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PubMed1986

Inhibition of human lymphocyte transformation by tomato lectin.

The lectin from tomato (Lycopersicon esculentum) fruits was found to be non-mitogenic for human lymphocytes in culture and actually suppressed spontaneous DNA synthesis. It also inhibited the transformation of human peripheral blood lymphocytes induced by recall antigens or allogeneic cells in vitro. This inhibition was most effective when the lectin was present from the beginning of the culture period, and could be abolished by the simultaneous addition of oligomers of N-acetylglucosamine. The tomato lectin was able to bind to several major lymphocyte cell surface glycoproteins, but not to the major histocompatibility (HLA) antigens. The binding of tomato lectin to lymphocytes could be inhibited by wheat germ agglutinin (WGA), but not by concanavalin A. Tomato lectin could agglutinate monocytes and B lymphocytes as well as T lymphocytes. Human serum used to supplement the culture medium supporting lymphocyte transformation was equally effective after passage through a tomato lectin-Sepharose column. The inhibition of lymphocyte transformation brought about by tomato lectin was not stopped by exogenously added interleukin 1 and/or interleukin 2, even at very high concentrations.

Binding, Competitive↗

PubMed1992

Spurious thrombocytopenia due to EDTA-independent cold-reactive agglutinins.

Spurious thrombocytopenia is an infrequent laboratory problem that may be confused with true thrombocytopenia, leading to inappropriate testing to determine the cause of the thrombocytopenia. Spurious thrombocytopenia has been associated most often with temperature-independent, ethylene diaminetetraacetic acid (EDTA)-dependent antibodies. Two cases of spurious thrombocytopenia due to temperature-dependent, EDTA-independent agglutinins are reported. Modification of sample processing to maintain the sample near 37 degrees C was necessary to obtain accurate platelet counts. The initial blood cell histograms were abnormal in each case, leading to the diagnosis. However, in one case significant platelet agglutination was not flagged on a subsequent histogram. These cases illustrate that spurious thrombocytopenia may be caused by more than one type of agglutinin and that not all samples with in vitro agglutination are detected by blood cell histograms.

Aged↗

PubMed1973

Surface changes in temperature-sensitive Simian virus 40-transformed cells.

A binding assay that shows consistent differences in the amounts of tritium-labeled concanavalin A that bind to normal and virally transformed cells was used to study the kinetic changes of cell surface in SV40-transformed 3T3 cells that express the transformed phenotype in a temperature-sensitive manner (tsSV3T3 cells). The increase in concanavalin A binding, which paralleled the appearance of the characteristics of transformed cells, was dependent on the synthesis of cellular DNA. In agreement with the results of binding studies, exponentially growing tsSV3T3 cells agglutinated at much lower lectin titers (concanavalin A as well as wheat-germ agglutinin) at 32 degrees than at 39 degrees .

Agglutination↗

PubMedDate not supplied

Purification of an N-acetyl-D-glucosamine specific lectin (P.B.A.) from epidermal cell membranes of Pieris brassicae L.

We report the isolation and the purification of an N-acetyl-D-glucosamine specific lectin capable of agglutinating either fixed trypsinized rabbit erythrocytes or chitin particles. An agglutinin assay based on the affinity of this lectin for the chitin was devised with fluorescent particles of scorpion cuticle to measure lectin activity during purification steps. Lectin was isolated from epidermal cell membranes; its molecular weight was determined by gel filtration and polyacrylamide electrophoresis in sodium dodecyl sulfate. Mr was estimated to be 43,000. Lectin could be constituted by two subunits. Mr of which was estimated to be 23,000. The specificity of this lectin against N-acetyl-D-glucosamine and its oligomers suggests a possible role in the dynamics of these saccharides during the cuticle cycle.

Acetylglucosamine↗

PubMed1977

A Waldenström macroglobulin that is both a cold agglutinin and a cryoglobulin because it binds N-acetylneuraminosyl residues.

A purified human monoclonal IgM(kappa) (cold agglutinin MKV) has been characterized as both a cold agglutinin and a cryoglobulin. Since its reactivity with human erythrocytes but not with dog erythrocytes is reduced by treatment of the cells with ficin and its reactivity with both is abolished by treatment of the cells with neuraminidase, it has by definition Pr(2) specificity [Roelcke, D. (1974) Clin. Immunol. Immunopath. 2, 266-280]. Presumably, the membrane receptors for cold agglutinin MKV are sialic acid-containing glycoproteins in human cells and sialic acid-containing glycolipids in dog cells. Agglutination of erythrocytes is specifically inhibited by II(3)-N-acetylneuraminosyllactosylceramide (GM(3)) and N-acetylneuraminosylparagloboside but not by their N-glycolylneuraminosyl forms or by lactosylceramide or paragloboside, and the reactivity of neuraminidase-treated cells can be restored by allowing them to absorb either GM(3) or N-acetylneuraminosylparagloboside. When large amounts of ganglioside are absorbed, the cells are agglutinated not only in the cold, but also at 37 degrees , showing that the density of receptor sites on the erythrocyte surface can influence the thermal amplitude of cold agglutinins. Liberation of sialic acid from cold agglutinin MKV by treatment with neuraminidase (acylneuraminosyl hydrolase; EC 3.2.1.18) does not affect its agglutinating properties but the asialoprotein is no longer a cryoglobulin. Apparently the physical basis for its precipitation in the cold is the intermolecular immune binding of N-acetylneuraminosyl residues.

Adult↗

PubMed1999

Inverse association between IgG-anti-kappa and antierythrocyte autoantibodies in patients with cold agglutination.

It has been known for a long time that IgG-anti-F(ab')(2) antibodies (Abs) are able to suppress the B-cell response. We showed that natural IgG-anti-F(ab')(2) autoantibodies appear in the serum of patients with cold agglutination. If the anti-F(ab')2 Ab suppresses cold agglutinin (CA)-producing B cells, one would expect an inverse correlation between the titers of these two Abs. Our study confirmed this correlation. Subsequent experiments showed that some anti-F(ab')(2) Abs bind to the hinge region of IgG. It was difficult to explain how this Ab suppresses CA-producing B cells, which are of IgM isotype. Here we show that patients with cold agglutination have an IgG-anti-kappa light chain autoantibody in their serum. This is another member of the anti-F(ab')(2) Ab group. Because the vast majority of CAs are IgM-kappa Abs, the anti-kappa Ab might suppress CA-producing B cells. If this is the case, there should be an inverse association between the titer of anti-kappa Ab and CA. In a group of 302 patients, we found that high titers of the anti-kappa Ab correlate with low titers of CA and vice versa (P =.009). Interestingly, this association is found only in patients whose disease is caused by noninfectious agents, including mainly B-cell proliferations (P =.0058). Our data show that the inverse correlation is not confined to a particular CA autoantibody specificity. The results are discussed in the light of recent findings showing that anti-IgM Abs may either inactivate or kill tumoral B cells by apoptosis.

Anemia, Hemolytic, Autoimmune↗

PubMed1983

Trypanosoma rhodesiense bloodstream trypomastigote and culture procyclic cell surface carbohydrates.

Bloodstream trypomastigote and culture procyclic (insect midgut) forms of a cloned T. rhodesiense variant (WRAT at 1) were tested for agglutination with the lectins concanavalin A (Con A), phytohemagglutinin P (PP), soybean agglutinin (SBA), fucose binding protein (FBP), wheat germ agglutinin (WGA), and castor bean lectin (RCA). Fluorescence-microscopic localization of lectin binding to both formalin-fixed trypomastigotes and red cells was determined with fluorescein isothiocyanate (FITC)-conjugated Con A, SBA, FBP, WGA, RCA, PNA (peanut agglutinin), DBA (Dolichos bifloris), and UEA (Ulex europaeus) lectins. Electron microscopic localization of lectin binding sites on bloodstream trypomastigotes was accomplished by the Con A-horseradish peroxidase-diamino-benzidine (HRP-DAB) technique, and by a Con A-biotin/avidin-ferritin method. Trypomastigotes, isolated by centrifugation or filtration through DEAE-cellulose or thawed after cryopreservation, were agglutinated by the lectins Con A and PP with agglutination strength scored as Con A greater than PP. No agglutination was observed in control preparations or with the lectins WGA, FBA or SBA. Red cells were agglutinated by all the lectins tested. Formalin-fixed bloodstream trypomastigotes bound FITC-Con A and FITC-RCA but not FITC-WAG, -SBA, -PNA, -UEA or -DBA lectins. All FITC-labeled lectins bound to red cells. Con A receptors, visualized by Con A-HRP-DAB and Con A-biotin/avidin-ferritin techniques, were distributed uniformly on T. rhodesiense bloodstream forms. No lectin receptors were visualized on control preparations. Culture procyclics lacked a cell surface coat and were agglutinated by Con A and WGA but not RCA, SBA, PP and FBP. Procyclics were not agglutinated by lectins in the presence of competing sugar at 0.25 M.(ABSTRACT TRUNCATED AT 250 WORDS)

Agglutination Tests↗

PubMedDate not supplied

[Infection with species of the genus Bordetella in adults, a factor in maintaining morbidity for whooping cough. Serological studies].

A number of 1021 serological investigations were performed to identify agglutinating antibodies against B. pertussis and B. parapertussis in adults. The investigations were initiated to study the presence of agglutinins in serum, in response to a previous infection with Bordetella species. The serological tests revealed the presence of agglutinating antibodies at titres considered to be positive (> or = 1/320) in 136 (13.3%) sera. The results obtained suggest that pertussis is relatively frequent in adults, and must be considered as a factor of maintaining morbidity.

Adolescent↗

PubMed1987

Cryptic cold agglutinin activity of monoclonal macroglobulins.

One hundred and twenty sera with monoclonal immunoglobulin M's (IgM's) were tested for cryptic cold agglutinin activity against papain- and neuraminidase-treated adult and cord red blood cells (RBC). Fifteen sera (12.5%) agglutinated papain-treated RBC. Fourteen of these 15 sera also agglutinated neuraminidase-treated RBC. Ten additional sera agglutinated neuraminidase-treated but not papain-treated cells. Three patterns were observed among agglutinators of papain-treated RBC: either predominant agglutination of adult RBC, or of cord RBC or equal reaction, thus resembling I, i and non-Ii patterns of conventional cold agglutinins. We propose to call these patterns, tentatively, Icr (cr for cryptic), icr, and non-Iicr, respectively. Purified monoclonal IgM's retained the above patterns. Eluates from enzyme-treated cells contained monoclonal IgM's. Investigation of neuraminidase-treated RBC has shown that in distinction to T-anti-T system (Thomsen-Friedenreich receptor system), the majority of sera with monoclonal IgM's agglutinated more strongly adult RBC, and some agglutinated more strongly cord RBC. There was no loss of agglutinating activity after repeat freezing and thawing of the sera. Thus, it seems that monoclonal IgM's which react with neuraminidase-treated RBC detect antigenic determinants different from the T antigen. Cryptic CA activity of IgM's should be added to the list of antibody activities of these monoclonal immunoglobulins.

Adult↗

PubMed1982

Stimulation of B cells, but not T cells or thymocytes, by a sialic acid-specific lectin.

Haemolymph of the American lobster, Homarus americanus, contains several lectins. One of these, lobster agglutinin 1 (LAg1) is specific for N-acetylneuraminic acid and agglutinates mouse and human erythrocytes. In addition, this lectin agglutinates peripheral T cells and cortisone-resistant thymocytes, but agglutinates whole thymocytes poorly. Because this material is being used to prepare purified populations of cortical thymocytes, and then to study their maturation, it was important to determine if it is mitogenic for thymocytes and T cells. Thus, the studies described here were conducted to find if LAg1 is a mitogen for mouse lymphocytes, and if so for what cell populations. The data show that purified LAg1, but not purified lobster agglutinin 2 (LAg2) is a mitogen for mouse spleen cells, and that LAg1 is a polyclonal activator. Furthermore, LAg1 is a B-cell mitogen since it stimulates nude spleen cells, nude spleen cells depleted of pre-T cells, and normal spleen cells which have been treated with rabbit anti-mouse brain antiserum and complement. Moreover, LAg1 does not stimulate division by thymocytes or T cells, that is, spleen cells which do not adhere to nylon wool columns. Mitogenic activity of LAg1 but not of LPS is inhibited by N-acetylmannosamine, demonstrating that the mitogenic effects of LAg1 are unlikely to be due to contaminants.

Animals↗

PubMed1969