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PubMed1982

Interactions of lectins with CHO cell surface membranes. I. Competition studies indicate concanavalin a and WGA bind to discrete populations of sites.

The binding of radioiodinated lectins to the CHO cell surface was measured for the following affinity purified plant agglutinins; concanavalin A, wheat germ agglutinin, Ricinus agglutinins (I, II) pea agglutinin, peanut agglutinin, and Bandeiria simpliciafolia agglutinin (BSLI). The number of binding sites at saturation ranged from 6 x 10(5) for BSL I to 5 x 10(7) for pea and Ricinus. Affinity constants calculated by the Steck-Wallach procedure ranged form 2 x 10(5) m(-1) for pea lectin to 4.5 x 10(5) M(-1) L for peanut lectin. Competition studies between homologous and heterologous radiolabeled and unlabeled lectins indicated that homologous unlabeled lectin could fully block binding of radiolabeled lectin. For heterologous pairs, a variety of results were observed. Of particular interest is the finding that concanavalin A and wheat germ agglutinin mutually failed to compete for binding indicating that these two lectins bind to distinct, nonoverlapping populations of surface sites. This finding suggests that the binding sites for WGA and Con A reside, for the most part, on discrete populations of membrane molecules; this concept is further validated in a companion paper in the upcoming issue of this journal (Schwartz et al., 1982).

Animals↗
PubMed1976

Life cycle patterns and their genetic control: an attempt to reconcile evolutionary and mechanistic speculation.

A model is proposed which implicates molecular recognition systems as the major controlling factors in life cycle expression. It is envisaged that such systems are important in immune functioning and catabolic, metabolic molecule recognition at both inter- and intra-cellular level. These recognition systems have the following characteristics: 1) Specific recognition molecules (recognisers), e.g. vertebrate antibodies, invertebrate agglutinins and plant agglutinins may recognise specific substances, e.g. antigens, catabolic and metabolic molecules. 2) The range of possible recognisable substances is very wide and variable. 3) The recognisers may themselves be recognised by other recognisers. 4) Recognisers are usually produced in large amounts only on presentation of the appropriate recognisable molecule. 5) The progressive introduction of new recognisable molecules increases the recogniser interaction, this interaction causing depression of some recogniser types (immune depression) and facilitation of other types among which may be recognisers specific for self components (e.g. auto-immunity). 6) Low juvenile viability is associated with a restricted range of available recognisers, high adult viability with increasing recogniser range and some auto-immunity/immune depression, senescence with a wide range of available recognisers and extensive auto-immunity/immune depression. Life cycle patterns and their control are discussed. It is suggested control mechanisms may include: 1) Dietary restriction and in some periods complete nutritional abstinence. 2) Specific recogniser depression, genes implicated here are the various antigens (species and polymorphic) found on cell surfaces, in the serum and in various body fluids of vertebrates, e.g. ABO, MNSs, P, Rh, Le and other blood groups, the ABO and Le secretor antigens and the HL-A antigens. In addition the immune response and mixed lymphocyte culture loci are implicated. Finally life cycle control is discussed with relation to sexual selection.

Aging↗
PubMed1987

Occurrence and characterization of lympho-agglutinins in Indian plants.

Lympho-agglutinins have been detected and characterized in 31 plant species. Out of these, 14 agglutinated only the neuraminidase-treated cells. The lectin-rich genera included Crotalaria and Erythrina (Fabaceae), Amaranthus (Amaranthaceae), Artocarpus (Moraceae) and Clerodendron (Verbenaceae). The new lectins varied in their potency and biological action spectra. The 3 Artocarpus species were found to be exceptionally potent and specific for melibiose, an alpha-D-galactoside. Among the most effective sugar inhibitors for other lectins were N-acetyl-galactosamine, lactose, galactose and asialofetuin/fetuin.

Animals↗
PubMed1983

Cytochemical localization of small intestinal glycoconjugates by lectin histochemistry in controls and subjects with cystic fibrosis.

Human mucosal glycoconjugates were examined in normal small intestinal biopsies from five control subjects using six different fluorescein-conjugated lectins: Triticum vulgare agglutinin (WGA), Ulex europaeus agglutinin I (UEA1), Ricinus communis agglutinin I (RCA1), glycin max-soy bean agglutinin (SBA), Dolichus biflorus agglutinin (DBA), and Arachis hypogaea peanut agglutinin (PNA). These plant agglutinins bind to specific nonreducing end-terminal carbohydrate residues. Only the lectins derived from WGA, which produced the strongest staining, and UEA1 consistently bound to both intestinal goblet cell mucin and epithelial cell microvillar membranes. The intensity of lectin binding was greatest in the upper villus and diminished down towards the crypt, being weakest in the crypt base. Similar histochemical studies carried out on small bowel biopsies from five patients with cystic fibrosis revealed no major qualitative differences between the intestinal glycoconjugates in normal subjects and those with cystic fibrosis. These results suggest that glycoconjugate biosynthesis of human intestinal goblet cell mucin and epithelial cell membranes may be complete and hence full differentiation achieved only when these cells have migrated out of the crypt and onto the villus.

Biopsy↗
PubMed2003

Relationships between degree of binding, cytotoxicity and cytoagglutinating activity of plant-derived agglutinins in normal lymphocytes and cultured leukemic cell lines.

PURPOSE: To clarify the relationships between the degree of lectin-cell binding, cytotoxicity and cytoagglutinating activity of plant-derived lectins in normal lymphocytes and cultured leukemic cell lines. METHODS: Plant lectins with different quaternary structures and saccharide specificity were used: Dolichos biflorus agglutinin (DBA), Soybean agglutinin (SBA) and Wheat germ agglutinin (WGA). The leukemic cell lines used were: Jurkat, MOLT-4, RPMI-8402, HPB-ALL, CCR-HSB-2 and BALL-1 (derived from acute lymphoblastic leukemia); Raji and Daudi (derived from Burkitt's lymphoma); K-562 (derived from myelogenous leukemia). The lectin-cell binding was detected microscopically and fluorimetrically using FITC-conjugated lectins. Cytotoxicity was estimated by the CellTiter-Glo luminescent cell viability assay, and cytoagglutinating activity by a spectrophotometric method. RESULTS: The binding of DBA and SBA to normal lymphocytes was negligible, while their binding to leukemic cells increased markedly with increasing lectin concentration. Analogous results were obtained for WGA. However, it was found that WGA also interacted to a significant degree with normal lymphocytes. The degree of lectin-cell binding increased in the order: DBA<SBA<WGA. The cytoagglutinating activity and cytotoxicity of lectins increased in the same order. DBA did not exhibit a cytotoxic effect against normal or leukemic cells, and showed a poor cytoagglutinating activity only in MOLT-4, CCR-HSB-2 and BALL-1 cells. SBA exhibited poor cytotoxicity against Jurkat, RPMI-8402, HPB-ALL and CCR-HSB-2 cells, but a well-defined cytotoxicity against Raji and Daudi cells. SBA showed poor cytoagglutinating activity in leukemic cells. In contrast, WGA at concentrations higher than 0.05 microM showed high cytotoxicity against all leukemic cell lines tested as well as against normal lymphocytes. WGA also showed a well-expressed cytoagglutinating effect in all cell lines except normal lymphocytes. There was a moderate inverse correlation between cell viability and the velocity of cytoagglutination ( r=-0.56, P<0.001), and a good correlation between cell viability and the degree of lectin-cell binding ( r=-0.75, P<0.001). There was a low positive correlation between the velocity of cytoagglutination and the degree of lectin-cell binding ( r=0.43, P<0.001). CONCLUSION: The results suggest that the lectins that bound most strongly to leukemic cells expressed higher cytotoxic and cytoagglutinating activities.

Agglutination↗
PubMed1999

Lactose-containing starburst dendrimers: influence of dendrimer generation and binding-site orientation of receptors (plant/animal lectins and immunoglobulins) on binding properties.

Starburst glycodendrimers offer the potential to serve as high-affinity ligands for clinically relevant sugar receptors. In order to define areas of application, their binding behavior towards sugar receptors with differential binding-site orientation but identical monosaccharide specificity must be evaluated. Using poly(amidoamine) starburst dendrimers of five generations, which contain the p-isothiocyanato derivative of p-aminophenyl-beta-D-lactoside as ligand group, four different types of galactoside-binding proteins were chosen for this purpose, i.e., the (AB)(2)-toxic agglutinin from mistletoe, a human immunoglobulin G fraction, the homodimeric galectin-1 with its two binding sites at opposite ends of the jelly-roll-motif-harboring protein and monomeric galectin-3. Direct solid-phase assays with surface-immobilized glycodendrimers resulted in obvious affinity enhancements by progressive core branching for the plant agglutinin and less pronounced for the antibody and galectin-1. High density of binding of galectin-3 with modest affinity increases only from the level of the 32-mer onwards points to favorable protein-protein interactions of the monomeric lectin and a spherical display of the end groups without a major share of backfolding. When the inhibitory potency of these probes was evaluated as competitor of receptor binding to an immobilized neoglycoprotein or to asialofetuin, a marked selectivity was detected. The 32- and 64-mers were second to none as inhibitors for the plant agglutinin against both ligand-exposing matrices and for galectin-1 on the matrix with a heterogeneous array of interglycoside distances even on the per-sugar basis. In contrast, a neoglycoprotein with the same end group was superior in the case of the antibody and, less pronounced, monomeric galectin-3. Intimate details of topological binding-site presentation and the ligand display on different generations of core assembly are major operative factors which determine the potential of dendrimers for applications as lectin-targeting device, as attested by these observations.

Animals↗
PubMed2001

Modulation of interleukin-15-induced human neutrophil responses by the plant lectin Viscum album agglutinin-I.

The plant lectin Viscum album agglutinin-I (VAA-I) and the interleukin-15 (IL-15) cytokine are two molecules with potential therapeutic properties known to modulate neutrophil functions when used separately. This study was conducted in order to better understand the mode of action of VAA-I and to elucidate how VAA-I could modulate IL-15-induced neutrophil responses. We found that VAA-I cannot induce phosphorylation events in human neutrophils. However, it enhances phagocytosis by itself without altering IL-15-induced phagocytosis. VAA-I was found to reverse the ability of IL-15 to delay neutrophil apoptosis and this was correlated with an inhibition of IL-15-induced de novo protein synthesis. In addition, we also found that IL-15 cannot reverse or attenuate the caspase-induced gelsolin fragmentation observed during apoptosis as assessed by immunoblotting. We conclude that VAA-I can be used to modulate some, but not all, IL-15-induced neutrophil responses and that it acts independent of phosphorylation events.

Adjuvants, Immunologic↗
PubMed1982

Occurrence and characterization of lympho-agglutinins in Indian plants.

A survey of the occurrence of lympho-agglutinins was carried out on seeds of 150 species of wild and cultivated plants. Potent agglutinins were detected in 17 extracts by employing lymphocytes of man, guinea pig, goat and sheep in the bioassay. Except for one species each of Mimosoideae, Euphorbiaceae and Clusiaceae, all the agglutinins were found in fabaceous seeds. Two of the agglutinins, namely, Parkia biglandulosa and Erythrina arborescens, were found to be monospecific for guinea pig and human lymphocytes, respectively, while the others agglutinated lymphocytes of 2-4 different species. The agglutination inhibition tests revealed the predominance of galactose (or its derivatives) binding lectins over those specific for glucose-mannose series.

Acetylgalactosamine↗
PubMed1975

Wheat germ agglutinin and Ticinus communis agglutinin as specific saccharide stains in light and electron microscopy.

Two plant agglutinins, wheat germ agglutinin and Ricinus communis agglutinin, were used for light and electron microscopic detection of certain carbohydrate-containing cell surface components and extracellular polysaccharides. For light microscopic studies on various tissues fluorescein isothiocyanate coupled lectins were prepared. The ferritin coupling of the lectins for electron microscopy was performed by glutarldehyde in the presence of the specific hapten. The specificity of the reactions was demonstrated by blocking with the hapten.

Antibody Formation↗
PubMed1997

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).

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 specificity as well as on the source. The results indicate that endogenous lectins may be involved in the regulation of neutrophil and lymphocyte functions by elicitation of selective biosignaling reactions.

Amiloride↗
PubMed1980

Lectin-like activity from Persea americana.

An extract from the seeds of Persea americana possessed an erythro-agglutinating activity. The agglutinin was devoid of specificity for carbohydrates, but interacted readily with basic proteins or basic polyamino acids. The interaction between the agglutinin and egg-white lysozyme was not inhibited by chaotropic salts, but was sensitive to relatively low concentrations of urea. An affinity chromatographic procedure was developed in an effort to purify the agglutinin. Products from the chromatographic procedure were found not to contain higher specific agglutinating activities than the crude extract. Amino acid acid analyses of the extract showed the presence of relatively high proportions of glutamic and aspartic acids. In addition, the extract contained phosphorus and a visible chromophore. The agglutinin was resistant to detergents and denaturants, and proteases, nucleases, and other enzymes. The results suggest that, as opposed to other plant agglutinins, the active component from Persea is not a protein. Similarly, in contrast to many lectins, the agglutinin from Persea was not mitogenic for mouse lymphocytes. The agglutinin partially inhibited the mitogenesis of lymphocytes when the cells were treated with concanavalin A, or with bacterial lipopolysaccharide.

ABO Blood-Group System↗
PubMed1976

A new agglutinating activity from wheat flour inhibited by tryptophan.

A new compound endowed with agglutinating activity, designated the flour agglutinin, was extracted from wheat flour with water and purified by gel filtration and ion-exchange chromatography. The haptenic inhibitors of the plant agglutinins do not affect flour agglutinin activity which, on the other hand, is inhibited by D- and L-tryptophan. Flour agglutinin has a molecular weight of about 5 - 10(4) as determined by gel filtration. It consists of a neutral heteropolysaccharide constituted of D-xylose and L-arabinose, and is homogeneous as judged by sedimentation analysis. Flour agglutinin activity is destroyed by treatment with Cellulase 2000 and periodate, but is not affected by alpha-amylase and proteolytic enzymes. Compared to germ agglutinin, flour agglutinin exhibits a peculiar range of cell specificity. It agglutinates several normal cell types, but has no effects on some neoplastic cells tested. Tryptic digestion of erythrocytes does not affect their susceptibility to flour agglutinin-induced agglutination.

Agglutination Tests↗