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PubMed1975

Interactions between ricinus agglutinin and human IgM and IgG.

Ricinus agglutinin, purified until homogeneous, precipitates serum glycoproteins with terminal nonreducing galactose residues including IgM and IgG. Almost 100% of IgM reacted with anti-IgM and ricinus agglutinin in quantitative precipitin tests. In similar tests, almost 100% of polyclonal IgG was precipitated by excess anti-IgG, whereas only about 10% reacted with ricinus agglutinin. In quantitative precipitin analyses and affinity chromatography experiments with insolubilized ricinus agglutinin and isolated monoclonal IgG1 and IgG3 proteins, only IgG3 proteins reacted with ricinus agglutinin.

Antibodies, Anti-Idiotypic↗
PubMed1979

Properties of succinylated wheat-germ agglutinin.

The physicochemical and binding properties of succinylated wheat germ agglutinin are described in comparison with these of unmodified wheat germ agglutinin. Succinylated wheat germ agglutinin is an acidic protein with a pI of 4.0 +/- 0.2 while the native lectin is basic, pI of 8.5. The solubility of succinylated wheat germ agglutinin is about 100 times higher than that of the unmodified lectin at neutral pH. Both lectins are dimeric at pH down to 5, and the dissociation occurs at pH lower than 4.5. The binding of oligosaccharides of N-acetylglucosamine to both lectins is very similar on the basis of fluorescence and phosphorescence studies. The minimal concentration required to agglutinate rabbit red blood cells is about 2 microgram/ml with both lectins and the concentrations of N-acetylglucosamine and di-N-acetylchitobiose which inhibit agglutination are similar with both lectins. The number of succinylated wheat germ agglutinin molecules bound to the surface of mouse thymocytes was ten times lower than that of the unmodified lectin although the apparent binding constant was only slightly different between the two lectins. The dramatic decrease of the apparent number of cell surface receptors upon succinylation of the lectin is discussed on the basis of the decrease of the isoelectric point and of the acidic properties of the cell surface.

Fluoresceins↗
PubMed1986

Peanut agglutinin receptor is a marker of myelin in rat brain. Developmental changes in its distribution.

Peanut agglutinin receptor, which is a glycoconjugate with terminal Gal(beta 1-3)GalNAc residues, was found to be a specific biochemical marker of the myelin in rat brain. The localization of peanut agglutinin receptor in rat brain was studied by use of fluorescein-conjugated peanut agglutinin. In adult rat brain, receptors were found only on myelin. In contrast, the receptors in fetal brain were not found in the white matter, but only in the ependyma. Peanut agglutinin receptors were extracted from adult and fetal rat brains with 2% Triton X-100, subjected to electrophoresis on 10% sodium dodecyl sulfate-polyacrylamide gel, blotted onto nitrocellulose filters, and detected by their reaction with peroxidase-conjugated peanut agglutinin. A major receptor of Mr 130,000 and a minor one of Mr 200,000 were found in both adult and fetal rat brains.

Age Factors↗
PubMed1967

Lambda chains in cold agglutinins.

Type L light chains have been found in the cold agglutinins in the serums of three patients with chronic hemolytic anemia. Altholugh two of these cold agglutinins are unusual in that they do not have specificity to I or i red-cell antigens (one of these has, in addition, cryoglobuilin property), the third is a cold agglutinin of I specificity. Previously reported cold agglutinins from such patients have all been of type K; this is tlhe first report of type L cold agglutinins associated with chronic hemolytic anemia.

Anemia, Hemolytic, Autoimmune↗
PubMed1968

Horse agglutinins in infectious mononueleosis. 3. riterion for differential diagnosis.

One hundred infectious mononucleosis and the same number of non-infectious mononucleosis sera were studied to evaluate the sensitivity and specificity of horse erythrocytes in the diagnosis of infectious mononucleosis. Titres of horse agglutinins in infectious mononucleosis sera ranged from 28 to 7,168 with a geometric mean of 550, whereas the corresponding sheep agglutinin titres ranged from less than 7 to 3,584, with a geometric mean of 126. Horse agglutinin titres of non-infectious mononucleosis sera ranged from less than 7 to 896, with a geometric mean of 59. Infectious mononucleosis sera tested with horse erythrocytes before and after absorption with guinea pig kidney and beef erythrocytes showed patterns different from those of non-infectious mononucleosis sera, even when sheep agglutinin titres were too low for satisfactory evaluation. After absorption with guinea pig kidney, horse agglutinin titres of infectious mononucleosis sera were uniformly higher than in the corresponding serum absorbed with beef erythrocytes. This was not the case for non-infectious mononucleosis sera. Results confirm our previously expressed view that horse erythrocytes are preferable to sheep erythrocytes in the serological diagnosis of infectious mononucleosis.

Animals↗
PubMed1983

Distribution of peanut agglutinin binding sites in rat lymphatic organs.

Distribution of peanut agglutinin binding sites was studied histologically with horseradish peroxidase labelled and fluorescein isothiocyanate labelled peanut agglutinin in terms of cell differentiation in rat lymphatic organs, (thymus, spleen, lymph nodes). In this study, alcohol-fixed paraffin-embedded tissue sections were used and proved to be useful for the histochemical study with peanut agglutinin. In the germinal center of the lymph node, cells were weakly positive for peanut agglutinin binding sites but not in the mantle zone of the lymph follicle. In the thymus, the cortical thymocytes were weakly positive for peanut agglutinin binding sites but not in the medulla. In the spleen, some cells on the periphery of the white pulp were weakly positive for PNA binding sites but cells around the central artery were not positive. Large cells with granular cytoplasma around the sinus of the spleen and lymph node, thought to be fixed macrophages, were strongly positive for PNA binding sites.

Animals↗
PubMed1976

Natural anti-ovalbumin agglutinins in adult chickens.

Sera from inbred SPF White Leghorn chickens at 6 weeks or 19-22 months of age did not have anti-OA agglutinins as determined by the passive HA reaction; 2-day-old chicks also lacked the anti-OA activity. Inbred chickens kept in SPF isolators for 6 weeks, then transferred to a conventional environment for 7 weeks, produced anti-OA agglutinins. Inbred White Leghorn adult chickens conventionally reared had a high anti-OA agglutinin titer. It appeared that natural anti-OA agglutinin s are elaborated in response to environmental pathogens in certain lines of chickens. The titer in the individual chicken appeared as early as 10 weeks and was maintained until old age. The presence of natural anti-OA agglutinins did not prevent egg-laying but appears to have delayed it. The HA reaction is specific and can be absorbed.

Age Factors↗
PubMed1975

Peanut agglutinin, a new mitogen that binds to galactosyl sites exposed after neuraminidase treatment.

Peanut agglutinin, purified by affinity chromatography, agglutinates lymphocytes from mouse, rat, guinea pig, and man only after their treatment with neuraminidase. However, it stimulates only neuraminidase-treated rat and human cells. A similar number cell surface receptors for peanut agglutinin was found on neuraminidase-treated rat and mouse lymphocytes although the latter cells were not stimulated by the lectin. Galactose specifically inhibited the agglutination and stimulation of lymphocytes by peanut agglutinin. Sequential treatment of lymphocytes with neuraminidase and beta-galactosidase markedly reduced the response of the cells to stimulation by peanut agglutinin, soybean agglutinin, and galactose oxidase. It is suggested that the same galactosyl residue may be the target for the initial step in triggering lymphocytes by the above mentioned mitogens.

Agglutination Tests↗
PubMed1989

Actin cytoskeletal lesions in differentiated human colon carcinoma Caco-2 cells after exposure to soybean agglutinin.

We have investigated the effects of soybean agglutinin on the cytoskeletal element actin in differentiated Caco-2 cells. The actin cytoskeleton of the cells was visualized by fluorescence microscopy using 7-nitrobenz-2-oxa-1, 3-diazole phallacidin as a specific marker for F-actin. Compared with control Caco-2 cells no changes in the fluorescence pattern were observed after incubation with soybean agglutinin. However, using the deoxyribonuclease-I inhibition assay a dose-related response was noted in the increase of intracellular G-actin after a 2-hour incubation period with soybean agglutinin. Already after exposure for 15 min to soybean agglutinin a decrease in intracellular F-actin was demonstrable. This apparent depolymerization could be prevented by incubating the Caco-2 cells with soybean agglutinin and the appropriate monosaccharide simultaneously. The increase in the amount of G-actin appeared to be correlated with a shortening of microvilli on the Caco-2 cells.

Actins↗
PubMed1977

Wheat germ agglutinin inhibits basal- and stimulated-adenylate cyclase activity as well as the binding of [3H] caerulein to rat pancreatic plasma membranes.

Wheat germ agglutinin, but not concanavalin A or soybean lectin, inhibited the basal-and stimulated-adenylate cyclase activity which was present in a plasma membrane preparation from the rat pancreas. The inhibition by wheat germ agglutinin was rapid and sustained. It was of the non-competitive type and never exceeded 20% for Gpp (NH) p- and NaF-stimulated adenylate cyclase activity. The inhibition of secretin-stimulated activity was also non-competitive but more pronounced (57% inhibition at a wheat germ agglutinin concentration of 20 microgram/ml). For the C-terminal octapeptide of cholecystokinin-pancreozymin (OC-PZ)-stimulated cyclase, the inhibition amounted to 68% and was of a mixed type (both competitive and non-competitive). This last observation might be explained by the competitive inhibition exerted by wheat germ agglutinin on the binding of peptides of the OC-PZ family to their membrane specific receptors. The various inhibitory effects of wheat germ agglutinin were completely suppressed by incubating the membranes in the presence of ovomucoid, a N-acetyl-D-glucosamine rich glycoprotein. The possible functional implication of these results is discussed.

Adenylyl Cyclases↗
PubMed1978

Identification of the dietary lectin, wheat germ agglutinin, in human intestinal contents.

Plant lectins are known to have potent biological actions of normal and malignant cells. High concentrations of these lectins are present in many types of high residue diets. The specific binding of wheat germ agglutinin, a dietary plant lectin, to N-acetylglucosamine was used as the basis for purification of this lectin by biospecific chitin affinity chromatography. Subsequently, methods were developed for the extraction, purification, and identification of wheat germ agglutinin from fecal samples. Biologically intact wheat germ agglutinin was detected in ileostomy effluent and fecal collections from human subjects consuming a diet containing wheat germ. These studies demonstrate that wheat germ agglutinin can traverse the human small intestine intact. It is feasible that orally ingested wheat germ agglutinin and other plant lectins which interact with a wide variety of cell membranes may alter intestinal epithelial or bacterial cell function in the human bowel.

Feces↗
PubMed1976

Spontaneously occurring agglutinins in primate sera. II. Their classification and implications for the mechanism of antibody formation.

Spontaneously occurring agglutinins in animal sera are shown to fall into several categories, namely, 1. cold-reactive agglutinins; these often are nonspecific and act as autoagglutinins, 2. agglutinins reactive at room as well as refrigerator temperatures; these, like cold agglutinins, are usually IgM immunoglobulins which may be species-specific in their activity, or type-specific, notably, like anti-A and anti-B and 3. agglutinins reactive at body temperature, usually IgG immunoglobulins, and most often due to maternofetal incompatibility and transplacental immunization of the mother by fetal red cells. The naturally occurring cold autoantibodies are physiologic in nature and appear to be the raw materials for antibody production. This is postulated to be adaptive in nature by enzyme action, through in part genetically determined, as evidenced by the so-called constant polypeptide sections of the immunoglobulin molecules.

Animals↗
PubMed1989

Carbohydrate components recognized by the cone-specific monoclonal antibody CSA-1 and by peanut agglutinin are associated with red and green-sensitive cone photoreceptors.

Previous investigations have demonstrated that the monoclonal antibody CSA-1 and peanut agglutinin label specifically cone photoreceptor cells. In the present study, we compared the binding of CSA-1 and peanut agglutinin to that of the monoclonal antibodies COS-1 and OS-2, which have been shown to recognize the red/green- and blue-sensitive cone visual pigments, respectively. Using lectin and immunocytochemistry on serial semithin sections of the pig retina, we have demonstrated in the present study that both CSA-1 and peanut agglutinin label specifically the red-, and green-sensitive, but not the blue-sensitive cone cell outer segments. Peanut agglutinin does bind, however, to the cone matrix sheaths associated with all three types of cones. These observations support the idea that red-, and green-sensitive cone cells share some common molecular epitopes and may represent a differentiation line of cones, considerably different from that of blue-sensitive cones.

Animals↗
PubMed2001

Purification and characterization of a natural agglutinin in the hemolymph of the prawn Penaeus indicus H. Milne Edwards.

A natural agglutinin in the hemolymph of the marine prawn Penaeus indicus was isolated by gel filtration chromatography, purified using polyacrylamide gel electrophoresis, and characterized. Prawn agglutinin has a native molecular mass of 181 kDa and consists of two monomeric units (97 and 84 kDa), maintains some agglutinating activity over a wide pH range (7-9), and is inactivated at 85 degrees C. The agglutinin was denatured upon mixing with trichloroacetic acid, phenol, chloroform, and 45% ammonium sulfate. It was also sensitive to trypsin digestion. The results indicate that prawn agglutinin is proteinaceous in nature, with agglutinating, hemolytic, and antibacterial properties against marine bacteria and erythrocytes with carbohydrate binding sites.

Agglutinins↗
PubMed1994

Cholinesterases and peanut agglutinin binding related to cell proliferation and axonal growth in embryonic chick limbs.

Embryonic cholinesterases are assigned important functions during morphogenesis. Here we describe the expression of butyrylcholinesterase and acetylcholinesterase, and the binding of peanut agglutinin, and relate the results to mitotic activity in chick wing and leg buds from embryonic day 4 to embryonic day 9. During early stages, butyrylcholinesterase is elevated in cells under the apical ectodermal ridge and around invading motoraxons, while acetylcholinesterase is found in the chondrogenic core, on motoraxons and along the ectoderm. Peanut agglutinin binds to the apical ectodermal ridge and most prominently to the chondrogenic core. Measurements of thymidine incorporation and enzyme activities were consistent with our histological findings. Butyrylcholinesterase is concentrated near proliferative zones and periods, while acetylcholinesterase is associated with low proliferative activity. At late stages of limb development, acetylcholinesterase is concentrated in muscles and nonexistent within bones, while butyrylcholinesterase shows an inverse pattern. Thus, as in other systems, in limb formation butyrylcholinesterase is a transmitotic marker preceding differentiation, acetylcholinesterase is found on navigating axons, while peanut agglutinin appears in non-invaded regions. These data suggest roles for cholinesterases as positive regulators and peanut-agglutinin-binding proteins as negative regulators of neural differentiation.

Acetylcholinesterase↗
PubMed1988

Regeneration of the cell wall in protoplasts of Candida albicans. A cytochemical study using wheat germ agglutinin and concanavalin A.

To assess the dynamics of synthesis of the wall by regenerating Candida albicans protoplasts deposition of chitin and mannoproteins were investigated ultrastructurally using wheat germ agglutinin conjugated with either horseradish peroxidase or colloidal gold, and Concanavalin A coupled to ferritin respectively. Freshly prepared protoplasts lacked wheat germ agglutinin receptor sites but after 1-2 h of regeneration, they were detected. After 4-5 h of regeneration, the cell wall showed a discrete structure which was only labelled with wheat germ agglutinin in thin sections. At this stage of regeneration the outermost layer of the wall was labelled with clusters of Concanavalin A-ferritin particles. After 8 h regeneration, the cell wall appeared compact, and homogenously marked with wheat germ agglutinin whereas only the surface layers appeared consistently labelled with Concanavalin A-ferritin. From these observations we conclude that C. albicans protoplasts are able to regenerate in liquid medium a cell wall consisting of a network of chitin fibrils and mannoproteins at least (glucan polymers were not determined in the present cytological study). The former are the fundamental component of the inner layers at early stages of regeneration, whereas the latter molecules are predominant in the outer layers of the wall.

Candida albicans↗
PubMed1984

Binding of concanavalin A and wheat germ agglutinin by murine peritoneal macrophages: ultrastructural and cytophotometric studies.

Concanavalin A and wheat germ agglutinin were employed in conjunction with the horseradish peroxidase-diaminobenzidine method for the detection of sugar residues on the surface coat of exudate and resident murine peritoneal macrophages. Electron microscopical and cytophotometric techniques were used for the visualization and quantification of the final reaction product on the surface of cells. After incubation with concanavalin A and wheat germ agglutinin, both exudate and resident macrophages showed readily detectable final reaction product indicating the presence of numerous, easily accessible, alpha-methyl-D-mannosyl and N-acetyl-D-glucosaminyl residues on their surface. The binding of concanavalin A was higher with resident than with exudate macrophages. With wheat germ agglutinin, a different pattern of lectin binding was observed: more electron-dense product was deposited on exudate than on resident macrophage surfaces. The binding of concanavalin A and wheat germ agglutinin to macrophages was inhibited by the competing sugars alpha-methyl-D-mannoside and N-acetyl-D-glucosamine, respectively.

Animals↗
PubMed1998

Regulated expression of keratan sulphate and peanut agglutinin binding sites during organogenesis in the developing chick.

Keratan sulphate proteoglycans are potentially important during development and are possible binding molecules for the lectin, peanut agglutinin, a marker for areas that are inhibitory for axonal growth in early embryos. The present study describes the spatiotemporal distributions of keratan sulphate epitopes and peanut agglutinin binding sites during organogenesis in the developing chick from E5 to hatching. The widespread distributions of these molecules did not often overlap but clearly delimited different carbohydrate compartments demonstrating that peanut agglutinin does not necessarily bind to keratan sulphate proteoglycans. These markers were mostly extracellular but keratan sulphate, in particular, was found within certain specific cells in cartilage, gonad, heart and pancreas, at certain ages. The presence of keratan sulphate in putative germ cells during their migrations and in the gonads may be of particular importance. Their distributions generally evoke modulation of adhesion allowing cell migrations or morphogenetic movements related to epitheliomesenchymal interactions, but may also suggest an involvement in axonal guidance in skin, cartilage, gut and possibly heart. Furthermore, in the kidney, peanut agglutinin binding sites seem to be related to the functional differentiation of the nephrons.

Animals↗