Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0023418 (leukemia)
93,477 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Guinea pig T lymphocyte proliferation induced by sodium periodate (NaIO4) or neuraminidase-galactose oxidase (NG) occurs when lymphocytes and macrophages are cultured together after treatment of either purified T lymphocytes or macrophages with these agents. Regardless of which cell initially bears the modified surface carbohydrate, lymphocyte proliferation requires the presence of viable homologous macrophages and fails to occur when they are replaced with fibroblasts, erythrocytes, L2C leukemia cells, thymocytes, PMN, line I hepatoma cells, or murine macrophages. Lymphocyte proliferation resulting from NaIO4 or NG treatment of lymphocytes is diminished when these cells are treated with proteolytic enzymes or aged in in vitro culture for 48 hr. By contrast, proteolytic enzyme treatment or in vitro aging has no effect on the ability of NaIO4 or NG-treated macrophages to induce lymphocyte proliferation. The requirement for macrophage-lymphocyte interaction in NaIO4 or NG-induced lymphocyte proliferation is indicative of a central role for the macrophage in the initiation of T lymphocyte proliferation.
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PMID:The requirement for macrophage-lymphocyte interaction in T lymphocyte proliferation induced by generation of aldehydes on cell membranes. 17 Mar 38

Interferon treatment appears to induce a number of changes in the plasma membrane of uninfected cells. Interferon treatment altered the surface exposure of gangliosides of both Ly and KB cell membranes. The differences were found in the amount and pattern of incorporation of tritium after galactose oxidase treatment. In AKR,C- (AKR-2B) mouse cells, not only was there an apparent increase in the number of intramembranous particles in response to treatment with interferon but also the kinetics of the increase followed that of the establishment of the antiviral activity. The buoyant density of plasma membrane was also found to be significantly increased in interferon-treated cells. Moloney murine leukemia virus produced in interferon-treated mouse thymus and bone marrow cells had a high particle to infectivity ration. This virus contained a prominent glycoprotein with a molecular weight of about 85,000. This large glycoprotein was only a very minor component of Moloney leukemia virus produced in control TB cells and might be an uncleaved precursor to gp 69-71.
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PMID:Membrane alterations following interferon treatment. 21 15

We have labeled surface glycoproteins of normal and malignant human blood leukocytes by the galactose oxidase-NaB3H4 and periodate-NaB3H4 labeling techniques. The labeled glycoproteins were separated by slab gel electrophoresis in the presence of sodium dodecyl sulfate and visualized by fluorography. The different types of normal blood cells could be distinguished by their surface glycoprotein patterns. The surface glycoproteins of cells from patients with acute lymphoblastic, myeloid, or monoblastic leukemia were different from those of normal cells. The leukemic cells could be classified by their surface glycoprotein patterns with respect to their relationships to normal blood cells, and an estimation of their degree of differentiation was obtained.
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PMID:Identification and characterization of normal and malignant human blood leukocytes by surface glycoprotein patterns. 29 63

Human and mouse lymphocytes were surface-labeled by lactoperoxidase-catalyzed iodination, or by galactose oxidase oxidation followed by reduction with tritiated sodium borohydride. The labeled cells were lysed with Nonidet P-40. Proteins binding to Helix pomatia A hemagglutinin (HP) were isolated by affinity chromatography on HP-Sepharose and analyzed by sodium dodecyl sulfate polyacrylamide gel electrophoresis and autoradiography. A major cell surface glycoprotein (apparent mol. wt. 150 000, using reducing conditions) on human lymphocytes was responsible for almost all binding of HP. This protein was present on normal and malignant thymus-derived lymphocytes, e.g. thymocytes, blood T cells and T leukemia cell lines. It was also found on chronic lymphocytic leukemia cells, one null cell leukemia line, one unidentified leukemia line, one lymphoblastoid cell line of B origin and on one stem cell lymphoma line. In contrast, this protein was not found on various B cells at different steps of differentiation, e.g. four B lymphoma lines or one myeloma line. It was also absent from a histiocytic leukemia line. However, two of the four B lymphoma lines and the myeloma line had another HP-binding surface glycoprotein (mol. wt. 200 000) instead of the 150 000 protein. Studies of mouse lymphocytes similarly showed that thymus-derived lymphocytes (normal and malignant) but not normal adult B cells expressed a major HP-binding surface glycoprotein of apparent mol. wt. 130 000 (reducing conditions).
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PMID:Helix pomatia A hemagglutinin: selectivity of binding to lymphocyte surface glycoproteins on T cells and certain B cells. 30 19

We have labelled the exposed surface glycoproteins of human blood T- and B-lymphocytes and cells from patients with chronic lymphocytic leukemia by the galactose oxidase-tritiated sodium borohydride method. The labelled glycoproteins were separated by polyacrylamide slab gel electrophoresis and visualized by autoradiography. The T- and B-lymphocytes show different and characteristic surface glycoprotein patterns. The surface glycoprotein patterns of the leukemic cells differ from those of normal, non-malignant lymphocytes. A relationship between the altered surface glycoprotein pattern of leukemic cells and the expression of leukemia-associated antigens is discussed.
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PMID:Different surface glycoprotein patterns on human T-, B- and leukemic-lymphocytes. 108 48

The human T leukemia line Jurkat maintains functional characteristics of normal T cells in responding to inducing stimuli by the release of interleukin 2 (IL 2). Presence of a phorbol ester during stimulation eliminated the requirement for specialized accessory cells in the response to cell mitogenic agents such as the lectin concanavalin A or treatment with neuraminidase and galactose oxidase. Antibodies directed against the T cell receptor-associated antigen T3 served as efficient stimuli, especially if aided by agents that cross-link immunoglobulin, indicating that a triggering signal is received by a T cell via aggregation of its antigen receptor complex. A Burkitt lymphoma cell line, Raji, was found to selectively trigger Jurkat cells, suggesting the ability of those cells to respond to certain foreign stimuli. The Jurkat cell line has been instrumental in the purification of IL 2 and cloning of the corresponding gene. Our data suggest it can also serve as a useful model for induction of T cell responses.
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PMID:Analysis of human T lymphocyte activation in a T cell tumor model system. 387 19

We investigated interferon (IFN) production by peripheral blood mononuclear cells from four patients with chronic OKT4 T-lymphocytic leukaemia and three patients with abnormal expansions of granular lymphocytes. No spontaneous production of IFN-gamma was found in supernatants of cultures from both patients and normal controls. However, whereas the enzyme galactose oxidase or staphylococcal enterotoxin B was able to induce IFN-gamma production by normal cells, no production could be obtained in the cells under study. The possibility that this lack of production might have been attributed to an excess of N-acetylneuraminic acid masking galactose residues or to a defect of monocyte accessory cells was ruled out either by pre-treating the cells with neuraminidase or by adding normal adherent cells to the cultures, both of which resulted in a lack of production. On the contrary, the calcium ionophore A23187 (considered to act as a second specific step, following oxidation of galactose residues, toward genetic derepression of IFN-gamma) induced considerable IFN-gamma production in all the three tested patients. It can be concluded that, although in rare cases, as previously reported by other authors, cells from patients with T or NK lymphoproliferative disorders may spontaneously produce IFN-gamma, this is not a general mechanism that underlies the disease. In fact, in all our cases a defect of IFN-gamma production was found. This defect seems due to an alteration at the membrane level of the galactose-containing glycoproteins and can be restored by induction with a calcium ionophore.
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PMID:Impaired gamma interferon production by cells from patients with lymphoproliferative disorders of mature T and NK cells. 392 10

Surface exposed membrane proteins of malignant cells may offer important clues about the differentiation stage of the cell or may contain proteins specific for the malignant state. We have studied the surface exposed membrane proteins of human acute myeloid leukemia cells employing the lactoperoxidase, periodate, or the neuraminidase/galactose oxidase ectolabeling procedures. One-dimensional membrane protein patterns were prepared from 20 patients, and from 19 patients, two-dimensional patterns were prepared according to O'Farrell. No consistent differences in membrane proteins could be found between patients classified as M1, M2, M4, or M5 (FAB classification). A diagram of membrane proteins from acute myeloid leukemia cells subjected to two-dimensional electrophoresis could be composed from the results obtained. About 25 different membrane proteins can be indicated. Two-dimensional patterns, after the various ectolabeling procedures, were also prepared from mature myeloid cells, visualizing about 18 different membrane proteins. Comparison of these and the undifferentiated myeloid leukemia cell pattern reveals some maturation-linked or leukemia-associated differences. The most relevant proteins will be discussed, along with their association with a recently described "malignancy marker" with a molecular weight of 68,000 daltons.
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PMID:Two-dimensional membrane protein patterns of acute myeloid leukemia cells and mature myeloid cells after various ectolabeling procedures. 632 77

An attempt has been made to prepare antibodies against leukaemia-specific surface antigens by immunizing (C57 B1/6 X C3H/He)F1 mice with formaldehyde-stabilized AKR leukaemic cells. The presence of antibodies was examined by indirect immunofluorescence microscopy (IFM) and the indirect antiglobulin rosetting reaction (IARR). Galactose oxidase treatment destroyed the ability of leukaemic cells to react with antibodies prepared in the hybrid mice, an effect that was reversed by treating the enzyme-modified cells with borohydride. Analysis by immunoprecipitation and polyacrylamide gel electrophoresis of leukaemic cells, labelled by the galactose oxidase/[3H]-NaBH4 technique, indicated that a group of glycoproteins of apparent molecular weight greater than 70 000 was involved. Antibodies could be raised in AKR mice to the same group of glycoproteins by immunization with irradiated leukaemic cells or irradiated neuraminidase-treated leukaemic cells. The level of antibody raised in AKR mice had no effect on the growth of leukaemic lymphoblasts introduced subcutaneously into the host. Antibodies prepared in hybrid mice against leukaemic cells also were absorbed by lymphoid cells of pre-leukaemic 6-month-old AKR mice, indicating that contrary to previous claims in the literature antigens detected by such antisera are not related to malignancy. Hybrid mouse serum cross-reacted with antigens from purified RNA virus isolated from Abelson lymphoma, as demonstrated by the immunoelectrophoretic blotting technique. The pattern of reactivity was not appreciably altered following the absorption of antibodies directed against leukaemic cells. It is concluded that the glycoproteins detected by us may not be viral antigens but normal high molecular weight lymphoid glycoproteins with altered glycosylation patterns that are induced when the viral genomes are expressed.
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PMID:Glycoproteins of the AKR leukaemia cell surface and their relevance to leukaemia-specific surface antigens. 636 29

The role of the carbohydrate portion of the receptor for IgE in the interaction with IgE was investigated. Membrane carbohydrates of rat basophilic leukemia (RBL) cells and rat mast cells (RMC) were labeled by treating the cells with galactose oxidase followed by [3H]-NaBH4. IgE receptors were separated from detergent solubilized membranes and examined by SDS-polyacrylamide gel electrophoresis (SDS-PAGE). Pretreatment with neuraminidase markedly increased the incorporation of 3H into both the total membrane extract and into the IgE receptors. SDS-PAGE analysis demonstrated the presence of galactose in all IgE-binding components of 2 RBL cell lines and the presence of sialic acid on the major IgE-binding component. Prior saturation of the cells with IgE did not prevent the carbohydrate labeling of the receptor, although it did block the labeling of its protein part, indicating that carbohydrates are not located in the binding site. Removal of terminal sialic acid residues with neuraminidase increased the affinity of the receptor for IgE without appreciably affecting the number of receptors per cell. In order to more drastically modify the receptor carbohydrates, RBL cells were grown in the presence of Tunicamycin (TN). TN was shown to markedly inhibit the incorporation of [3H]-glucosamine into the receptor. RBL cells grown in the presence of TN expressed fewer receptors at the cell surface, as judged both by ligand binding studies and external labeling procedures. These data cumulatively suggest that the carbohydrate moieties of the receptor are not directly located in the binding site of the IgE receptor; however, the TN studies suggest that receptor carbohydrate may play a role in transport of the receptor to the plasma membrane or in its orientation thereafter.
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PMID:Functional and partial chemical characterization of the carbohydrate moieties of the IgE receptor on rat basophilic leukemia cells and rat mast cells. 720 80


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