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Artículos de revistas sobre el tema "Lectins"

Autor: Grafiati

Publicado: 4 de junio de 2021

Última modificación: 25 de julio de 2025

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1

Ogilvie, Mary L., JoAnn Wilson Byl, and T. Kent Gartner. "Platelet Aggregation Is Stimulated by Lactose-lnhibitable Snake Venom Lectins." Thrombosis and Haemostasis 62, no. 02 (1989): 704–7. http://dx.doi.org/10.1055/s-0038-1646887.

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SummaryFive lactose-specific lectins from snake venoms were tested for the ability to stimulate the aggregation of human platelets. Three of the lectins, bushmaster (Lachesis muta), cottonmouth (Aricistrodon piscivorous leukostoma) and rattlesnake (Crotalus atrox) lectins, consistently stimulated secretion and aggregation. Thrombolectin (Bothrops atrox) occasionally caused aggregation. Copperhead (Agkistrodon contortrix contortrix) lectin did not by itself cause platelet aggregation. Lactose, a specific inhibitor of hemagglutination mediated by these lectins was a potent inhibitor of lectin-in

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2

Kothari, Sajani, Rebecca Heineman, and Rene Harrison. "Optimizing Lectin Staining Methodology to Assess Glycocalyx Composition of Legionella-Infected Cells." Undergraduate Research in Natural and Clinical Science and Technology (URNCST) Journal 7, no. 7 (2023): 1–10. http://dx.doi.org/10.26685/urncst.490.

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Introduction: Legionella is a gram-negative bacterium that replicates intracellularly within macrophages. Legionella utilizes effector proteins to hijack ER-Golgi vesicle trafficking to sustain proliferation in its intracellular niche. Legionella has a considerable influence on O-glycosylation but not N-glycosylation events in the Golgi of infected cells. This research aims to optimize the use of fluorescent lectins, which are proteins that bind carbohydrates, to effectively label host-cell glycocalyx during Legionella infection. Methods: Epifluorescence imaging or flow cytometry were used to

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3

Bonnardel, François, Julien Mariethoz, Serge Pérez, Anne Imberty, and Frédérique Lisacek. "LectomeXplore, an update of UniLectin for the discovery of carbohydrate-binding proteins based on a new lectin classification." Nucleic Acids Research 49, no. D1 (2020): D1548—D1554. http://dx.doi.org/10.1093/nar/gkaa1019.

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Abstract Lectins are non-covalent glycan-binding proteins mediating cellular interactions but their annotation in newly sequenced organisms is lacking. The limited size of functional domains and the low level of sequence similarity challenge usual bioinformatics tools. The identification of lectin domains in proteomes requires the manual curation of sequence alignments based on structural folds. A new lectin classification is proposed. It is built on three levels: (i) 35 lectin domain folds, (ii) 109 classes of lectins sharing at least 20% sequence similarity and (iii) 350 families of lectins

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4

Lakhtin, M., V. Lakhtin, V. Alyoshkin, and S. Afanasyev. "Lectins of beneficial microbes: system organisation, functioning and functional superfamily." Beneficial Microbes 2, no. 2 (2011): 155–65. http://dx.doi.org/10.3920/bm2010.0014.

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In this review our last results and proposals with respect to general aspects of lectin studies are summarised and compared. System presence, organisation and functioning of lectins are proposed, and accents on beneficial symbiotic microbial lectins studies are presented. The proposed general principles of lectin functioning allows for a comparison of lectins with other carbohydrate-recognition systems. A new structure-functional superfamily of symbiotic microbial lectins is proposed and its main properties are described. The proposed superfamily allows for extended searches of the biological

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5

Melgarejo, Luz Marina, Nohora Vega, and Gerardo Pérez. "Isolation and characterization of novel lectins from Canavalia ensiformis DC and Dioclea grandiflora Mart. ex Benth. seeds." Brazilian Journal of Plant Physiology 17, no. 3 (2005): 315–24. http://dx.doi.org/10.1590/s1677-04202005000300006.

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Two lectins were isolated from Canavalia ensiformis and Dioclea grandiflora seeds. Gel filtration produced a fraction corresponding to Con A or D. grandiflora lectin while erythroagglutination assays revealed a distinct fraction presenting a lectin that agglutinates human red blood cells (RBCs) but not rabbit RBCs. Hydrophobic interaction chromatography showed that the latter fraction yielded a protein that readily agglutinates human erythrocytes; the lectin was also purified by affinity chromatography on Lac-Sepharose showing similar properties to that of the Phenyl-Sepharose-purified lectin.

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6

Ideo, Hiroko, Akiko Tsuchida, and Yoshio Takada. "Lectin-Based Approaches to Analyze the Role of Glycans and Their Clinical Application in Disease." International Journal of Molecular Sciences 25, no. 18 (2024): 10231. http://dx.doi.org/10.3390/ijms251810231.

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Lectin-based approaches remain a valuable tool for analyzing glycosylation, especially when detecting cancer-related changes. Certain glycans function as platforms for cell communication, signal transduction, and adhesion. Therefore, the functions of glycans are important considerations for clinical aspects, such as cancer, infection, and immunity. Considering that the three-dimensional structure and multivalency of glycans are important factors for their function, their binding characteristics toward lectins provide vital information. Glycans and lectins are inextricably linked, and studies o

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7

Van Holle, Sofie, and Els J. M. Van Damme. "Signaling through plant lectins: modulation of plant immunity and beyond." Biochemical Society Transactions 46, no. 2 (2018): 217–33. http://dx.doi.org/10.1042/bst20170371.

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Lectins constitute an abundant group of proteins that are present throughout the plant kingdom. Only recently, genome-wide screenings have unraveled the multitude of different lectin sequences within one plant species. It appears that plants employ a plurality of lectins, though relatively few lectins have already been studied and functionally characterized. Therefore, it is very likely that the full potential of lectin genes in plants is underrated. This review summarizes the knowledge of plasma membrane-bound lectins in different biological processes (such as recognition of pathogen-derived

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8

Mewe, Marco, Denis Tielker, Robert Schönberg, Melitta Schachner, Karl-Erich Jaeger, and Udo Schumacher. "Pseudomonas aeruginosa lectins I and II and their interaction with human airway cilia." Journal of Laryngology & Otology 119, no. 8 (2005): 595–99. http://dx.doi.org/10.1258/0022215054516313.

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The bacterium Pseudomonas aeruginosa (PA) produces two carbohydrate binding lectins, designated PA lectin-I and lectin-II (PA-IL, PA-IIL). Both lectins are used by the bacterium to adhere to the glycocalyx of mammalian cells. In addition, the lectins immobilize ciliary beat. The kinetics of ciliary beat inhibition by each individual lectin have been analysed; however, their joint action on cilia has not been reported. Here we demonstrate that PA-IL and PA-IIL inhibit ciliary beat in a similar time-dependent manner. If applied simultaneously, ciliary beat inhibition after five hours of incubati

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9

Lesman-Movshovich, Efrat, Batia Lerrer, and Nechama Gilboa-Garber. "Blocking ofPseudomonas aeruginosalectins by human milk glycans." Canadian Journal of Microbiology 49, no. 3 (2003): 230–35. http://dx.doi.org/10.1139/w03-027.

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The opportunistic human pathogen Pseudomonas aeruginosa produces a D-galactophilic (PA-IL) lectin and another lectin (PA-IIL) that binds L-fucose > D-arabinose > D-mannose in close association with its host-attacking factors. These lectins contribute to the virulence of P. aeruginosa by their involvement in the production, adhesion, and pathogenic effects of its biofilm on host cells. Therefore, they are considered targets for anti-Pseudomonas therapy. The present study compares their blocking by human milk samples with that of the plant lectin Con A. It demonstrates that human milk inhi

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10

Coelho, Luana Cassandra Breitenbach Barroso, Priscila Marcelino dos Santos Silva, Vera Lúcia de Menezes Lima, et al. "Lectins, Interconnecting Proteins with Biotechnological/Pharmacological and Therapeutic Applications." Evidence-Based Complementary and Alternative Medicine 2017 (2017): 1–22. http://dx.doi.org/10.1155/2017/1594074.

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Lectins are proteins extensively used in biomedical applications with property to recognize carbohydrates through carbohydrate-binding sites, which identify glycans attached to cell surfaces, glycoconjugates, or free sugars, detecting abnormal cells and biomarkers related to diseases. These lectin abilities promoted interesting results in experimental treatments of immunological diseases, wounds, and cancer. Lectins obtained from virus, microorganisms, algae, animals, and plants were reported as modulators and tool markers in vivo and in vitro; these molecules also play a role in the induction

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11

Gerhardus, M. J. T., J. M. C. Baggen, W. P. W. Van Der Knaap, and T. Sminia. "Analysis of surface carbohydrates of Trichobilharzia ocellata miracidia and sporocysts using lectin binding techniques." Parasitology 103, no. 1 (1991): 51–59. http://dx.doi.org/10.1017/s003118200005928x.

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Miracidia and in vitro-derived primary sporocysts of the avian schistosome Trichobilharzia ocellata were studied for the expression and the characteristics of glycoconjugate moieties comprising the surface coat. Using a panel of 9 peroxidase labelled lectins, several different lectin binding sites were demonstrated on the larvae. Fixed miracidia have binding sites for 7 of the lectins; wheat-germ agglutinin binds to both the ciliated plates and the tegumental ridges between them; the other 6 lectins bind to the plates only. Three of the miracidia-binding lectins, wheat-germ agglutinin, concana

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12

Levine, E., R. Werner, and G. Dahl. "Cell-cell channel formation and lectins." American Journal of Physiology-Cell Physiology 261, no. 6 (1991): C1025—C1032. http://dx.doi.org/10.1152/ajpcell.1991.261.6.c1025.

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The oocyte cell-cell channel assay was used to investigate determinants of the rate of channel formation. After injection of connexin-specific mRNA, oocytes accumulate a pool of precursors from which cell-cell channels can form after oocytes are paired. Channel formation was found to be increased if oocytes are pretreated with lectins before pairing. Several lectins differing in their carbohydrate binding affinities can exert this effect. Lectin-specific sugars suppress the effect on cell-cell channel formation only if the sugar is mixed with the lectin before application to the oocyte. If the

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13

WRIGHT, Lisa M., Els J. M. VAN DAMME, Annick BARRE, et al. "Isolation, characterization, molecular cloning and molecular modelling of two lectins of different specificities from bluebell (Scilla campanulata) bulbs." Biochemical Journal 340, no. 1 (1999): 299–308. http://dx.doi.org/10.1042/bj3400299.

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Two lectins have been isolated from bluebell (Scilla campanulata) bulbs. From their isolation by affinity chromatography, they are characterized as a mannose-binding lectin (SCAman) and a fetuin-binding lectin (SCAfet). SCAman preferentially binds oligosaccharides with α(1,3)- and α(1,6)-linked mannopyranosides. It is a tetramer of four identical protomers of approx. 13 kDa containing 119 amino acid residues; it is not glycosylated. The fetuin-binding lectin (SCAfet), which is not inhibited by any simple sugars, is also unglycosylated. It is a tetramer of four identical subunits of approx. 28

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14

Folowosele, Morenikeji Tolulope, Oludele Olayemi Odekanyin, Adenike Oluwaseun Adefila, Sinaola Praise Oyepitan, Eniola Racheal Owolabi, and Ayomide Ifeoluwa Alobaloye. "Chemical Modification and Denaturation Effects on the Hemagglutinating Activity of Two Pterocarpus Species Seeds Lectins." Chemical Science International Journal 33, no. 3 (2024): 89–99. http://dx.doi.org/10.9734/csji/2024/v33i3896.

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Aims: Pterocarpus osun and Pterocarpus soyauxii seeds lectins were subjected to various chemical modifications in order to detect the amino acid residues involved in their hemagglutinating and sugar-binding activities. Methodology: The lectins were purified using salt precipitation and size exclusion chromatography. Hemagglutinating activity and sugar specificity of the lectins were also established. Chemical modification of arginine was done using phenylglyoxal hydrate, and 5,5- dithiobis-(2-nitrobenzoic acid) (DTNB) was used to modify cysteine. Phenylmethylsulfonyl fluoride (PMSF) was employ

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15

Adamcová, Anežka, Kristian Holst Laursen, and Nicolai Zederkopff Ballin. "Lectin Activity in Commonly Consumed Plant-Based Foods: Calling for Method Harmonization and Risk Assessment." Foods 10, no. 11 (2021): 2796. http://dx.doi.org/10.3390/foods10112796.

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Lectins are ubiquitous proteins characterized through their ability to bind different types of carbohydrates. It is well known that active lectins from insufficiently prepared legumes can cause adverse human health effects. The objective of this study was to determine the activity of lectins in samples across plant families representing commercially available edible plants, and the feasibility of inactivating lectins through soaking and boiling. Lectins were extracted from the plant families Adoxaceae, Amaranthaceae, Cannabaceae, Fabaceae, Gramineae, Lamiaceae, Linaceae, Pedaliaceae, and Solan

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16

Hatakeyama, Tomomitsu, and Hideaki Unno. "Functional Diversity of Novel Lectins with Unique Structural Features in Marine Animals." Cells 12, no. 14 (2023): 1814. http://dx.doi.org/10.3390/cells12141814.

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Due to their remarkable structural diversity, glycans play important roles as recognition molecules on cell surfaces of living organisms. Carbohydrates exist in numerous isomeric forms and can adopt diverse structures through various branching patterns. Despite their relatively small molecular weights, they exhibit extensive structural diversity. On the other hand, lectins, also known as carbohydrate-binding proteins, not only recognize and bind to the diverse structures of glycans but also induce various biological reactions based on structural differences. Initially discovered as hemagglutin

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17

Ahmmed, Mirja Kaizer, Shuva Bhowmik, Stephen G. Giteru, et al. "An Update of Lectins from Marine Organisms: Characterization, Extraction Methodology, and Potential Biofunctional Applications." Marine Drugs 20, no. 7 (2022): 430. http://dx.doi.org/10.3390/md20070430.

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Lectins are a unique group of nonimmune carbohydrate-binding proteins or glycoproteins that exhibit specific and reversible carbohydrate-binding activity in a non-catalytic manner. Lectins have diverse sources and are classified according to their origins, such as plant lectins, animal lectins, and fish lectins. Marine organisms including fish, crustaceans, and mollusks produce a myriad of lectins, including rhamnose binding lectins (RBL), fucose-binding lectins (FTL), mannose-binding lectin, galectins, galactose binding lectins, and C-type lectins. The widely used method of extracting lectins

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18

Arruda, Francisco Vassiliepe Sousa, Arthur Alves Melo, Mayron Alves Vasconcelos, et al. "Toxicity and Binding Profile of Lectins from the GenusCanavaliaon Brine Shrimp." BioMed Research International 2013 (2013): 1–7. http://dx.doi.org/10.1155/2013/154542.

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Lectins are sugar-binding proteins widely distributed in nature with many biological functions. Although many lectins have a remarkable biotechnological potential, some of them can be cytotoxic. Thus, the aim of this study was to assess the toxicity of five lectins, purified from seeds of different species ofCanavaliagenus. In order to determine the toxicity, assays withArtemianauplii were performed. In addition, a fluorescence assay was carried out to evaluate the binding of lectins toArtemianauplii. In order to verify the relationship between the structure of lectins and their cytotoxic effe

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19

Battistella, Roberta, Marios Kritsilis, Hana Matuskova, et al. "Not All Lectins Are Equally Suitable for Labeling Rodent Vasculature." International Journal of Molecular Sciences 22, no. 21 (2021): 11554. http://dx.doi.org/10.3390/ijms222111554.

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The vascular system is vital for all tissues and the interest in its visualization spans many fields. A number of different plant-derived lectins are used for detection of vasculature; however, studies performing direct comparison of the labeling efficacy of different lectins and techniques are lacking. In this study, we compared the labeling efficacy of three lectins: Griffonia simplicifolia isolectin B4 (IB4); wheat germ agglutinin (WGA), and Lycopersicon esculentum agglutinin (LEA). The LEA lectin was identified as being far superior to the IB4 and WGA lectins in histological labeling of bl

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20

Chen, C., H. J. Durrant, R. P. Newton, and N. A. Ratcliffe. "A study of novel lectins and their involvement in the activation of the prophenoloxidase system in Blaberus discoidalis." Biochemical Journal 310, no. 1 (1995): 23–31. http://dx.doi.org/10.1042/bj3100023.

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Endogenous and exogenous lectins have been found to activate the prophenoloxidase (proPO) system of the cockroach, Blaberus discoidalis, to the same extent as laminarin, a previously known microbial activator of proPO. The lectins can also further enhance this laminarin activation of the proPO system. Non-lectin proteins did not display any activation properties. The time course of proPO activation was studied after reconstitution of the reaction system using purified lectins, a trypsin-like enzyme, a trypsin inhibitor and partially purified lectin-binding proteins from the cockroach haemolymp

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21

Tirta Ismaya, Wangsa, Raymond Rubianto Tjandrawinata, and Heni Rachmawati. "Lectins from the Edible Mushroom Agaricus bisporus and Their Therapeutic Potentials." Molecules 25, no. 10 (2020): 2368. http://dx.doi.org/10.3390/molecules25102368.

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The mushroom Agaricus bisporus secretes biologically active compounds and proteins with benefits for human health. Most reported proteins from A. bisporus are tyrosinases and lectins. Lectins are of therapeutic or pharmaceutical interest. To date, only limited information is available on A. bisporus lectins and lectin-like proteins. No therapeutic products derived from A. bisporus lectin (ABL) are available on the market despite its extensive exploration. Recently, A. bisporus mannose-binding protein (Abmb) was discovered. Its discovery enriches the information and increases the interest in pr

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22

Detilleux, P. G., N. F. Cheville, and B. J. Sheahan. "Ultrastructure and Lectin Histochemistry of Equine Cutaneous Histiolymphocytic Lymphosarcomas." Veterinary Pathology 26, no. 5 (1989): 409–19. http://dx.doi.org/10.1177/030098588902600506.

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Tissues from subcutaneous lymphosarcomas and regional lymph nodes were examined by light and electron microscopy and by lectin histochemistry. Tumors were composed of two major cell types: small lymphocytes with few organelles and pleomorphic histiocytic cells with undulant surfaces, large numbers of cytoplasmic vacuoles, and many mitochondria with large crystalline inclusions. A large gram-positive coryneform bacterium was isolated from tumor nodules but was not identified morphologically in tumor tissues. Evaluation of sections of tumors with lectins as histochemical probes revealed three st

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23

Singh, Keerti, Lokita Agrawal, Rhea Gupta, Divyam Singh, Meghavi Kathpalia, and Navkiran Kaur. "Lectins as a promising therapeutic agent for breast cancer: A review." Breast Disease 43, no. 1 (2024): 193–211. http://dx.doi.org/10.3233/bd-230047.

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Efficient treatment of cancer has been a subject of research by scientists for many years. Current treatments for cancer, such as radiotherapy, chemotherapy and surgery have been used in traditional combination therapy, but they have major setbacks like non-specificity, non-responsiveness in certain cancer types towards treatment, tumor recurrence, etc. Epidemiological data has shown that breast cancer accounts for 14% of cancer cases occurring in Indian women. In recent years, scientists have started to focus on the use of natural compounds like lectins obtained from various sources to counte

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24

Barre, Annick, Mathias Simplicien, Hervé Benoist, Els J. M. Van Damme, and Pierre Rougé. "Mannose-Specific Lectins from Marine Algae: Diverse Structural Scaffolds Associated to Common Virucidal and Anti-Cancer Properties." Marine Drugs 17, no. 8 (2019): 440. http://dx.doi.org/10.3390/md17080440.

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To date, a number of mannose-specific lectins have been isolated and characterized from seaweeds, especially from red algae. In fact, man-specific seaweed lectins consist of different structural scaffolds harboring a single or a few carbohydrate-binding sites which specifically recognize mannose-containing glycans. Depending on the structural scaffold, man-specific seaweed lectins belong to five distinct structurally-related lectin families, namely (1) the griffithsin lectin family (β-prism I scaffold); (2) the Oscillatoria agardhii agglutinin homolog (OAAH) lectin family (β-barrel scaffold);

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Lim, Anita WW, André A. Neves, Sarah Lam Shang Leen, et al. "Lectins in Cervical Screening." Cancers 12, no. 7 (2020): 1928. http://dx.doi.org/10.3390/cancers12071928.

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Cervical screening in low-resource settings remains an unmet need. Lectins are naturally occurring sugar-binding glycoproteins whose binding patterns change as cancer develops. Lectins discriminate between dysplasia and normal tissue in several precancerous conditions. We explored whether lectins could be developed for cervical screening via visual inspection. Discovery work comprised lectin histochemistry using a panel of candidate lectins on fixed-human cervix tissue (high-grade cervical intraepithelial neoplasia (CIN3, n = 20) or normal (n = 20)), followed by validation in a separate cohort

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Timoshenko, A. V., S. André, H. Kaltner, X. Dong, and H. J. Gabius. "Generation of H2O2 by Human Neutrophils and Changes of Cytosolic Ca2+ and pH of Rat Thymocytes in Response to Galactoside-Binding Proteins (Lectins or Immunoglobulins)." Bioscience Reports 17, no. 2 (1997): 219–30. http://dx.doi.org/10.1023/a:1027389614391.

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In contrast to plant agglutinins, biological activities of animal/human lectins are not well defined yet. Testing a panel of seven mammalian carbohydrate-binding proteins we have found that the dimeric lectin from chicken liver (CL-16) was a stimulator of H2O2 release from human neutrophils as well as effector for induction of cytosolic Ca2+ and pH increase in rat thymocytes. Activity of this lectin was comparable to potent galactoside-specific plant lectins such as Viscum album L. agglutinin. The activities of the tested plant lectins depended significantly on their nominal carbohydrate speci

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Vrcić, H., B. Horvat, and I. Damjanov. "Lectin histochemistry of mouse vagina during the estrous cycle." Journal of Histochemistry & Cytochemistry 39, no. 12 (1991): 1685–92. http://dx.doi.org/10.1177/39.12.1940320.

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Estrous cycle-related histochemical changes in the vaginal epithelium of sexually mature female mice were studied with 30 fluorescein isothiocyanate (FITC)-labeled lectins. On the basis of the staining pattern the lectins were divided into five groups: I, seventeen lectins that reacted with mucinous surface layer of proestrus. This group comprised two subgroups: Ia, seven lectins that reacted exclusively with the mucinous layer, and Ib, ten lectins that reacted with mucinous cells and the underlying squamous epithelium of proestrus; II, two lectins that reacted with squamous epithelium of proe

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Chikalovets, Irina, Alina Filshtein, Valentina Molchanova, et al. "Activity Dependence of a Novel Lectin Family on Structure and Carbohydrate-Binding Properties." Molecules 25, no. 1 (2019): 150. http://dx.doi.org/10.3390/molecules25010150.

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A GalNAc/Gal-specific lectins named CGL and MTL were isolated and characterized from the edible mussels Crenomytilus grayanus and Mytilus trossulus. Amino acid sequence analysis of these lectins showed that they, together with another lectin MytiLec-1, formed a novel lectin family, adopting β-trefoil fold. In this mini review we discuss the structure, oligomerization, and carbohydrate-binding properties of a novel lectin family. We describe also the antibacterial, antifungal, and antiproliferative activities of these lectins and report about dependence of activities on molecular properties. Su

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Raposo, Cláudia D., André B. Canelas, and M. Teresa Barros. "Human Lectins, Their Carbohydrate Affinities and Where to Find Them." Biomolecules 11, no. 2 (2021): 188. http://dx.doi.org/10.3390/biom11020188.

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Lectins are a class of proteins responsible for several biological roles such as cell-cell interactions, signaling pathways, and several innate immune responses against pathogens. Since lectins are able to bind to carbohydrates, they can be a viable target for targeted drug delivery systems. In fact, several lectins were approved by Food and Drug Administration for that purpose. Information about specific carbohydrate recognition by lectin receptors was gathered herein, plus the specific organs where those lectins can be found within the human body.

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C. Torres, Jose, Jose G. Hernandez, Edwin C. Hernandez, et al. "EVALUATION OF ANOMERICRECOGNITION IN GALACTOSE BINDING LECTINS USING CROSSLINKED HEMICELLULOSE: A COMPARATIVE STUDY THROUGH AFFINITY CHROMATOGRAPHY." International Journal of Advanced Research 9, no. 07 (2021): 391–400. http://dx.doi.org/10.21474/ijar01/13138.

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The isolation of lectins by affinity chromatography with crosslinked hemicelluloses has been a common practice because of the variety of glycosides that they present, improving the isolation of different kinds of lectins, such as the galactose ligands.Lectins affinity for carbohydrates is so specific that a simple configuration of the chiral carbon can affect affinity, and there are lectins that are more related to alfa-galactosidic than beta-galactosidic residues, setting up that way, an anomeric recognition.The anomeric configuration of galactose residuesseems to have biological importance r

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Ramiro-Diaz, Juan, Alma Barajas-Espinosa, Erika Chi-Ahumada, et al. "Luminal endothelial lectins with affinity for N-acetylglucosamine determine flow-induced cardiac and vascular paracrine-dependent responses." American Journal of Physiology-Heart and Circulatory Physiology 299, no. 3 (2010): H743—H751. http://dx.doi.org/10.1152/ajpheart.00790.2009.

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Coronary blood flow applied to the endothelial lumen modulates parenchymal functions via paracrine effectors, but the mechanism of flow sensation is unknown. We and others have demonstrated that coronary endothelial luminal membrane (CELM) oligosaccharides and lectins are involved in flow detection, and we proposed that cardiac effects of coronary flow result from a reversible flow-modulated lectin-oligosaccharide interaction. Recently, glycosylated and amiloride-sensitive Na+/Ca++ channels (ENaCs) have been proposed to be involved in the flow-induced endothelial responses. Because N-acetylglu

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Rauschenberg, Melanie, Eva-Corrina Fritz, Christian Schulz, Tobias Kaufmann, and Bart Jan Ravoo. "Molecular recognition of surface-immobilized carbohydrates by a synthetic lectin." Beilstein Journal of Organic Chemistry 10 (June 16, 2014): 1354–64. http://dx.doi.org/10.3762/bjoc.10.138.

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The molecular recognition of carbohydrates and proteins mediates a wide range of physiological processes and the development of synthetic carbohydrate receptors (“synthetic lectins”) constitutes a key advance in biomedical technology. In this article we report a synthetic lectin that selectively binds to carbohydrates immobilized in a molecular monolayer. Inspired by our previous work, we prepared a fluorescently labeled synthetic lectin consisting of a cyclic dimer of the tripeptide Cys-His-Cys, which forms spontaneously by air oxidation of the monomer. Amine-tethered derivatives of N-acetyln

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Thurston, G., P. Baluk, A. Hirata, and D. M. McDonald. "Permeability-related changes revealed at endothelial cell borders in inflamed venules by lectin binding." American Journal of Physiology-Heart and Circulatory Physiology 271, no. 6 (1996): H2547—H2562. http://dx.doi.org/10.1152/ajpheart.1996.271.6.h2547.

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Plasma leakage in inflammation results from intercellular gaps that form in the endothelium of venules. These gaps and related morphological changes in endothelial cells are not readily seen by light microscopy. In this study we sought to visualize such changes by using the selective binding properties of plant lectins. Acute inflammation was induced in the trachea of pathogen-free F344 rats by injecting substance P intravenously, and 1, 3, or 10 min later the vasculature was perfused with fixative followed by a biotinylated lectin. Lectin binding was localized by avidinbiotin complex-peroxida

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Kumar, Pawan. "Novel Insights into Lectin Binding Patterns in the Nasopharyngeal Tonsil of Buffaloes (Bubalus bubalis)." Journal of Buffalo Science 14 (March 30, 2025): 50–64. https://doi.org/10.6000/1927-520x.2025.14.06.

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Background: The present study investigates the specificity of lectin binding in the nasopharyngeal tonsil of six healthy adult buffaloes (Bubalus bubalis), a species not extensively studied regarding its immune system. Lectins, proteins that bind specifically to carbohydrates, are used to identify and characterize different cell types that may have roles in immune responses. This study explores how lectins bind to various cells within the nasopharyngeal tonsil, shedding light on cellular differentiation, interactions, and the potential functional roles of these cells in mucosal immunity. Metho

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35

Colyer, J., M. J. G. Farthing, P. J. Kumar, M. L. Clark, A. D. Ohannesian, and N. M. Waldron. "Reappraisal of the ‘lectin hypothesis' in the aetiopathogenesis of coeliac disease." Clinical Science 71, no. 1 (1986): 105–10. http://dx.doi.org/10.1042/cs0710105.

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1. The agglutinating properties of a crude gluten digest, purified gliadin fractions and established plant lectins were investigated using mammalian erythrocytes, rat enterocytes and normal and coeliac human enterocytes as the target systems. 2. Gliadin preparations failed to cause agglutination of any of the cells tested, whereas established pure plant lectins were active cell agglutinins. 3. These studies indicate that gliadin peptides do not interact with intestinal cells in a polyvalent, lectin-like manner and as such cannot be regarded as true lectins. 4. Mucosal damage in coeliac disease

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Ferreira, Hugo Jefferson, Evandro Moreira de Almeida, Wildson Max Barbosa da Silva, Edson Holanda Teixeira, and Luiz Gonzaga do Nascimento Neto. "Molecular Mechanisms Involved in the Antitumor Activity of Isolated Lectins from Marine Organisms: A Systematic Review." Current Drug Targets 21, no. 6 (2020): 616–25. http://dx.doi.org/10.2174/1389450120666191122113850.

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Introduction: Tumor cells may present several molecular alterations that favor their malignancy, among which there is the expression of tumor-related antigens, such as truncated T-glycans, Thomsen-nouvelle, sialyl-Lewis X and sialyl Tn, which may help in the diagnosis and treatment using specific target molecules. Lectins are ubiquitous proteins capable of interacting with specific carbohydrates. Lectins isolated from marine organisms have important characteristics such as low immunogenicity and can bind to complex glycans compared to plant lectins. Objective: This work evaluated, through a sy

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Rodrigues, Éllen F., Flavia Alves Verza, Felipe Garcia Nishimura, et al. "Exploring the Structural Diversity and Biotechnological Potential of the Rhodophyte Phycolectome." Marine Drugs 23, no. 1 (2024): 8. https://doi.org/10.3390/md23010008.

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Lectins are non-covalent glycan-binding proteins found in all living organisms, binding specifically to carbohydrates through glycan-binding domains. Lectins have various biological functions, including cell signaling, molecular recognition, and innate immune responses, which play multiple roles in the physiological and developmental processes of organisms. Moreover, their diversity enables biotechnological exploration as biomarkers, biosensors, drug-delivery platforms, and lead molecules for anticancer, antidiabetic, and antimicrobial drugs. Lectins from Rhodophytes (red seaweed) have been ex

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Chen, Pengyu, Kristof De Schutter, Els J. M. Van Damme, and Guy Smagghe. "Can Plant Lectins Help to Elucidate Insect Lectin-Mediated Immune Response?" Insects 12, no. 6 (2021): 497. http://dx.doi.org/10.3390/insects12060497.

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Lectins are carbohydrate-binding proteins that recognize and selectively bind to specific sugar structures. This group of proteins is widespread in plants, animals, and microorganisms, and exerts a broad range of functions. Many plant lectins were identified as exogenous stimuli of vertebrate immunity. Despite being the largest and most diverse taxon on earth, the study of lectins and their functions in insects is lagging behind. In insects, research on lectins and their biological importance has mainly focused on the C-type lectin (CTL) family, limiting our global understanding of the functio

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Ooi, Linda SM, Hexiang Wang, T. B. Ng, and Vincent EC Ooi. "Isolation and characterization of a mannose-binding lectin from leaves of the Chinese daffodil Narcissus tazetta." Biochemistry and Cell Biology 76, no. 4 (1998): 601–8. http://dx.doi.org/10.1139/o98-022.

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A mannose-binding lectin was isolated from leaves of the Chinese daffodil Narcissus tazetta (family Amaryllidaceae) using a procedure that comprised extraction with aqueous buffer, ammonium sulfate precipitation, ion exchange chromatography on DEAE-cellulose, affinity chromatography on Affi-gel Blue gel and mannose-agarose, and FPLC-gel filtration on Superose 12. The lectin was adsorbed on mannose-agarose and unadsorbed on DEAE-cellulose and Affi-gel Blue gel. It was an unglycosylated homodimer with a molecular mass of 26 kDa. Analysis of the N-terminal sequence of the N. tazetta lectin reveal

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40

Lakhtin, M. V., V. M. Lakhtin, A. Yu Mironov, V. A. Aleshkin, S. S. Afanasyev, and S. Yu Kombarova. "The Potential of Lectins and their Recognized Glycoconjugates in the Human Body." Успехи современной биологии 144, no. 1 (2024): 3–25. http://dx.doi.org/10.31857/s0042132424010015.

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The modern concepts of lectins and glycoconjugates binding to them, the features and patterns of their interaction, the protective role and potential in the human body are summarized. The analysis of terms, approaches to classifications of lectins is carried out. The features of natural and synthetic glycoconjugates, recognized and bound by lectins, in symbiotic relationships, in innate immunity at the reception level are emphasized. The levels of specificity of lectins are considered. There is a need to expand research on the glycoconjugate specificity of lectins and their systems, to assess

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GRUBHOFFER, L., V. KOVÁŘ, and N. RUDENKO. "Tick lectins: structural and functional properties." Parasitology 129, S1 (2004): S113—S125. http://dx.doi.org/10.1017/s0031182004004858.

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Few papers have been published on tick lectins so far, and therefore more data are needed to complete the mosaic of knowledge of their structural and functional properties. Tissue-specific lectin/haemagglutinin activities of both soft and hard ticks have been investigated. Some tick lectins are proteins with binding affinity for sialic acid, various derivatives of hexosamines and different glycoconjugates. Most tick lectin/haemagglutinin activities are blood meal enhanced, and could serve as molecular factors of self/non-self recognition in defence reactions against bacteria or fungi, as well

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Singh, Ram, and Amandeep Walia. "Antioxidant and antimicrobial activities of Penicillium sp. lectins." Archives of Biological Sciences 71, no. 3 (2019): 517–24. http://dx.doi.org/10.2298/abs190529035s.

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Lectins are a diverse group of proteins of non-immune origin that interact specifically with glycans. Owing to their specificity, they can mediate various cellular and molecular recognition processes. To explore information on biological activities of lectins from Penicillium duclauxii, P. proteolyticum and P. griseoroseum, they were investigated for their antioxidant and antimicrobial activities. Penicillium sp. lectins exhibited moderate antioxidant activity. P. duclauxii, P. proteolyticum and P. griseoroseum lectins inhibited DPPH with an IC50 value of 71.42, 75.04 and 82.11 ?g/mL, respecti

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Abdulina, D. R., L. M. Purish, and G. O. Iutynska. "Specificity of Lectins Labeled with Colloidal Gold to the Exopolymeric Matrix Carbohydrates of the Sulfate-Reducing Bacteria Biofilm Formed on Steel." Mikrobiolohichnyi Zhurnal 82, no. 5 (2020): 11–20. http://dx.doi.org/10.15407/microbiolj82.05.011.

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The studies of the carbohydrate composition of the sulfate-reducing bacteria (SRB) biofilms formed on the steel surface, which are a factor of microbial corrosion, are significant. Since exopolymers synthesized by bacteria could activate corrosive processes. The aim of the study was to investigate the specificity of commercial lectins, labeled with colloidal gold to carbohydrates in the biofilm exopolymeric matrix produced by the corrosive-relevant SRB strains from man-caused ecotopes. Methods. Microbiological methods (obtaining of the SRB biofilms during cultivation in liquid Postgate B media

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Michael Stanley, C., and Thomas E. Phillips. "Sequential staining and de-staining of a single section by a panel of fluorescently-tagged lectins." Proceedings, annual meeting, Electron Microscopy Society of America 53 (August 13, 1995): 1054–55. http://dx.doi.org/10.1017/s0424820100141640.

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Numerous previous studies have used fluorescently tagged lectins to demonstrate the mucin glycoprotein secretory product of intestinal goblet cells are heterogeneous in respect to their lectin binding sites . Lectins stain the mucin secretory product in partially overlapping subpopulations of goblet cells. There are several difficulties in using a panel of fluorescently tagged lectins to determine the overlapping sites of binding. First, steric hindrances resulting from the binding of the first lectin compete with the subsequent binding of other lectins to the same or adjacent sites. Secondly,

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45

Lauc, Gordan, Mirna Flögel, and Werner E. G. Müller. "Biotinylated Carbohydrate Markers -A Novel Tool for Lectin Research." Zeitschrift für Naturforschung C 49, no. 11-12 (1994): 843–48. http://dx.doi.org/10.1515/znc-1994-11-1220.

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One of the key obstacles in lectin research is the lack of specific techniques for their detection. Novel markers, biotin-labeled carbohydrates, could contribute to overcome this problem. Being at least 10 times more sensitive than neoglycoproteins in the membranescreening assays, they also enable direct detection of lectins in complex mixtures. The markers were synthesized by linking biotin to one, and a carbohydrate (galactose or glucose) to the other amino group of (the amino acid) lysine. After synthesis the markers were chromatographically purified on lectin (RCA for galactose marker, Con

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Yogitha, N. sagar. "Characterisation of Lectin from Pisum sativum and Agaricus bisporus and their Immunomodulatory Effects on Earthworm Coelomocytes (Immunomodulatory studies)." International Journal of Innovative Science and Research Technology 7, no. 3 (2022): 511–19. https://doi.org/10.5281/zenodo.6400167.

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:- The paper is focused on lectin characterisation from Pisum sativum and Agaricus bisporous by different experimental methods and assays such as antimicrobial effect, Haemagglutination and Sugar specificity. Lectins recognise cellular and molecular moieties and attach them by their sugar specificity. These are highly specific to carbohydrate moieties and the binding is reversible. Invertebrate system sample was taken to check the immunomodulatory effect of lectins. Trypan blue test for cell viability and catalase assay for antioxidant mechanism were assessed in this respect. And presence of l

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Krotkiewska, Bozena, Marta Pasek, and Hubert Krotkiewski. "Interaction of glycophorin A with lectins as measured by surface plasmon resonance (SPR)." Acta Biochimica Polonica 49, no. 2 (2002): 481–90. http://dx.doi.org/10.18388/abp.2002_3807.

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Glycophorin A (GPA), the major sialoglycoprotein of the human erythrocyte membrane, was isolated from erythrocytes of healthy individuals of blood groups A, B and O using phenol-water extraction of erythrocyte membranes. Interaction of individual GPA samples with three lectins (Psathyrella velutina lectin, PVL; Triticum vulgaris lectin, WGA and Sambucus nigra I agglutinin SNA-I) was analyzed using a BIAcore biosensor equipped with a surface plasmon resonance (SPR) detector. The experiments showed no substantial differences in the interaction between native and desialylated GPA samples originat

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Khan, Farha, Devanshu Kurre та K. Suguna. "Crystal structures of a β-trefoil lectin from Entamoeba histolytica in monomeric and a novel disulfide bond-mediated dimeric forms". Glycobiology 30, № 7 (2020): 474–88. http://dx.doi.org/10.1093/glycob/cwaa001.

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Abstract β-Trefoil lectins are galactose/N-acetyl galactosamine specific lectins, which are widely distributed across all kingdoms of life and are known to perform several important functions. However, there is no report available on the characterization of these lectins from protozoans. We have performed structural and biophysical studies on a β-trefoil lectin from Entamoeba histolytica (EntTref), which exists as a mixture of monomers and dimers in solution. Further, we have determined the affinities of EntTref for rhamnose, galactose and different galactose-linked sugars. We obtained the cry

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Szydlak, Renata, Ingrid H. Øvreeide, Marcin Luty, et al. "Bladder Cancer Cells Interaction with Lectin-Coated Surfaces under Static and Flow Conditions." International Journal of Molecular Sciences 24, no. 9 (2023): 8213. http://dx.doi.org/10.3390/ijms24098213.

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Aberrant expression of glycans, i.e., oligosaccharide moiety covalently attached to proteins or lipids, is characteristic of various cancers, including urothelial ones. The binding of lectins to glycans is classified as molecular recognition, which makes lectins a strong tool for understanding their role in developing diseases. Here, we present a quantitative approach to tracing glycan–lectin interactions in cells, from the initial to the steady phase of adhesion. The cell adhesion was measured between urothelial cell lines (non-malignant HCV29 and carcinoma HT1376 and T24 cells) and lectin-co

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Carter, Mariama D., Tuan M. Tran, Matthew L. Cope-Arguello, et al. "Lectins and polysaccharide EPS I have flow-responsive roles in the attachment and biofilm mechanics of plant pathogenic Ralstonia." PLOS Pathogens 20, no. 9 (2024): e1012358. http://dx.doi.org/10.1371/journal.ppat.1012358.

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Bacterial biofilm formation and attachment to hosts are mediated by carbohydrate-binding lectins, exopolysaccharides, and their interactions in the extracellular matrix (ECM). During tomato infection Ralstonia pseudosolanacearum (Rps) GMI1000 highly expresses three lectins: LecM, LecF, and LecX. The latter two are uncharacterized. We evaluated the roles in bacterial wilt disease of LecF, a fucose-binding lectin, LecX, a xylose-binding lectin, and the Rps exopolysaccharide EPS I. Interestingly, single and double lectin mutants attached to tomato roots better and formed more biofilm under static

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