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PubMed1972

Chemical characterization and surface orientation of the major glycoprotein of the human erythrocyte membrane.

The major glycoprotein of the human erythrocyte membrane has been isolated by treatment with lithium di-iodosalicylate and found to be a single polypeptide chain with a molecular weight of about 50,000. This molecule, which is 60% carbohydrate and 40% protein, carries multiple blood-group antigens, the receptors for influenza viruses, and various plant agglutinins. Four unique carbohydrate-containing peptides (alpha-1, alpha-2, alpha-3, and beta) are produced by tryptic digestion of the isolated glycoprotein; their order in the molecule has been determined by sequential tryptic digestion of intact erythrocyte membranes and partially digested glycoprotein fragments. Cleavage of the native protein with cyanogen bromide produces five fragments; two of these (C-5 and C-1) contain most of the carbohydrate in the molecule and are derived from the N-terminal half of the polypeptide chain. The nonpolar amino acids of this glycoprotein are located predominantly in the C-terminal fragment (C-2). Phytohemagglutinin conjugated to ferritin has been used to map the distribution of glycoprotein receptors over the surfaces of intact erythrocytes by freeze-etching and electron microscopy. This label localizes to sites on the membrane that overlie the intramembranous particles. These findings suggest that the glycoprotein is oriented at the cell surface with its oligosaccharide-rich N-terminal end exposed to the exterior, while its C-terminal segment interacts with other components in the interior of the membrane to form intramembranous particles.

Amino Acids↗
PubMed1979

Inhibition of human neuroblastoma DNA polymerase activities by plant lectins and toxins.

The effects of concanavalin A and ricin (RCAII, Mr 65,000) on [3H]thymidine incorporation into human neuroblastoma IMR-32 DNA showed reduction of total DNA synthesis to 50% and 70% of control, respectively. Two DNA polymerase (DNA nucleotidyltransferase, EC 2.7.7.7.) activities (alpha and beta) involved in the biosynthesis in vitro of DNA were separated by sucrose density gradient centrifugation from IMR-32 cell homogenate. The DNA polymerase alpha activity was also purified by selective precipitation with polyethylene glycol (Mr 6000) followed by agarose-concanavalin A column chromatography. The activities of both DNA polymerases were examined at various concentrations of mutagenic and nonmutagenic plant agglutinins and the toxin ricin. Concanavalin A and ricin specifically inhibited DNA polymerase alpha activity (activity reduced to 19% and 10%, respectively), whereas DNA polymerase beta activity was inhibited (reduced to 16%) by red kidney bean agglutinin (PHA-P).

Cell Line↗
PubMed1977

Isolation of mammalian tRNAAsp and tRNATyr by lectin-Sepharose affinity column chromatography.

tRNAAsp from rabbit liver, rat liver and rat ascites hepatoma was readily isolated by concanavalin A-Sepharose (Con A-Sepharose) affinity column chromatography. tRNATyr from these sources was extensively purified by Ricinus communis lectin-Sepharose column chromatography. These results, together with the chromatographic behaviour of four tRNAs (tRNATyr, tRNAHis, tRNAAsn and tRNAAsp) on acetylated DBAE-cellulose column chromatography suggested that tRNAAsp contains a Q nucleoside species having a mannose moiety while tRNATyr contains Q nucleoside with galactose. The sugars attached in 4-position of cyclopentene diol in the Q molecule are therefore not present at random in the four tRNAs, but present only in each specific tRNA. This is the first case which shows that plant agglutinin interacts with nucleic Acid as well as polysaccharide and glycoproteins.

Animals↗
PubMed1997

Quantitation and histochemical localization of galectin-1 and galectin-1-reactive glycoconjugates in fetal development of bovine organs.

The display of cellular oligosaccharide chains is known to undergo marked developmental changes, as monitored histochemically with plant lectins. In conjunction with endogenous lectins respective ligand structures may have a functional role during fetal development. The assumption of a recognitive, functionally productive interplay prompts the study of the expression of a tissue lectin and of lectin-reactive glycoconjugates concomitantly. Focusing on common beta-galactosides as constituents of oligosaccharide chains and the predominant member of the family of galectins in mammals, namely galectin-1, the question therefore is addressed as to whether expression of lectin and lectin-reactive glycoconjugates exhibits alterations, assessed in three morphologically defined fetal stages and in adult bovine organs. Using a sandwich ELISA, the level of the rather ubiquitous galectin-1 is mostly increased in adult organs relative to respective fetal stages, except for the case of kidney. This developmental course is seen rather seldom, when the amounts of lectin-reactive glycoproteins or glycolipids are quantitated in solid-phase assays after tissue homogenization. Western blotting, combined with probing by labeled galectin-1, discloses primarily quantitative changes in the reactivity of individual glycoproteins. Performing the same assays on extract aliquots with a plant agglutinin, namely the galactoside-binding mistletoe lectin, whose fine specificity is different from galectin-1, its reduced extent of binding in solid-phase assays and the disparate profile of lectin-reactive glycoproteins reveal a non-uniform developmental alteration within the group of structural variants of beta-galactosides. Although sample preparation can affect ligand preservation and/or presentation and thus restricts the comparability of biochemical and histochemical results, especially for soluble reactants, the histochemical studies on frozen and paraffin-embedded sections of bovine heart, kidney and liver demonstrate that the localization of the galectin and of lectin-reactive epitopes can show a similar distribution, as seen in liver and heart, with organ-typical quantitative changes of a rather similar staining profile (heart, kidney) or notable changes in the spatial distribution (liver) in the course of development. This report emphasizes the potential value of combined monitoring of the lectin and its potential in vivo ligands to contribute to eventually unravel organ-related function(s) of a tissue lectin.

Animals↗
PubMed1996

V beta-specific deletion of mature thymocytes induced by the plant superantigen Urtica dioica agglutinin.

Urtica dioica agglutinin (UDA), a plant protein, is a superantigen activating in a MHC class II-restricted manner the V beta 8. 3-bearing T-cells (Galelli and Truffa-Bachi, J. Immunol. 151, 1821, 1993). Administration of UDA to adult mice provokes the clonal expansion of the responding cells which is followed by the deletion of the major fraction of the UDA-sensitive cells, whereas the remaining cells become anergic (Galelli et al., J. Immunol. 154, 2600, 1995). We have analyzed the effect of UDA on thymocytes. Injection of UDA resulted in a rapid, but transient, deletion of a large fraction of the V beta 8.3-bearing mature T-cells. In contrast to other exogenous superantigens, this deletion was not preceded by the clonal expansion of the UDA-responding thymocytes. Moreover, the V beta 8.3-bearing mature T-cells escaping the deletion were not anergic to an in vitro UDA restimulation. UDA and the other superantigens also differ as the general, V beta-unrestricted, thymic atrophy induced by classical superantigens was not observed with UDA.

Animals↗
PubMed1983

Cell-surface changes during mitogenic stimulation of lymphocytes assessed by the binding of wheat-germ agglutinin and other plant lectins.

Lymphocytes from murine lymph node, cultured in the presence of an optimally mitogenic dose of phytohaemagglutinin, were stained with fluoresceinated lectins and analysed by flow cytometry. A marked increase in the ability of lymphocytes to bind wheat-germ agglutinin was observed that is particularly pronounced for the blast cells, reaching a maximum at about 40 h, when they are 5.5-times brighter than cells at zero time. The corresponding intensification of the small cells is 2-fold. Much smaller increases in binding accompanying blast transformation were observed when fluoresceinated concanavalin A or Lens culinaris haemagglutinin were used. Polyacrylamide gel electrophoresis of plasma membranes followed by treatment of the gels with radioactively labelled lectins and autoradiography also showed a very distinct increase in the binding of wheat-germ agglutinin to membranes from mitogen-stimulated porcine lymphocytes. Less marked changes in the binding of concanavalin A, Lens culinaris heamagglutinin and Ricinus communis agglutinin 120 were also noted. The apparent multiplicity of glycoproteins that bind each lectin, suggests that in each case the sites are heterogeneous. We conclude that lymphocytes stimulated by the T-cell mitogen phytohaemagglutinin expose new glycoprotein receptors for wheat-germ agglutinin that are most abundant on blast cells at 40 h. Attempts to characterize the receptor biochemically suggest that the carbohydrate moiety recognised by wheat-germ agglutinin is present on a glycoprotein of approx. 120 kDa molecular mass and also possibly on glycoproteins of 170-190 kDa.

Animals↗
PubMed2001

The interaction between wheat germ agglutinin and other plant lectins with prostate cancer cells Du-145.

The bioadhesive properties of fluorescein-labeled plant lectins with different carbohydrate specificities were investigated by flow cytometry at 4 and 37 degrees C using Du-145 prostate cancer cells. At both temperatures the lectin association rate increased following the order: Dolichos biflorus agglutinin (DBA)<peanut agglutinin<Ulex europaeus isoagglutinin I<Lens culinaris agglutinin<Solanum tuberosum lectin << wheat germ agglutinin (WGA), reflecting the glycosylation pattern of Du-145 cells. Both, the BSA-binding capacity of the cells referring to nonspecific binding and inhibition studies using the complementary carbohydrate, assured specificity of the lectin-cell interactions except for DBA. The WGA-association rate of Du-145 cells was dependent on temperature indicative for cellular uptake of membrane-bound WGA. Intracellular enrichment of WGA was confirmed by confocal microscopy. As resulted from experiments in presence of ouabain active transport mechanisms were involved in cellular uptake of WGA. Equilibration of the intracellular pH with monensin pointed to accumulation of intracellular located WGA within acidic compartments of Du-145 cells such as the lysosomes or the trans-Golgi complex. Consequently the interaction of WGA with Du-145 cells at 37 degrees C is a one way process due to immediate active transport of membrane-bound lectin into acidic compartments of prostate cancer cells.

Adenocarcinoma↗
PubMed1980

Distribution of wheat germ agglutinin in young wheat plants.

A liquid phase, competition-binding radioimmunoassay for wheat germ agglutinin, with a detection limit of 10 nanograms, was developed in order to determine the distribution of this lectin in young wheat plants. Affinity columns for wheat germ agglutinin removed all antigenically detectable activity from crude extracts of wheat tissue; thus, the antigenic cross-reactivity detected by the assay possesses sugar-binding specificity similar to the wheat germ-derived lectin. The amount of lectin per dry grain is approximately 1 microgram, all associated with the embryo. At 34 days of growth, the level of lectin per plant was reduced by about 50%, with approximately one-third in the roots and two-thirds in the shoot. The data also indicate that actively growing regions of the plant (the bases of the leaves and rapidly growing adventitious roots) contain the highest levels of lectin. Half of the lectin associated with the roots could be solubilized by washing intact roots in buffer containing oligomers of N-acetylglucosamine, whereas the remainder is liberated only upon homogenization of the tissue.

Journal Article↗
PubMed1989

Lectin binding in colorectal mucosa.

Lectin binding of goblet cell mucin in human colonic mucosa was studied in patients with irritable bowel syndrome, colorectal malignancy and ulcerative colitis using plant lectins, Dolichos biflorus agglutinin (DBA) and peanut agglutinin (PNA). Normal colonic mucosa demonstrated a strong binding with DBA (100%) but did not bind to PNA at all. Colonic carcinomas showed strong PNA binding (7 of 15 biopsies) while DBA binding was absent in 14 of 15 biopsies. The transitional mucosa showed reduced or absent DBA binding in 6 and positive PNA binding in 2 of 15 biopsies. During the active phase of ulcerative colitis, there was a loss of DBA binding in 10 of 15 biopsies, which was restored during remission in all. One biopsy with severe dysplasia showed PNA binding. It is concluded that normal colorectal mucosa binds DBA strongly but not PNA. Malignant tissue and transitional mucosa reveal PNA binding often, with decreased DBA binding. In ulcerative colitis DBA binding decreases during phases of activity.

Arachis↗
PubMedDate not supplied

Distribution of binding sites for the plant lectin Ulex europaeus agglutinin I on primary sensory neurones in seven different mammalian species.

There is an increasing body of evidence to suggest that different functional classes of neurones express characteristic cell-surface carbohydrates. Previous studies have shown that the plant lectin Ulex europaeus agglutinin-I (UEA) binds to a population of small to medium diameter primary sensory neurones in rabbits and humans. This suggests that a fucose-containing glycoconjugate may be expressed by nociceptive primary sensory neurones. In order to determine the extent to which this glycoconjugate is expressed by other species, in the current study, we have examined the distribution of UEA-binding sites on primary sensory neurones in seven different mammals. Binding sites for UEA were associated with the plasma membrane and cytoplasmic granules of small to medium dorsal root ganglion cells and their axon terminals in laminae I-III of the grey matter of the spinal cord, in the rabbit, cat and marmoset monkey. However, no binding was observed in either the dorsal root ganglia or spinal cord in the mouse, rat, guinea pig or flying fox. These results indicate an inter-species variation in the expression of cell-surface glycoconjugates on mammalian primary sensory neurones.

Animals↗
PubMed1980

The prickly lettuce agglutinin. I. Isolation from leaves of the prickly lettuce plant (Lactuca scariole).

An agglutinin has been isolated from leaves of the prickly lettuce plant (Lactuca scariole). The prickly lettuce agglutinin (PLA) agglutinates erythrocytes of the mouse and rat, and binds to, but does not agglutinate erythrocytes of other species. PLA can be precipitated from crude plant extracts by cold acetone and ammonium sulfate treatment, is sensitive to proteolytic enzyme activity, and contains carbohydrate residues, suggesting that it is a glycoprotein. The agglutinin has a molecular weight of approximately 84,000 as determined by SDS-PAGE studies. The receptor for PLA has not been elucidated but may involve, in part, sialic acid residues.

Animals↗
PubMed1999

Selective modulation of phosphatidylserine exposure on subpopulations of human peripheral blood lymphocytes by a plant lectin, Viscum album agglutinin (VAA)-I and its recombinant form (rVAA) in vitro.

Growing evidence suggests that lectin-carbohydrate interactions are involved in the regulation of the balance between cell growth and programmed cell death. Viscum album agglutinin (VAA)-I is a galactoside-specific, type II ribosome-inactivating plant lectin. At concentrations less than 10 ng/ml, VAA-I has been shown to induce gene expression and secretion of proinflammatory cytokines as well as apoptosis in cultures of human peripheral blood mononuclear cells (PBMC). This study analyzes the effects of VAA-I and its recombinant nonglycosylated form (rVAA) on alterations of cell membrane permeability of cultured human peripheral lymphocytes (PBL) and on membrane exposure of phosphatidylserine characteristic of apoptosis. Analyses were performed by flow cytometry after staining with propidium iodide (PI) and/or with FITC-Annexin V/PI. After 24 h incubation of PBMC with 100 ng/ml VAA-I and rVAA, staining with supravital concentration of PI (20 microg/ml) for 1 h revealed no differences in percentages of PI-positive cells induced by the two forms of lectin (32.3% and 29.4%), but the exposure to 5 microg/ml PI for 15 min resulted in a significant difference: 35.1% and 8.0% after VAA-I and rVAA treatment, respectively. Kinetic analysis of membrane alterations showed mainly Annexin V positivity after 24 h, whereas after 48 h and 72 h incubation with 100 ng/ml VAA-I or rVAA loss of membrane integrity occurred, as demonstrated by PI staining. Similar to VAA-I, rVAA showed a higher binding affinity for monocytes and granulocytes than for lymphocytes. In cultures of PBL, the binding rank order of both lectins to lymphocyte subsets was NK, CD19+ > CD8+ > CD4+. The amount of Annexin/PI staining of PBL subsets corresponds to the degree of their binding capacity. In conclusion, present results demonstrate that VAA-I and its nonglycosylated recombinant form rVAA exhibit comparable effects on cell membrane alterations in the subsets of human PBLs.

Annexins↗
PubMed1985

Induction of human monocyte-mediated tumor cell killing by a plant lectin, wheat germ agglutinin.

Human peripheral blood monocytes from healthy donors were separated by discontinuous gradient centrifugation and adherence to yield highly purified adherent cell populations (greater than 99% monocytes). Five different plant lectins were tested for ability to induce lectin-dependent monocyte-mediated cytotoxicity (LDMC). Only one lectin, wheat germ agglutinin (WGA), induced significant and reproducible LDMC activity. All the tumor target cells tested were sensitive to variable extents to cytotoxicity mediated by WGA-treated monocytes. Pretreatment of monocytes with WGA did not result in development of LDMC. N-Acetylglucosamine, which specifically binds WGA, inhibited WGA-dependent monocyte-mediated cytotoxicity. Treatment of adherent monocyte-rich monolayers with monoclonal anti-natural killer cell antibody (anti-Leu-11b) and complement did not affect the LDMC activity induced by WGA. These results indicate that the plant lectin WGA, which binds specifically to both human monocytes and tumor cells, renders human blood monocytes cytotoxic to human tumor cells.

Acetylglucosamine↗