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PubMed1987

Lectin affinity high-performance liquid chromatography: interactions of N-glycanase-released oligosaccharides with leukoagglutinating phytohemagglutinin, concanavalin A, Datura stramonium agglutinin, and Vicia villosa agglutinin.

We have developed a lectin affinity high-performance liquid chromatography technique for analysis of oligosaccharides using columns of silica-bound lectins. Purified leukoagglutinating phytohemagglutinin (L-PHA), concanavalin A (Con A), Datura stramonium agglutinin (DSA), and Vicia villosa agglutinin (VVA) were covalently coupled to periodate-oxidized diol-silica by reductive amination. Homogeneous oligosaccharides of known structure, purified following release from Asn with N-glycanase and reduction with NaBH4, were tested for their ability to interact with the silica-bound lectins. The characteristic elution position obtained for each oligosaccharide was reproducible and correlated with specific structural features. The oligosaccharide specificities displayed by silica-bound L-PHA, Con A, and DSA were virtually identical to those established utilizing lectin-agarose conjugates. Analysis of oligosaccharides by lectin affinity HPLC allowed further definition of the specificity of VVA for N-glycanase-released, reduced oligosaccharides. Lectin affinity HPLC is rapid and convenient, providing an important structure-specific dimension to oligosaccharide analysis. This technique is particularly useful when utilized in conjunction with anion-exchange and ion-suppression amine adsorption HPLC methods, which fractionate on the basis of charge and size, respectively. In addition to their utility for oligosaccharide characterization, these affinity columns demonstrate the high degree of oligosaccharide specificity displayed by plant and animal lectins.

Agglutinins↗
PubMed1988

Wheat germ agglutinin and Helix pomatia agglutinin lectin binding on cochlear hair cells.

The fluorescein labelled lectins FITC-WGA and FITC-HPA were used to identify specific carbohydrates in cochlear hair cells. Wheat germ agglutinin (WGA) bound with the cell coat of both inner and outer hair cells (IHC and OHC) suggesting the presence of either N-acetyl-D-glucosamine or sialic acid. In contrast, glycoconjugates with terminal N-acetyl-D-galactosamine residues that bind with Helix pomatia agglutinin (HPA), were demonstrated inside the plasma membrane of outer hair cells. WGA and HPA lectin binding implies the presence of anionic glycoconjugates that furnish added negative charge on the membranes to which they are fixed. The presence of sialic acid or N-acetyl-D-glucosamine on the extracellular surface of cochlear hair cell plasma membrane is consistent with the normal distribution of these glycoconjugates in the cell coat. The presence of the membrane associated oligosaccharide N-acetyl-D-galactosamine within the outer hair cell is inconsistent with the distribution of glycoproteins in internal membrane systems of other cell types.

Acetylgalactosamine↗
PubMed1983

Different T cell antigens and receptors for peanut agglutinin and Helix pomatia agglutinin on steroid-sensitive and resistant lymphocytes in the rabbit using double immunofluorescence.

Rabbit T lymphocytes were characterized using fluorochrome-labelled antisera against thymus cell determinants and fluorochrome-labelled lectins. Three anti-T cell antisera were used, detecting different antigenic determinants on the majority of T cells. Only small subpopulations were found stained by one of the three antisera. After dexamethasone (DX) treatment, the proportion of T cells was significantly increased in bone marrow and appendix, presumably by different mechanisms. Cells binding peanut agglutinin, mainly belonging to the T cell population, were present in small numbers in thymus, spleen, lymph node, and appendix from normal as well as from DX-treated animals. In bone marrow, however, a large PNA+ population showing neither T nor B cell surface properties was observed. After treatment with neuraminidase (NA), PNA binding sites were exposed on B as well as on an increased number of T cells. It is suggested, therefore, that T and B cells retained their PNA receptors during maturation. Masking of these receptors will take place before differentiation of T cells is initiated within the thymus. After NA treatment, also binding sites for Helix pomatia agglutinin were exposed on T cells and to different extents, revealing subsets of negative, weakly and strongly positive HPA cells. HPA weakly positive cells form the major population present in the thymus, while HPA strongly positive cells constitute the major population of the T cells in spleen and lymph node. The exposure of receptors for PNA of HPA appears not to be related to the steroid sensitivity of the cells.

Animals↗
PubMed1988

Wheat-germ-agglutinin and Ricinus communis-agglutinin-binding sites of BHK cells compared with each other and with 140 kDa fibronectin receptors.

We compared the wheat-germ agglutinin (WGA) and Ricinus communis agglutinin (RCA) binding sites of baby-hamster kidney (BHK) cells. There were 1.01 X 10(8) WGA-binding sites per cell (Kd = 0.027 nM) and 6 X 10(6) RCA-binding sites per cell (Kd = 0.014 nM). Binding of WGA or RCA to BHK cells resulted in more than 75% of the cell-surface binding sites becoming associated with the cytoskeleton (i.e. resistant to extraction with detergent), although no more than 10% of these sites were associated with the cytoskeleton before addition of the lectins. After binding of WGA to the cells, the cell surface was cross-linked so extensively that it remained intact even after detergent extraction of the treated cells, and could be observed by electron microscopy. A similar cross-linking effect did not occur after binding of RCA to cells, which may be because there were so many more binding sites for WGA than for RCA. The composition of WGA- and RCA-binding molecules was analysed by lectin affinity chromatography of metabolically radiolabelled BHK cells. We found that in the WGA-binding-molecule preparations there were eight major polypeptides, ranging in molecular mass from 93 to 340 kDa, and that the RCA-binding molecules were a subpopulation of the WGA-binding molecules. A polyclonal antibody against the 140 kDa fibronectin (FN) receptors of Chinese-hamster ovary (CHO) cells immunoblotted a 145 kDa polypeptide component in both WGA- and RCA-binding-molecule preparations. The results indicated that the 145 kDa component was present in at least two FN-receptor complexes that differed in glycosylation, only one of which was able to bind to RCA affinity columns. The oligomeric nature of the FN-receptor complex, which contained three polypeptides with molecular masses of 120-145 kDa, was demonstrated by using anti-(CHO-cell FN receptor) antibodies to immunoprecipitate extracts prepared from radioiodinated BHK cells.

Binding Sites↗
PubMed1998

Effect of the lectins wheat germ agglutinin (WGA) and Ulex europaeus agglutinin (UEA-I) on the alpha-amylase secretion of rat pancreas in vitro and in vivo.

Lectins are able to bind to cholecystokinin (CCK) receptors and other glycosylated membrane proteins. The lectins wheat germ agglutinin (WGA) and Ulex europaeus agglutinin (UEA-I) are used for affinity chromatography to isolate the highly glycosylated CCK-A receptor of pancreatic acinar cells. According to the working hypothesis that lectin binding to the CCK receptor should alter the ligand-receptor interaction, the effect of WGA and UEA-I on CCK-8-induced enzyme secretion was studied on isolated rat pancreatic acini in vitro. In vitro both lectins showed a dosage-dependent inhibition of CCK-8-induced alpha-amylase secretion of acini over 60 min. WGA showed a strong inhibitory effect on amylase secretion, approximately 40%, in vitro. UEA-I caused a smaller, but significant decrease, approximately 20%, in enzyme secretion of isolated acini. Additionally, both lectins inhibited cerulein/secretin- or cerulein-induced pancreatic secretion of rats in vivo, but not after secretin alone. The results are discussed with respect to a possible influence of both lectins on the interaction of CCK or cerulein with the CCK-A receptor.

Animals↗
PubMed1981

Discrete Distribution of binding sites for Dolichos biflorus agglutinin (DBA) and for peanut agglutinin (PNA) in mouse organ tissues.

The distribution of binding sites for two lectins with different specificities was studied in adult mice by staining paraffin sections with lectins labeled either with fluorescein isothiocyanate or horseradish peroxidase. Binding sites for Dolichos biflorus agglutinin, a lectin specific to terminal alpha-N-acetylgalactosamine residue, were detected only in several restricted regions, such as collecting tubules and Bowman's capsules of the kidney, bile ducts, pancreatic ducts, sperms, oocytes, some secreting cells, and the secreted mucin itself. Binding sites for peanut agglutinin (PNA), a lectin specific to terminal beta-galactosyl residue, were distributed more widely. However, differentiation-dependent alterations in the expression of PNA binding sites have been observed in two types of cell lineage. During the course of spermatogenesis, the binding sites were expressed at the stage of spermatocytes. In the epithelium of esophagus, the binding sites were present in cells of the superficial layer.

Animals↗
PubMed1989

Wheat germ agglutinin, concanavalin A, and lens culinalis agglutinin block the inhibitory effect of nerve growth factor on cell-free phosphorylation of Nsp100 in PC12h cells.

It has been shown that in PC12 and its subclone PC12h treatment of the cells with nerve growth factor (NGF) induces a selective decrease in the incorporation of radioactive phosphate into a 100,000-dalton protein, designated in an earlier study as Nsp100, in the subsequent phosphorylation of soluble extracts from cells with (gamma-32P)ATP. In the present study, we show that plant lectins, wheat germ agglutinin (WGA), concanavalin A (Con A), and lens culinaris agglutinin (LCA), inhibit the action of NGF on Nsp100 phosphorylation in PC12h cells. Treatment of the cells with WGA, which binds to N-acetylglucosamine and sialic acid residues on glycoproteins, strongly blocked the inhibitory action of NGF on the protein phosphorylation. Con A and LCA, both of which recognize the same specific sugars (mannose, glucose), displayed only a moderate blocking effect. Unlike the native lectin, succinylated WGA, which has the ability to bind to N-acetylglucosamine but not to sialic acid residues, and other lectins examined in this study did not inhibit the action of NGF on Nsp100. WGA-mediated inhibition of NGF action was reversed by the addition of N-acetylglucosamine and by the addition of a much lower concentration of a sialoglycoprotein, mucin, into the culture. Since the binding of succinylated WGA to N-acetylglucosamine residues of cell-surface glycoconjugates is not sufficient to prevent the action of NGF, WGA might act on sialic acid residues of the NGF receptor molecule to effect the inhibition of biological actions of NGF.

Adrenal Gland Neoplasms↗
PubMed2002

Prostaglandin D2 generation by rat peritoneal mast cells stimulated with Datura stramonium agglutinin and its inhibition by haptenic sugar and wheat germ agglutinin.

The production of prostaglandin D2 (PGD2) by rat peritoneal mast cells incubated with N-acetyl glucosamine (GlcNAc) oligomer-specific Datura stramonium agglutinin (DSA) for 10 min in the presence of 0.3 mM Ca2+ was examined. Previously, our group reported that the incubation of rat mast cells with DSA (5 - 100 microg/ml) under similar conditions resulted in a calcium influx and histamine release via a pertussis toxin-sensitive G-protein pathway of the mast cells, and the histamine release was inhibited by haptenic sugar chitooligosaccharides or GlcNAc-specific lectin wheat germ agglutinin (WGA) (K. Matsuda et al., Jpn J Pharmacol 66, 195 - 204 (1994)). DSA (5 - 100 microg/ml) dose-dependently stimulated the mast cells to generate PGD2. Chitooligosaccharides (1% w/v) and WGA (100 microg/ml) inhibited the production of PGD2 induced by 100 microg/ml of DSA, suggesting that the effect of DSA is sugar-specific. A prostaglandin G/H synthase inhibitor NS-398 (N-[cyclohexyloxy-4-nitrophenyl] methanesulfonamide) (10 microM) inhibited the formation of PGD2 induced by DSA (20 microg/ml). These results suggest that the binding of DSA to the corresponding sugar residues on the mast cell surface mediates the signaling of the prostaglandin G/H synthase pathway.

Acetylglucosamine↗
PubMed1985

[Binding of peanut agglutinin (PNA) and Dolichos biflorus agglutinin (DBA) to human colonic carcinomas, adenomas, and polyps: histochemical staining by the lectin-antilectin-PEP method].

Binding of 2 lectins--peanut agglutinin (PNA) and Dolichos biflorus agglutinin (DBA)--with human colonic carcinomas, adenomas, juvenile and hyperplastic polyps, and polyps in Cronkhite-Canada syndrome was examined histochemically by the lectin-antilectin-PAP method. With PNA, brush borders of the carcinoma cell were stained(90.9%), while the cytoplasm of the adenomas and polyps were stained granularly (88.0%). With DBA, the cytoplasm of the carcinomas was stained diffusely (72.7%), though 25% of the cases showed the fringed type cytoplasmic staining similar to adenomas, polyps and normal crypts. It appears important to recognize the differences in the staining patterns, especially in PNA, between carcinomas and other benign lesions, which apparently reflect changes of sugar residues during cancerization.

Adenocarcinoma↗
PubMed1983

Interactions of lectins and monoclonal antibodies with human mononuclear cells. I. Specific inhibition of OKT4 and OKT8 binding by Ricinus communis agglutinin and wheat germ agglutinin.

We used flow cytometry to examine effects of lectins on interactions between human lymphocytes and the anti-T cell monoclonal reagents OKT4 (T helper-specific) and OKT8 (T suppressor-specific). Wheat germ agglutinin (WGA) inhibited OKT8 binding to lymphocytes by a mean 77% and Ricinus communis agglutinin (RCA-I) inhibited OKT4 binding by 66%. Inhibition was abolished in each case by appropriate carbohydrate hapten inhibitors of lectin binding, indicating it was mediated by the lectin saccharide combining sites. Neither WGA nor RCA-I inhibited binding of OKT3, a pan-T cell monoclonal reagent. In addition, a group of other lectins with a variety of nominal carbohydrate specificities did not inhibit OKT4 or OKT8 binding. Preincubation experiments and gel filtration indicated that inhibition in each case was due to competition between lectin and monoclonal for binding to cell surfaces, not to direct lectin-monoclonal antibody interactions. Treatment of lymphoid cells with OKT8 and complement reduced OKT8- and WGA-binding cells concurrently, whereas treatment with OKT4 and complement did not reduce percentages of either type of cell. Similarly, specific depletion of OKT8-binding cells abolished the mitogenic response to WGA but not that to PHA. Cell populations enriched for WGA-binding cells prepared by flow cytometry and cell sorting demonstrated parallel enrichment for OKT8-binding and depletion of OKT4-binding cells. Therefore, these data demonstrate specific inhibition of OKT4 and OKT8 binding by the lectins, RCA-I and WGA, respectively. Inhibition was mediated by lectin binding to lymphoid cell surfaces, perhaps directly to the T4 or T8 antigens. The observations indicate that lectins may prove useful for investigating structural features of some immunologic cell surface markers. Furthermore, they provide the possibility that certain in vitro effects of lectins on immune function may result from their interactions with molecules such as the T4 and T8 antigens.

Animals↗
PubMed1975

Influence of Concanavalin A, wheat germ agglutinin, and soybean agglutinin on the fusion of myoblasts in vitro.

Although muscle cell fusion was shown to be an energy-requiring process, release of myoblasts from an EGTA fusion block could be accomplished with Earle's balanced salt solution (containing 1.8 mM Ca++) free of glucose or any other energy-produced metabolite. The effect of concanavalin A, abrin, and the lectins from wheat germ, soybean, and Lens culinaris on myoblast fusion was examined with synchronized myoblast cultures upon release from fusion block. At a concentration of 15 mug/ml, these lectins were found to inhibit the fusion process to the extent of 62%, 41%, 32%, 8%, and 19%, respectively. Concanavalin A inhibition could be prevented by alpha-methyl-D-mannoside. The inhibitory effect of all the lectins except abrin could be reversed by changing to the normal, serum-containing medium. The number of binding sites was 3.4 X 10(7), 6.1 X 10(7), and 1.7 X 10(6), respectively. Although myoblasts were found to have about twice as many binding sites for wheat germ agglutinin as for concanavalin A, concanavalin A was determined to be twice as effective as wheat germ agglutinin as an inhibitor of myoblast fusion. These findngs raise the possibility that specific cell surface glycoproteins may be an important factor in this process.

Abrin↗
PubMed2005

Oligomerization endows enormous stability to soybean agglutinin: a comparison of the stability of monomer and tetramer of soybean agglutinin.

Soybean agglutinin is a tetrameric legume lectin, each of whose subunits are glycosylated. This protein shows a very high degree of stability when compared to the other proteins of the same family. In a previous work, it was shown that the unusual stability of the protein is due to a high degree of subunit interactions. In this study we present the thermodynamic parameters for the stability of soybean agglutinin monomer. The monomeric species is found at pH 2 and below which it is most populated at pH 1.9, as evident from size-exclusion chromatographic and dynamic light scattering studies. The analyses of circular dichroism and fluorescence spectroscopy suggest that the monomer is well folded, and that it has certain characteristic features when compared to its tetrameric counterpart. The conformational stabilities of the tetramer and the monomer at the temperature of their maximum stabilities (310 K) are 59.2 kcal/mol and 9.8 kcal/mol, respectively, indicating that oligomerization contributes significantly to the stability of the native molecule. Also, the T(g) difference for the two forms of the protein is approximately 40 K, whereas the difference in DeltaC(p) is only 1.6 kcal/mol/K. This suggests that the major hydrophobic core is present in the monomer itself, and that oligomerization involves mainly ionic interactions.

Biophysical Phenomena↗
PubMed1985

Corticocortical and collateral thalamocortical connections of postcentral somatosensory cortical areas in squirrel monkeys: a double-labeling study with radiolabeled wheatgerm agglutinin and wheatgerm agglutinin conjugated to horseradish peroxidase.

Experiments were performed to determine whether thalamic neurons send collaterals to more than one subdivision of postcentral somatosensory cortex, and to evaluate the fidelity of somatotopic connections between cortical representations of the body surface. After microelectrode recordings identified the locations of the representations of the fingertips along the border of area 3b with area 3a and along the border of area 1 with area 2, one tracer, tritiated N-acetyl wheatgerm agglutinin ([3H]WGA), was injected into the rostral representation at the 3a-3b border, and another, wheatgerm agglutinin conjugated to horseradish peroxidase (WGA:HRP), was injected into the caudal representation at the 1-2 border. The results indicate that three thalamic regions are interconnected with both border zones. Regions of overlapping retrograde and anterograde label included the ventromedial portion of the lateral division of the ventroposterior nucleus (VPL), which is known to represent the digits; the medial extent of a dorsal capping zone of VPL that we term the ventroposterior superior nucleus (VPS); and the anterior pulvinar (Pa). Cells labeled with one or the other tracer, as well as cells labeled with both tracers, were found in VPL, VPS, and Pa. Our procedures necessarily underestimated the numbers of cells projecting to both rostral and caudal injection zones, but at least 15-20% of VPL and 20-40% of VPS neurons that were autoradiographically labeled appeared to have such collaterals. While only a few cells in Pa were autoradiographically labeled from injections at the 3a-3b border, the presence of several double-labeled cells suggests that at least some Pa neurons project to both injected zones. By relating the present results to those from studies where connections were determined for single architectonic fields, we conclude that many neurons in VP project to both areas 3b and 1, and that many neurons in VPS project to both areas 3a and 2. In addition, both areas 3a and 2 appear to have interconnections with Pa. Connections of Pa with area 2 have only recently been reported (Pons and Kaas, in press), and connections of Pa with area 3a have not been described. The results imply that, in part, the same information from cutaneous receptors is relayed to areas 3b and 1, and the same information from deep receptors is relayed to areas 3a and 2.(ABSTRACT TRUNCATED AT 400 WORDS)

Animals↗
PubMed1977

Stimulation of human peripheral blood lymphocytes by periodate, galactose oxidase, soybean agglutinin, and peanut agglutinin: differential effects of adherent cells.

Blastogenic responses of normal human peripheral lymphocytes to three distinct groups of mitogens were studied: Group I--phytohemagglutinin (PHA), concanavalin A (Con A), and pokeweed mitogen (PWM); Group II--soybean agglutinin (SBA) and peanut agglutinin (PNA); and Group III--galactose oxidase (GO) and sodium periodate (IO4-). SBA was mitogenic for human cells, and this effect was enhanced by treating the cells with neuraminidase (NA). PNA was mitogenic only after cells had been treated with NA. GO was effective before and activity was increased after lymphocytes were treated with NA. Responses to Group II and III mitogens were more variable than were those to Group I mitogens. Studies with purified T and B cells indicated that SBA and PNA were T cell mitogens, whereas IO4- and GO failed to stimulate either T or B cells. Adding macrophages back to this system indicated that they were both T cell mitogens with strict macrophage requirements. T cell responses to SBA and PNA were enhanced over responses to unfractionated cells to a degree that could not be explained simply by enrichment of the cultures with T cells. Removal of adherent cells from unfractionated cell suspensions again revealed a marked enhancement of responses to SBA and PNA, a consistent decrease in responses to IO4-, and a variable decrease in responses to GO. Similar results were found with 14C-leucine and 3H-uridine incorporation, as well as 3H-thymidine for the assessment of bastogenic response. Mechanisms responsible for these differential effects of macrophage depletion on lymphocyte responses to different groups of mitogens are yet to be determined. Either different mitogens require different lymphocyte to macrophage ratios for optimal stimulation, or some mitogens (i.e., SBA and PNA) form inhibitory complexees in the lymphocyte-macrophage mixture. In any case, variability in response to mitogenic agents in normal as well as pathologic states may be dependent on adherent cell populations, rather than on the lymphocytes themselves.

Alcohol Oxidoreductases↗
PubMed1987

Lectin affinity high-performance liquid chromatography. Interactions of N-glycanase-released oligosaccharides with Ricinus communis agglutinin I and Ricinus communis agglutinin II.

The structural determinants required for interaction of oligosaccharides with Ricinus communis agglutinin I (RCAI) and Ricinus communis agglutinin II (RCAII) have been studied by lectin affinity high-performance liquid chromatography (HPLC). Homogeneous oligosaccharides of known structure, purified following release from Asn with N-glycanase and reduction with NaBH4, were tested for their ability to interact with columns of silica-bound RCAI and RCAII. The characteristic elution position obtained for each oligosaccharide was reproducible and correlated with specific structural features. RCAI binds oligosaccharides bearing terminal beta 1,4-linked Gal but not those containing terminal beta 1,4-linked GalNAc. In contrast, RCAII binds structures with either terminal beta 1,4-linked Gal or beta 1,4-linked GalNAc. Both lectins display a greater affinity for structures with terminal beta 1,4-rather than beta 1,3-linked Gal, although RCAII interacts more strongly than RCAI with oligosaccharides containing terminal beta 1,3-linked Gal. Whereas terminal alpha 2,6-linked sialic acid partially inhibits oligosaccharide-RCAI interaction, terminal alpha 2,3-linked sialic acid abolishes interaction with the lectin. In contrast, alpha 2,3- and alpha 2,6-linked sialic acid equally inhibit but do not abolish oligosaccharide interaction with RCAII. RCAI and RCAII discriminate between N-acetyllactosamine-type branches arising from different core Man residues of dibranched complex-type oligosaccharides; RCAI has a preference for the branch attached to the alpha 1,3-linked core Man and RCAII has a preference for the branch attached to the alpha 1,6-linked core Man. RCAII but not RCAI interacts with certain di- and tribranched oligosaccharides devoid of either Gal or GalNAc but bearing terminal GlcNAc, indicating an important role for GlcNAc in RCAII interaction. These findings suggest that N-acetyllactosamine is the primary feature required for oligosaccharide recognition by both RCAI and RCAII but that lectin interaction is strongly modulated by other structural features. Thus, the oligosaccharide specificities of RCAI and RCAII are distinct, depending on many different structural features including terminal sugar moieties, peripheral branching pattern, and sugar linkages.

Carbohydrate Conformation↗
PubMed1996

Characterization of the binding specificity of Anguilla anguilla agglutinin (AAA) in comparison to Ulex europaeus agglutinin I (UEA-I).

Using immunochemical and immunohistochemical methods, the binding site of Anguilla anguilla agglutinin (AAA) was characterized and compared with the related fucose-specific lectin from Ulex europaeus (UEA-I). In solid-phase enzyme-linked immunoassays, the two lectins recognized Fuc alpha 1-2Gal beta-HSA. AAA additionally cross-reacted with neoglycolipids bearing lacto-N-fucopentaose (LNFP) I [H type 1] and II [Le(a)] and lactodifucotetraose (LDFT) as glycan moieties. UEA-I, on the other hand, bound to a LDFT-derived neoglycolipid but not to the other neoglycolipids tested. Binding of AAA to gastric mucin was competitively neutralized by Le(a)-specific monoclonal antibodies. UEA-I binding, on the other hand, was reduced after co-incubation with H type 2- and Le(y)-specific monoclonal antibodies. According to our results, AAA reacts with fucosylated type 1 chain antigens, whereas UEA-I binds only to the alpha 1-2-fucosylated LDFT-derived neoglycolipid. In immunohistochemical studies, the reactivity of AAA and UEA-I in normal pyloric mucosa from individuals with known Lewis and secretor status was analysed. AAA showed a broad reaction in the superficial pyloric mucosa from secretors and non-secretors, but AAA reactivity was more pronounced in Le(a+b-) individuals. On the other hand, UEA-I stained the superficial pyloric mucosa only from secretor individuals. A staining of deep mucous glands by the lectins was found in all specimens. Both reacted with most human carcinomas of different origin. Slight differences in their binding pattern were observed and may be explained by the different fine-specificities of the lectins.

Agglutinins↗
PubMed1980

Peanut agglutinin. VI. Identification of murine T lymphocyte subsets during ontogenesis by use of peanut agglutinin and Ly-6.2 antiserum.

Fluoresceinated peanut agglutinin (PNA-FTC), Thy-1.2, and Ly-6.2 antisera were used to identify various murine T lymphocyte subpopulations during fetal and perinatal life. By means of double immunofluorescence labeling, we identified three T lymphocyte subsets: PNA+Ly-6.2+, PNA+Ly-6.2-, PNA-Ly-6.2+ having distinct distribution in the adult thymus and spleen. The study of the appearance of these three subsets in fetal liver, thymus, and spleen has shown that they did not occur similarly. The PNA+Ly-6.2+ subset was present in all three organs during fetal life and at a level rather similar to that of adult life; the PNA+Ly-6.2- subset was also present in the three fetal organs; conversely, the percentage of the PNA-Ly-6.2+ spleen cells was very low in fetal and neonatal life and increased significantly between 1 and 2 wk of age. Our results demonstrate that during fetal life, lymphocyte subsets are phenotypically differentiated as in adult life and that differentiation of T lymphocytes occurs preferentially through various lineages present during early ontogenesis. Moreover, quantitative modulation of some of these subsets is shown from fetal to adult life and may explain some of the immunologic immature features of young murine spleen.

Adrenal Cortex Hormones↗
PubMed1982

The acquisition of receptors for peanut agglutinin by peanut agglutinin-negative thymocytes and peripheral T cells.

Using fluorescein-conjugated peanut agglutinin (PNA) and the fluorescence-activated cell sorter, we have shown that the cytotoxic T cells generated by culturing thymocytes (about 85% PNA+ cells) with Con A and medium conditioned by Con A-stimulated spleen cells were mostly PNA+. Cytotoxic T cells generated in parallel cultured of PNA- thymocytes or normal lymph node cells (in which the T cells are PNA-), however, were also mostly PNA+. The development of PNA+ cells from PNA- mature peripheral T cells was confirmed by using cultures of PNA- T cells separated on a fluorescence-activated cell sorter from lymph node cells. Immunization in vivo also resulted in the appearance of PNA+ T cells in the lymph node. These results indicate that receptors for PNA can no longer be regarded as unambiguous markers of T cell immaturity, or of the origin of a T cell from a PNA+ precursor. The possibility that a variable proportion of the PNA+ cells in the thymus may be generated by intrathymic activation of PNA- medullary thymocytes is discussed.

Animals↗