
    • Korean Journal of Pharmacognosy
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    • v.25 no.2
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    • pp.121-131
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    • 1994
  • Two kinds of new lectins, CATL-I and CATL-II, were partially purified from the intestine of Chlorostoma argyrostoma turbunatum by physical saline extraction, salt fractionation, ion exchange chromatography and gel filtration. CATL-I and CATL-II were purified 39.4 and 15.8 fold with a yield of 8.8 and 7.4%, respectively. On polyacrylamide gel electrophoresis, CATL-I demonstrated one major and one minor bands. This lectin agglutinated human and other animal erythrocytes nonspecifically and also agglutinated murine splenic lymphocytes. Carbohydrate specificity of the lectins was determined by inhibition of the agglutinability by methyl-${\alpha}-_D$-galactopyranoside and $_L-rhamnose$ at a final concentration of 6 mM. The lectins contained relatively high amounts of acidic amino acids, but the contents of sulfur containing amino acids were very low or was not estimated. Immunochemical studies were carried out to identify some properties of marine animal lectins.

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Lymphocytes Mitogenic and Immunochemical Properties of the Lectins from Marine Animal Lunella coronata coreensis (해양동물 눈알고둥 렉틴의 림프구 분열효과 및 면역화학적 특성)

  • 소명숙;전경희;정시련
    • YAKHAK HOEJI
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    • v.37 no.3
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    • pp.254-261
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    • 1993
  • Developing new substance for immunosuppressor or immunomodulator from natural products is extremely important in the present biomedicine. In this paper, we focused our efforts on the mitogenicity and immunochemical properties of the two lectins (LCC-I, LCC-II) obtained from marine animal Lunella coronata coreensis. Immunochemical techniques were employed to elucidate the structural and/or functional similarities between the LCC lectins. Molecular weight of the LCC lectins, LCC-I and LCC-II were estimated to be around 60 KD and 66-70 KD, respectively. LCC lectins were mitogens for murine splenic lymphocytes, and the optimum mitogenic doses were 31.25 $\mu\textrm{g}$/ml and 3.91 $\mu\textrm{g}$/ml, respectively. LCC-II lectin was a good mitogen toward human peripheral lymphocytes at a concentration about 31.25 $\mu\textrm{g}$/ml.

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Binding of Lectins to the Zona Pellucida on Sperm-oocytes Interaction in the Pig (체외에서 돼지 정자-난자의 상호작용시 투명대내 Lectin 결합)

  • Hwang, In-Sun;Kim, Choung-Ik;Cheong, Hee-Tae;Yang, Boo-Keun;Park, Choon-Keun
    • Clinical and Experimental Reproductive Medicine
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    • v.29 no.3
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    • pp.179-186
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    • 2002
  • 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-N-acetylglucosamine), Canavalin ensiformis (Con A, bind to $\alpha$-D-Mannose), Lens culinaris (LCA, bind to a-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 ($40{\sim}49%$) 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.

Studies on Lectins from Marine Shells (III) : Screening of Lectin-like Agglutinins from Marine Shells

  • Chung, See-Ryun;Kim, Jang-Hwan;Suh, Young-Ah;Jeunechung, Kyung-Hee
    • Archives of Pharmacal Research
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    • v.9 no.4
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    • pp.201-203
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    • 1986
  • Forty species of marine shells were collected from Korean coasts and studied extensively for their lectin activities by using erythrocytes of human blooc A, AB, B. O group and rabbit blood. In total, 7 species contained lectines :Neptunea intersculpta, Omphalius nigerrimus and Scapharca subcrenata, blood group nonspecific; Saxidomus purpuratus, human blood A and AB group specific; Lepidozona coreana, Tegilarca granosa and Neptunea polycosta, rabbit blood specific.

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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.

Studies on Lectins From Marine Shells (V) - Isolation and Purification of Letin from Tapes philippinarum. (해양 패류 렉틴성분 연구 (V) - 반지락조개의 렉틴성분 분리정제에 관한 연구)

  • 정시련;김장환;전경희
    • YAKHAK HOEJI
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    • v.31 no.2
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    • pp.52-59
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    • 1987
  • The result of the screening of lectins on 28 species of marine shell fishes(mollusks) showed that 10 species (Tapes philippinarum, Cyclosunetta menstrualis, Neptunea arthritica cumingii, Omphalius pfeifferi carpenteri, Chlorostoma argyrostoma turbinatum, Chiorostoma argyrostoma lischkei, Semisulcosira corea, Neptunea polycosta, Babylonica japonica, Noverita didyma) were present hemagglutinating properties to human A, B, and O group, and animal blood erythrocytes. A new lectin from Tapes philippinarum. was isolated and partially characterized. The lectin was purified by (NH$_4$)$_2$SO$_4$ precipitation and ion exchange chromatography on DE 53 column. Six fractions were obtained from DE 53 column by salt gradient elution but only 0.3M, and 0.4M NaCl fraction had strong lectin activity. On its 0.3M NaCl fraction, purity was identified by polyacrylamide gel electrophoresis. This lectin was inhibited by N-acetyl-D-galactosamine. It seems that two kinds of lectin react as antigen by immunochemical studies.

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Identification of Species-Specific Components between Hanwoo and Holstein Meat (한우 및 홀스타인육의 품종간 특이성분의 검색에 관한 연구)

  • 황보식;이수원;임태진;정구용
    • 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.

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