concanavalin-a has been researched along with Leukemia--Myeloid--Acute* in 11 studies
11 other study(ies) available for concanavalin-a and Leukemia--Myeloid--Acute
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Monitoring of urine nitric oxide (NO) related substrates and immunological competence in hematological malignancy.
It has been reported that concentrations of neopterin in the urine are changed according to the host immunological conditions. In the present study, we measured urinary concentration of neopterin in patients with malignant hematological disorders and investigated the relationship between urinary neopterin levels and laboratory indices for cellular immunity. Urine neopterin levels were correlated with serum sIL-2R levels in the patients with malignant lymphoma, and inversely correlated with lymphocyte reactivity with ConA in the patients with acute myelocytic leukemia. However, no significant correlation was observed between urine neopterin levels and lymphocyte reactivity with phytohemagglutinin and pokeweed mitogen, CD4/8 ratio, CD56+ 16+ subset or serum IFN-gamma levels. In the patients with malignant lymphoma, parallel changes in serum sIL-2R and urine neopterin were observed. The presented results suggest that urine neopterin levels are related to the activation of T cells in malignant lymphoma. Topics: Adult; Aged; Concanavalin A; Female; Humans; Leukemia, Myeloid, Acute; Lymphoma; Male; Middle Aged; Neopterin; Receptors, Interleukin-2 | 2002 |
Alternative myelomonocytic differentiation of HL-60 reflects dual prospective potency of promyelocytes in human.
The permanent promyelocytic cell line HL-60 was subjected to stimulation with dimethyl sulfoxide (DMSO) and retinoic acid (RA), as well as 12-O-tetradecanoylphorbol-13-acetate (TPA) and lymphokine conditioned media for the induction of granulocytic or monocytic differentiation, respectively. Cells were investigated cytochemically using alpha-naphthylacetate esterase (acid esterase; AcE), naphthol AS-D chloroacetate esterase, and peroxidase reactions. In addition, the granulocyte or monocyte specific isoenzyme patterns of AcE as an intracytoplasmic property and the immunoreactivity to monoclonal antibodies recognizing granulocytes and monocytes (Ki-M2, Ki-M5) or monocytes alone (Ki-M1) were considered. The results indicated that HL-60 cell line bear the potency to evolve into granulocytes as well as monocytes. Additional studies performed on normal human bone marrow stained for AcE led to the conclusion that the myeloid cell line remains bipolar until the maturation stage of promyelocytes. Myelocytes being AcE positive only in 11.5 +/- 5.0 are heterogeneous and display the first indications of separated monocytic or granulocytic differentiation. Topics: Antibodies, Monoclonal; Cell Differentiation; Cell Line; Concanavalin A; Dimethyl Sulfoxide; Esterases; Granulocytes; Humans; Immunoenzyme Techniques; Leukemia, Myeloid, Acute; Lymphocytes; Lymphokines; Monocytes; Peroxidase; Phenotype; Tetradecanoylphorbol Acetate; Tretinoin | 1984 |
Modifying the biological response in acute myeloid leukemia. II. Effect of BCG and leukemic cells on lymphocyte response to mitogens, and on helper and suppressor activity.
Lymphocyte response to mitogens and to lymphocyte suppressor and monocyte helper activity was studied in 18 patients with acute myeloid leukemia in complete remission, and in 17 healthy controls. Ten patients were maintained with chemotherapy alone (CT), and eight received chemoimmunotherapy with BCG + leukemic cells (CIT). In late remission the mitogen responsiveness was increased in CT patients and decreased in CIT patients. No significant difference in lymphocyte suppressor activity could be demonstrated between patients and controls, or between CT and CIT. When autologous CIT monocytes were added to mitogen-stimulated lymphocytes they acted as helper cells. CT monocytes, in contrast, seemed to act as suppressor cells. Control monocytes also acted as helper cells, but to a significantly lesser degree than CIT monocytes. Topics: Concanavalin A; Humans; Leukemia, Myeloid, Acute; Lymphocyte Activation; Lymphocytes; Macrophages; Mitogens; Monocytes; Phytohemagglutinins; T-Lymphocytes, Helper-Inducer; T-Lymphocytes, Regulatory | 1982 |
The specific inhibition of cellular clonogenic proliferation using 211At labelled lectins and antibodies--I.
A monoclonal antibody with a broad anti-human leucocyte specificity, designated BK 19.45 and the plant lectin Concanavalin A have been labelled with the alpha-emitting cyclotron produced radiohalogen astatine-211. Both human and murine tumour cell lines and human leukemic bone marrow samples have been specifically labelled with these radioactive proteins. In all cases the amount of 211At bound to the cells is directly correlated with a decrease in cellular reproductive potential as shown by the ability of the cells to proliferate in a clonogenic assay. For the labelled monoclonal antibody experiments, the radiation dose needed to yield 37% cell survival, the D37 dose, may be achieved with an average of 12 211At atoms/cell. Topics: Animals; Antibodies, Monoclonal; Astatine; Cell Line; Cell Survival; Colony-Forming Units Assay; Concanavalin A; Dose-Response Relationship, Radiation; Humans; Lectins; Leukemia, Myeloid; Leukemia, Myeloid, Acute; Mice; Plasmacytoma | 1982 |
Modulation of cell competence for induction of differentiation in myeloid leukemic cells.
Topics: Animals; Cell Differentiation; Concanavalin A; Culture Media; Dexamethasone; Hematopoiesis; Insulin; Leukemia, Experimental; Leukemia, Myeloid, Acute; Lipopolysaccharides; Mice; Tetradecanoylphorbol Acetate | 1982 |
Development of capping ability during differentiation of HL-60 human promyelocytic leukemia cells.
Developmental changes in cell surface and cytoskeletal elements have been studied in human promyelocytic leukemia cels (line HL-60) which differentiate into functionally mature myeloid cells when grown in dimethyl sulfoxide (DMSO)-supplemented medium. Both differentiated and undifferentiated HL-60 cells bind fluorescent concanavalin A (F-Con A) in a diffuse pattern over the entire cell surface. As with normal neutrophils, pretreatment of the differentiated HL-60 cells with colchicine before incubation with Con A causes the formation of large cytoplasmic protrusions over which the lectin associates into a cap. On the other hand, similarly treated undifferentiated HL-60 cells do not form the cytoplasmic protuberances and are unable to cap the Con A. Transmission electron microscopy reveals that the number and distribution of microtubules and microfilaments change during differentiation. Thus, developing myeloid cells undergo important alterations in the structure and function of the cytoskeleton as they differentiate into mature phagocytes. Topics: Cell Differentiation; Cell Line; Centrioles; Colchicine; Concanavalin A; Cytoskeleton; Granulocytes; Hematopoiesis; Humans; Immunologic Capping; Leukemia, Myeloid, Acute; Microtubules | 1981 |
Characterization of mononuclear blood cell-derived differentiation inducing factors for the human promyelocytic leukemia cell line HL-60.
A search was made for physiologically produced differentiation inducing factor(s) (DIF) for the human promyelocytic leukemia cell line HL-60. Mononuclear blood cells, when stimulated with various mitogens, produced DIF, which induced differentiation of HL-60 into phagocytizing nitro blue tetrazolium reducing cells with the morphologic characteristic of granulopoietic or myelomonocytic cells. Induction of differentiation occurred equally well in serum-containing and serum-free media. Protein synthesis was necessary for elaboration of DIF, which seems to be of a protein nature inasmuch as it is destroyed by proteases. Gel chromatography showed that one or two species of DIF with apparent molecular weights of 40,000 and 25,000 were produced, depending on the type of mitogen used. At least the 40,000-molecular weight DIF was distinct from the colony stimulating activity (CSA), which was produced simultaneously. Our results suggested a role of lymphocytes and/or monocytes for modulation of myelomonocytic hematopoiesis not mediated by CSA. The physiologic importance remains, however, to be demonstrated. Topics: Cell Differentiation; Cell Line; Colony-Stimulating Factors; Concanavalin A; Dose-Response Relationship, Drug; Glycoproteins; Growth Inhibitors; Humans; Interleukin-6; Leukemia Inhibitory Factor; Leukemia, Myeloid, Acute; Lymphocytes; Lymphokines; Molecular Weight; Monocytes; Pokeweed Mitogens; Staphylococcal Protein A | 1981 |
Electron microscopic observations of cell coat of childhood leukemic cells using concanavalin A-horseradish peroxidase method.
Topics: Bone Marrow; Bone Marrow Cells; Child; Concanavalin A; Cytological Techniques; Horseradish Peroxidase; Humans; Leukemia, Lymphoid; Leukemia, Myeloid; Leukemia, Myeloid, Acute | 1977 |
Concanavalin A-induced agglutination of human leukemic and lymphoma cells.
With a newly developed turbidometric method, concanavalin A was shown to agglutinate normal lymphocytes, lymphoma cells, and leukemic cells from chronic lymphocytic leukemia and from acute myelocytic and lymphocytic leukemia. However, there was a marked difference in the kinetics of this agglutination process. Leukemic blast cells and cells from a patient with convoluted lymphoma agglutinated poorly in this system. Conversely, the degree of agglutination for chronic lymphocytic leukemia cells was greater than that for the blast cells and also slightly greater than that for normal lymphocytes. Cultured cells from a Burkitt's lymphoma (Raji) and from a patient with poorly differentiated lymphoma agglutinated very rapidly with concanavalin A. Prior incubation of all cell types with neuraminidase markedly enhanced the agglutination process similar to that of trypsinization. Thus, these studies illustrate the usefulness of this method in quantitating the kinetics of agglutination of various human neoplastic cell types by concanavalin A. Topics: Agglutination; Concanavalin A; Humans; Leukemia; Leukemia, Lymphoid; Leukemia, Myeloid, Acute; Lymphocytes; Lymphoma; Neuraminidase; Trypsin | 1976 |
Difference in the mobility of carbohydrate containing structures on the surface membrane of normal and malignant transformed cells.
Topics: Agglutination; Agglutination Tests; Animals; Binding Sites, Antibody; Carbohydrates; Cell Line; Cell Membrane; Cell Transformation, Neoplastic; Concanavalin A; Cricetinae; Fibroblasts; Fluorescent Antibody Technique; Glycogen; Leukemia, Experimental; Leukemia, Myeloid, Acute; Lymphocytes; Lymphoma; Male; Mice; Movement; Rats; Tritium; Trypsin | 1974 |
Mobility of carbohydrate-containing structures on the surface membrane and the normal differentiation of myeloid leukemic cells to macrophages and granulocytes.
Clones (D(+)) of a cultured line of myeloid leukemic cells can be induced to undergo normal differentiation to mature macrophages and granulocytes. There are also clones derived from the same cell line (D(-)) that could not be induced to differentiate. The carbohydrate-binding protein concanavalin A was used as a probe to study the mobility of carbohydrate-containing sites on the surface membrane of these cells. Changes in the distribution of concanavalin A binding sites on the surface membrane can be induced by concanavalin A. With the appropriate site mobility, this induction of a new distribution resulted in a concentration of concanavalin A-membrane site complexes on one pole of the cell to form a cap. D(+) and D(-) clones showed 50 and 5% of cells with caps, respectively, although both types of cells bound a similar number of concanavalin A molecules. Treatment of cells with trypsin increased cap formation from 5 to 40% in D(-) cells, but did not change the percentage of cells with caps in D(+) cells. The results show a difference in the mobility of concanavalin A binding sites in these two types of cells and suggest a difference in the fluid state of these carbohydrate-containing structures on the surface membrane. It is suggested that a gain of the ability of myeloid leukemic cells to undergo normal differentiation is associated with an increase in the fluidity of structures on the surface membrane where the concanavalin A sites are located. Differences in fluidity of specific membrane sites may also explain differences in the response of cells to other differentiation-inducing stimuli. Topics: Agglutination; Animals; Antigen-Antibody Reactions; Binding Sites; Carbohydrate Metabolism; Cell Differentiation; Cell Membrane; Clone Cells; Concanavalin A; Fluoresceins; Lectins; Leukemia, Myeloid, Acute; Leukocytes; Macrophages; Mice; Microscopy, Fluorescence; Neoplasm Proteins; Protein Binding; Tritium; Trypsin | 1973 |