Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0026764 (multiple myeloma)
 36,148 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Spleen cells from a DBA/2 mouse immunized with RL male 1 tumor cells, a radiation induced BALB/c T-cell leukemia, were hybridized with the nonsecretor myeloma line NS.1. Four established hybrid cell lines continuously secreted antibodies that recognized a new alloantigenic specificity, tentatively called Ly-m22. This antigen is detectable on nearly 60% of lymph node cells, and 30% of spleen cells by direct cytotoxicity assay, but did not lyse significant number of cells of thymus and bone marrow. By absorption test, these lymphoid organs, i.e., lymph node, spleen, thymus, and bone marrow, were shown to express Ly-m22 determinant. The newly found antigen is expressed predominantly on T-cells. Analysis of BXD and SWXL recombinant inbred strains revealed close linkage between Ly-m22 and Ltw-4 loci on chromosome 1. The estimated recombination frequency is 0.027 +/- 0.081.
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PMID:Mouse alloantigen system Ly-m22 predominantly expressed on T lymphocytes and controlled by a gene linked to M1s region on chromosome 1. 633 54

Spleen and lymph node cells of BALB/c mice, previously immunized with chicken thymic or bursa cells, were fused with Sp2/0-Ag14 mouse myeloma cells. Hybridomas from two fusions were selected on the basis of reactivity of their secreted antibodies towards thymic or bursal tissues in an indirect immunofluorescence assay. Four monoclonal antibodies reacting with different cell surface proteins of chicken lymphocytes were characterized, as follows. One antibody (IgM X.14) reacted only with cortical thymocytes, and precipitated material of apparent molecular weight (AMW) 65,000 (65 kD), 125 kD, and 180 kD from these cells. A second antibody (IgGl L.17) reacted with both bursa- and thymus-derived lymphocytes, but with different high molecular weight glycoproteins (AMWs 210 kD and 180 kD, respectively) on the two cell types. These proteins may be homologues of the previously described mouse B-220 and T-200 antigens. A third antibody (IgGl L.22) reacted with a protein of AMW 70 kD present on bursa-derived cells of some, but not all, chicken strains. Genetic analysis suggested that the presence of this protein was controlled by a single gene not closely linked to the major histocompatibility complex. A fourth antibody (IgG2b L.43) reacted with bursa-derived cells, macrophages and fibroblasts, but not with thymus-derived lymphocytes. L.43 precipitated material of AMW 23 kD from bursal cells.
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PMID:Monoclonal antibodies against chicken lymphocyte surface antigens. 633 57

Some murine monoclonal T lymphoma cells express a surface component that reacts with chicken antisera produced against the Fab fragment of normal mouse IgG. In the present study, we use a solid phase immunoadsorbent consisting of affinity-purified chicken anti-Fab coupled to Sepharose to isolate a product produced by the in vitro T cell line, WEHI-7.1. The affinity-purified T cell surface molecule (IgT) migrated on SDS-PAGE as a single band of approximately 65,000 daltons. The object of these studies was to produce xenoantisera against the purified T cell product cross-reactive with Ig determinants and to characterize the antisera. Rabbits immunized with this purified molecule produced antibodies that reacted with Fab fragments of polyclonal mouse IgG and with the myeloma proteins MOPC-104E and MOPC-41, as detected by enzyme-linked immunosorbent assay (ELISA). This binding was eliminated by adsorption of the antisera with normal polyclonal IgG; however, adsorption with fetuin did not significantly affect the reactivity of the antisera. Radioimmune precipitation assays revealed that the rabbit anti-IgT bound to normal murine spleen and thymus cells; this reactivity was abrogated by adsorption with insolubilized polyclonal IgG. Competition radioimmunoassays demonstrated that detergent extracts of the thymus and the spleen contained material that inhibited the precipitation of MOPC-41; nonlymphoid cells lacked such material. The rabbit anti-IgT serum blocked the binding of antigen by normal T cells; adsorption of the antiserum with polyclonal IgG-Sepharose abrogated this blocking capacity. A solid phase immunoadsorbent prepared from the IgG fraction of the rabbit anti-IgT isolated a single component from formic acid-solubilized mouse thymus. This molecule had an approximate mass of 65,000 to 70,000 daltons. The anti-IgT serum isolated surface IgM and IgD from lactoperoxidase-catalyzed radioiodinated B cells. The anti-IgT serum detected IgM and IgG in mouse serum with the use of immunoelectrophoresis. The anti-IgT immunoadsorbent isolated several components from normal mouse serum, that, when analyzed by SDS-PAGE under reducing conditions, revealed bands corresponding to mu-, gamma-, and light chains as well as components that migrated between mu- and gamma-chains, and another component with an approximate mass of 45,000 daltons. Our results with antibodies to a purified T cell product indicate that a surface component of normal T cells and certain monoclonal T cell tumor lines is serologically related to the Fab fragment of serum Ig and is implicated in the binding of antigen.
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PMID:Xenoantisera against a murine T cell tumor product cross-react with immunoglobulin Fab determinants. 635 Apr 58

Monoclonal antibodies ( MCAs ) have been derived from a fusion of P3-NS1/1-Ag 4-1 (NS1) myeloma cells and splenocytes immunized to human glioma cell line D-54 MG. MCAs 2F3 , 4C7 , and 5B7 were analyzed by cell surface radioimmunoassay (CS-RIA), quantitative absorption, indirect immunofluorescence, and peroxidase-anti-peroxidase (PAP) immunohistology of unfixed tissue samples. MCA 2F3 exhibits the most highly restricted pattern of reactivity we have observed, reacting only with 5/12 glioblastoma cell lines and 1/4 fetal skin lines by CS-RIA, and to 9/11 glioblastoma tissue samples by PAP and absorption analysis; this MCA is totally nonreactive with melanomas, neuroblastomas, meningiomas, and control non-central nervous system tumors, and to adult and fetal tissues including brain, thymus, spleen, liver, lung, heart, gut, skin, and muscle by PAP analysis. MCAs 4C7 and 5B7 demonstrate neuroectodermal tumor cross-reactivity profiles, reacting with either melanomas ( 5B7 ) or melanomas and neuroblastomas ( 4C7 ); both are reactive with fetal skin, brain, and thymus of less than or equal to 16 weeks of gestational age. Other than this latter fetal antigen reactivity, these MCAs share the same negative reactivity profile described above for MCA 2F3 . Data from experiments using control or 0.02% EDTA-treated confluent cell monolayers of D-54 MG as antibody absorbents showed that the antigens detected are present in the extracellular matrix material remaining following cell removal. The data presented here establish that these highly restrictive anti-human glioma cell line MCAs are expressed in primary human gliomas; that the markers defined are developmental in nature, in that they are expressed by human fetal tissue, but not by adult tissue; and that in conjunction with previously characterized specificities, these markers of antigenic heterogeneity will be valuable in model system studies of therapeutic response heterogeneity.
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PMID:Characterization of three restricted specificity monoclonal antibodies raised against the human glioma cell line D-54 MG. 637 21

A hybridoma clone secreting a monoclonal antibody, designated MA158.2, that reacts with an antigen expressed on lymphokine-treated macrophages was produced by fusion of mouse myeloma cells with rat spleen cells immunized against C57BL/6 peritoneal macrophages rendered tumoricidal in vitro by incubation with the lymphokine macrophage-activating factor. The specificity of the antibody for activated macrophages and lack of reactivity with histologically diverse cell types was determined by radioimmune indirect binding and flow cytometry. MA158.2 antibody binds to mouse peritoneal macrophages elicited by nonspecific inflammatory agents and to tumoricidal macrophages elicited with Corynebacterium parvum. Resident peritoneal, splenic, and alveolar macrophages were only weakly positive. Several macrophage cell lines (P388D1, WEH1-231, J774, RAW 264.7), murine fibroblasts, and neutrophils did not bind detectable amounts of MA158.2. Radioimmune indirect binding analysis demonstrated that cell suspensions prepared from C57BL/6 mouse spleen, thymus, and lymph node as well as polymorphonuclear leukocytes, lymphocytes, and T- and B-cell murine lymphomas were MA158.2 negative. Expression of the reactive antigen on the macrophage cell surface was enhanced 3-fold following in vitro activation of elicited macrophages with macrophage-activating factor and the kinetics of activation to the tumoricidal state paralleled the increased expression of the antigen recognized by MA158.2. MA158.2 is a rat IgG2a antibody containing a single specific heavy and light chain that does not detect a polymorphic determinant. This monoclonal antibody will be a useful tool for monitoring the efficacy of agents in activating murine macrophages to the tumoricidal state and in analyzing the sequence of biochemical events that culminate in macrophage activation.
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PMID:Identification and characterization of a monoclonal antibody to an antigen expressed on activated macrophages. 637 46

A monoclonal antibody, AE3.d3, derived from the fusion of rat splenocytes immunized against mouse brain with the myeloma SP2, has been produced, which has the property of inducing the proliferation of mouse lymphocytes. The mitogenic effect is highest in spleen and lymph node cells, where up to a 10-fold stimulation of 3H-TdR incorporation is observed. B lymphocytes are the most susceptible to this proliferative stimulus, and they are induced to differentiate into plaque-forming cells. T lymphocytes and "null" cells (defined by the absence of Thy-1 or Ig on their surface) do proliferate, although to a smaller extent. The T cell subpopulation, isolated from either spleen or thymus, requires additional "helper factors" in order to proliferate. The mitogenic response is not genetically restricted by H-2 type, and strains such as C3H/HeJ and CBA/N, in which B cell function is defective, as well as T cell-deficient strains such as BALB/c nude mice, are capable of responding to the stimulus of AE3.d3. Using immunofluorescence, we also examined the distribution of AE3.d3-positive cells in various lymphoid organs. The highest percentage of stained cells is found in the spleen (approximately 28%) and lymph node (18%), whereas only 14% of the bone marrow and 5% of the cells of the thymus are brightly stained with AE3.d3.
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PMID:A monoclonal antibody (AE3.d3) with mitogenic properties for murine B cells. 638 64

In animals and in man, diverse immunologic functions are mediated by specialized T-cell (thymus-derived lymphocyte) subsets that are distinguishable from one another on the basis of differences in cell surface determinants. Unfortunately, in humans, subset-specific antibodies have been difficult to generate. In this study, production of a murine monoclonal antibody specific for a subset of human T cells was achieved by fusing a sensitized B cell (bone marrow-derived cell) with a myeloma cell and isolating the antibody secreted by the resultant hybrid clone. This antibody binds 30-35% of peripheral T lymphocytes (T(a) (+) cells) but fails to bind remaining T lymphocytes (T(a) (-) cells), B lymphocytes, or monocytes. T(a) (+) and T(a) (-) subpopulations were separated with a fluorescence-activated cell sorter and their in vitro responses to various stimuli were assessed. T(a) (+) and T(a) (-) cells respond equally well to soluble antigens, allogeneic B cells, and autologous B cells, but only T(a) (+) cells respond to concanavalin A. T(a) (+) cells cultured in the presence of concanavalin A gradually lose the T(a) marker, an effect not observed after stimulation with phytohemagglutinin, soluble antigens, or alloantigens. These results suggest that the functional subpopulation of T cells defined by T(a) does not correspond to any previously described human T cell subset. Furthermore, somatic cell hybridization has been shown to be a feasible method for production of monoclonal antibodies specific for subpopulations of human lymphocytes.
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PMID:Functional characteristics of human T-cell subpopulations distinguished by a monoclonal antibody. 644 60

Monoclonal autoantibodies specific for the thymic hormone thymulin (FTS-Zn) were obtained by cell fusion with the use of spleen cells from nonimmunized autoimmune B/W or diabetic (db/db) mice and myeloma cells. Culture supernatants were screened for their ability to inhibit in vitro and in vivo the biologic activity of synthetic and natural hormone and to bind specifically to thymic epithelial cells in indirect immunofluorescence. This binding was completely abolished by preincubation of the antibodies with the synthetic hormone. These monoclonal autoantibodies were shown by double labeling experiments to bind the same thymic epithelial cells as the antithymulin monoclonal antibodies prepared by immunization with thymic epithelial cells. These autoantibodies directed against the low m.w. thymic hormone thymulin do not explain the low thymulin serum level found in those mice because there is a concomitant decrease in the number of thymulin-containing cells in the thymus, but they could play a role in the maintenance of T lymphocyte defects observed in these mice.
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PMID:Autoimmune mice develop antibodies to thymic hormone: production of anti-thymulin monoclonal autoantibodies from diabetic (db/db) and B/W mice. 653 99

In previous studies it was demonstrated that rabbit anti-mouse thymus sera (RAT) but not rabbit anti-brain serum (RABR), block the activity of cytotoxic T lymphocytes (CTL). The aim of the present study was to determine to what extent inhibition of the lytic activity of CTL reflects inhibition of the attachment of CTL to target cells. Following heat inactivation RAT and RABR were absorbed with mouse liver and kidney and tested for their capacity to inhibit the attachment of sensitized peritoneal exudate T lymphocytes (PEL) to various target cells. The exposure of sensitized PEL to RABR markedly reduced their capacity to form conjugates with either allogeneic or syngeneic target cells. In contrast, RAT inhibited only the formation of conjugates of sensitized PEL with the respective target cells against which they were immunized. Treatment with RAT had no effect on the formation of conjugates with irrelevant target cells. Additive experiments in which PEL were exposed to a mixture of both RAT and RABR indicated that the two antisera blocked different types of attachment. The inhibitory activity of RAT on conjugate formation could be removed by absorption with B-lymphoma cells but not with myeloma cells. Analysis of the correlation between the inhibitory effect of RAT on cell-mediated lysis (CML) and on conjugate formation revealed that the serum was about twice as effective in its capacity to inhibit CML as to inhibit the attachment of PEL to target cells. The results indicate that while RABR inhibits non-specific attachment of CTL which does not lead to cell lysis. RAT exerts its effect by interfering with immunologically specific functional receptors on CTL.
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PMID:Cell surface receptors involved in the attachment of murine cytotoxic T lymphocytes to target cells - a study with xenoantisera to T-cell antigens. 660 81

The effect of the calf thymus extract thymustimulin (Tp-1) on lymphocyte subpopulations of 12 patients affected by lymphoproliferative disorders with low T-cell level was studied. T and B cells of four patients with non-Hodgkin lymphoma, three with Hodgkin's disease, one with myeloma and four with chronic lymphatic leukemia were evaluated before and after treatment for 3 months with Tp-1. The total number and the percentage of T-cells increased significantly (p less than 0.05) in patients with non Hodgkin lymphoma, Hodgkin's disease and myeloma and only numerically in patients with chronic lymphatic leukemia, while no significant change of the total WBC count and of the total number and percentage of B-cells occurred in any patients. These results suggest that Tp-1 treatment might be effective in restoring immunocompetence in patients with T-cell deficiency secondary to lymphoproliferative disorders.
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PMID:Effect of treatment with thymustimulin (Tp-1) on T and B cells in lymphoproliferative disorders. 660 85


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