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 rat immunized with mouse cerebellar cells were fused with mouse myeloma cells. One of the hybridomas secreted a monoclonal antibody that reacts with a surface antigen on vascular endothelial cells. The antibody stained endothelial cells lining blood vessels in brain, heart, lung, kidney, and liver. It did not, however, stain endothelial cells lining hepatic sinusoids. Parenchymal cells were always negative. So far, an antigen of similar tissue distribution has not been described in the mouse and we have called it mouse endothelial surface antigen-1 (MESA-1). The antibody could be used as a highly specific usefulness for identifying endothelium-derived cells in culture has been demonstrated on cultures of dissociated mouse cerebellum, where it stained a subclass of fibronectin-expressing cells.
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PMID:A surface marker for murine vascular endothelial cells defined by monoclonal antibody. 706 19

A monoclonal antibody-producing hybrid cell line was obtained by fusing mouse myeloma cells with spleen cells from a mouse immunized with C6 glioma cells. This antibody binds to a specific cell-surface antigen that is present on C6 rat glioma cells, transformed astrocytes and oligodendrocytes, and a human glioma cell line but is absent on a normal glial cell line, fibroblasts, and primary cultures of astrocytes and oligodendrocytes. The antigen also appears on tumor tissue of transformed oligodendrocytes but not on normal brain tissue.
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PMID:Development of a monoclonal antibody against a tumor-associated antigen. 706 42

To study the mechanism of the effects of alpha-interferon (alpha-IFN) on chronic hepatitis B, we examined its effect on hepatitis B virus (HBV)-specific cytotoxic T cells (CTL). Using two different HBV-DNA transfected human myeloma cell lines, one expressing hepatitis B core antigen (HBcAg; C4) and the other expressing hepatitis B surface antigen (HBsAg; S6) as targets in cytotoxic tests in vitro, peripheral blood mononuclear cells obtained from chronic hepatitis B patients who were treated with alpha-IFN were examined for their cytotoxic activity against these transfectants. During the treatment with alpha-IFN, in association with a decline of serum alanine amino transferase levels, CTL activities were significantly reduced. An inhibition study in vitro revealed that alpha-IFN did not directly inhibit these CTL activities, indicating that alpha-IFN may inhibit the induction of CTL, and thereby may be related to the reduction of hepatocyte injury.
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PMID:Effect of alpha-interferon on hepatitis B virus-specific cytotoxic T cells. 762 Jan 3

Two new monoclonal antibodies, Immu-133 and Immu-409, were raised against the human acute myelogenous leukemia cell line (KG-1a) and human immature erythroleukemic cells (TF1). These monoclonal antibodies were isolated from two different fusions of mouse myeloma cells with mouse splenic lymphocytes. The immunofluorescence studies performed on various target cells showed that these antibodies recognized a surface antigen expressed selectively on KG-1a, TF1 cells and on human hematopoietic progenitor cells. They also stained endothelial cells used in immunochemistry both in frozen and paraffin embedded tissue sections. Immu-133 and Immu-409 immunoprecipitated a KG-1a cell surface protein with an apparent molecular weight of 110-115 Kd. Competitive binding assays performed with a panel of referenced CD34 monoclonal antibodies revealed that Immu-133 and Immu-409 are monoclonal antibodies restricted to different epitopes of the CD34 molecule.
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PMID:Isolation and characterization of two new monoclonal antibodies against the CD34 molecule. 768 38

The lack of apoptosis or programmed cell death in human tumor cells has been suggested to be one factor allowing uncontrolled growth of neoplasms. We have developed a mouse monoclonal antibody (MAb) that induces programmed cell death in a human acute leukemia cell line (KM-3) of the pre B-cell type. Stable, antibody-producing hybridomas were produced by fusing mouse myeloma cells to spleen cells from mice immunized with viable KM-3 cells. Incubation of KM-3 cells with the MAb (designated anti-BAL) resulted in growth inhibition and subsequent cell death within 2-3 days. Anti-BAL required cross-linking with a rabbit anti-mouse antibody to induce DNA fragmentation typical of apoptosis. Immunoblotting experiments with anti-BAL identified a 37-kDa protein, apparently different from any previously described apoptosis-related surface antigen. Strongest expression of the antigen was generally found on cells of lymphoid or myeloid origin. However, several other cell types such as fibroblasts and endothelial cells were also stained by anti-BAL in flow cytometry but less intensively. Despite the apparent presence of this cell surface-bound 37-kDa antigen on several normal and malignant cell types, anti-BAL induced cell death only in human malignant cell lines expressing a more immature phenotype.
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PMID:A cell surface antigen (BAL) defined by a mouse monoclonal antibody inducing apoptosis in a human lymphocytic leukemia cell line. 818 58

Recent immunophenotypic analysis has shown that the heterogeneous expression of the adhesion molecule VLA-5 classifies myeloma cells into VLA-5+ mature and VLA-5- immature subpopulations. To further clarify the two myeloma subpopulations, we generated a monoclonal antibody, MPC-1, by immunizing mice with an adherent human myeloma cell line, KMS-5. The MPC-1 antibody recognized a 48-Kd surface antigen on KMS-5 but not on U-266, a nonadherent human myeloma cell line. Specificity characterization showed that MPC-1 antigen was expressed on mature myeloma cells, normal plasma cells, and mature B cells, whereas pre-B cells and germinal center B cells lacked its expression. Monocytes and a human bone marrow stromal cell line, KM102, also expressed this antigen. Two subclones of MPC-1+ VLA-5+ (KMS-5Ad) and MPC-1-VLA-5+ (KMS-5NAd) were separated from the KMS-5 cell line. The KMS-5NAd adhered to KM102 more tightly than did the KMS-5NAd, and the U-266 (MPC-1-VLA-5-) displayed almost no adherence to the KM102. The adhesion of the KMS-5Ad was partially inhibited by the MPC-1 antibody. These results, taken together, suggest that the MPC-1 antigen serves as a differentiation marker for B-lineage cells, including plasma cells, and may function as an adhesion molecule involved in the interaction of mature myeloma cells with bone marrow stromal cells.
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PMID:Heterogeneous expression of a novel MPC-1 antigen on myeloma cells: possible involvement of MPC-1 antigen in the adhesion of mature myeloma cells to bone marrow stromal cells. 826 Jul 9

Although the hairy cells (HCs) of hairy cell leukaemia (HCL) are now thought to be a form of activated B cell, they have long been known to possess certain monocytoid characteristics. Since the proto-oncogene c-fms is a feature of cells of the monocyte/macrophage lineage, we examined HCs for c-fms expression. We found that approximately 80% of peripheral blood HCs expressed the c-fms protein (8/8 cases). Expression of the 150 kD protein by HCs was shown using three different techniques, APAAP, immunofluorescence and immunoprecipitation, using two different antibodies. Other mature B cell lymphoproliferative disorders examined (PLL, CLL and multiple myeloma) did not express c-fms. We also examined the c-fms expression of normal B-cells: both the in vivo activated (low density) fraction of tonsil B cells and tonsil B cells activated in vitro with SAC plus IL-2 expressed the c-fms protein. As in the case of monocytes c-fms expression by HCs was shown to be down regulated by its ligand M-CSF, and by TNF alpha, both caused a decrease in the receptor expression from 80% to 30% and in the intensity of staining from 6 to 3 x 10(4) molecules/cell. However, as for monocytes, GM-CSF treatment of HCs had no effect on the expression of c-fms; alpha IFN also had no effect. M-CSF treatment of HCs also induced phosphorylation of c-fms, and a number of other proteins, on tyrosine. However, M-CSF was unable to induce HC proliferation either alone or in combination with IL-2, IL-4 or IL-6; in addition it had no effect on HC proliferation induced by SAC, anti-mu or TNF alpha. In addition, M-CSF either alone, or in combination with the above cytokines, had no effect on the differentiated state of HCs as shown by both immunoglobulin secretion and surface antigen expression. M-CSF also had no effect on the morphology or long-term survival of HCs in culture. This study therefore demonstrates that both HCs and activated B-cells express c-fms, and that M-CSF binds to and activates its receptor on HCs. Although c-fms and several other proteins were shown to be phosphorylated in response to M-CSF, the functional consequences of this phosphorylation remain unclear.
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PMID:C-fms protein expression by B-cells, with particular reference to the hairy cells of hairy-cell leukaemia. 830 20

We have produced and characterized a murine-human chimeric antibody with specificity for the pre-S2 surface antigen of hepatitis B virus (HBV) in baculovirus-infected insect cells. Recombinant baculovirus carrying the cDNA coding for the heavy or light chain of the chimeric antibody was constructed and co-infected into insect cells. The chimeric antibody (BV-S2) expressed in the cells was purified by an affinity chromatography on Protein A-Sepharose 4B column and characterized by N-terminal amino acid sequencing, affinity determination for pre-S2 peptide, endoglycosidase digestion and Clq binding assay, which were then compared with those of the chimeric antibody H69K that has the same amino acid sequence as BV-S2, but produced from transfected murine myeloma cells. The N-linked glycosylation of the BV-S2 antibody was also analyzed by culturing the baculovirus-infected cells in the presence of tunicamycin. The results showed that the BV-S2 was secreted following correct removal of the leader peptides, contained N-linked carbohydrate at the heavy chain, and had the same binding affinity and Clq binding ability as H69K, suggesting that the BV-S2 chimeric antibody is functional and thus may be useful in the prevention of HBV infection.
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PMID:Characterization of a murine-human chimeric antibody with specificity for the pre-S2 surface antigen of hepatitis B virus expressed in baculovirus-infected insect cells. 857 64

Aneuploidy and lg light chain restriction were used as separate, independent tumor specific markers to study 26 patients with multiple myeloma to determine whether bone marrow B cells, as defined by CD19 expression, are clonally related to myeloma plasma cells. Specimens were characterized using multidimensional flow cytometry to identify the presence of clonality in both the B lymphoid and plasma cell populations using both surface and cytoplasmic staining with antibodies specific for kappa or lambda lg light chain In none of the patients with multiple myeloma were CD19+ cells found to be clonally restricted to kappa or lambda. The monoclonal plasma cells (MPC) were found to be uniformly negative for CD10, CD19, and CD34, while the CD19+ B lymphoid cells present within the samples expressed normal intensities and relationships of these antigens, which allowed them to serve as internal positive controls. Combined analysis of call surface antigen expression and DNA content allowed plasma cell populations to be characterized for aneuploidy without interference from normal bone marrow cells. The MPC, detected on the basis of bright CD38 expression (CD38+2), demonstrated DNA aneuploidy in 65% of cases (DNA index range of 0.9 to 1.3). These aneuploid DNA distributions had typical cell cycle profiles (including G1,S and G2+M) expected of a proliferating population. In all cases, DNA aneuploidy was confined almost entirely to the CD38+2, CD19- malignant plasma cells, while cells expressing CD19 were diploid. These results support the concept that myeloma is a disease process mediated by self-replicating, late compartments of B-cell ontogeny.
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PMID:Tumor-specific aneuploidy not detected in CD19+ B-lymphoid cells from myeloma patients in a multidimensional flow cytometric analysis. 869 10

A human monoclonal antibody (mAb), designated mNKES, was generated by fusing B cells isolated from an enlarged cervical lymph node of a patient with a carotid body tumor (CBT), with human myeloma cell line KR-12 (6TG). The reactivity of mNKES was tested by the indirect immunofluorescence method. The antigen defined by mNKES was expressed on Burkitt's lymphoma cell lines Raji, Daudi, and Ramos and on B lymphoblastoid cell line IM-9. In addition, mNKES reacted with T cells stimulated with recombinant interleukin-2 (rIL-2) obtained from normal healthy donors. However, mNKES did not react with normal resting human T, B, or adherent cells (monocytes/macrophages). When the reactivity of mNKES and mouse mAbs recognizing the human adhesion-associated antigen (CD10, CD11a, CD11b, CD11c, CD14, CD16, CD18, CD23, CD28, CD29, CD31, CD43, CD44, CD45RA, CD50, CD54, CD58, CD80, CD102, CD106, and HLA class I, and HLA class II antigen) with various cell lines was compared, mNKES reactivity was found to be unique, not resembling that of any of these mouse mAbs. Interestingly, mNKES specifically and rapidly (within 2 hr) induced homotypic cell aggregation of IM-9 cells. This mNKES-induced cell aggregation was completely blocked by the addition of EDTA and when incubated at 4 degrees C. The mAbs reactive with CD11a/CD18 (leukocyte function-associated antigen-1; LFA-1) and CD54 (intercellular adhesion molecule-1; ICAM-1) completely blocked the IM-9 cell aggregation induced by mNKES, and induction of IM-9 cell aggregation by mNKES was significantly blocked in the presence of the protein kinase C inhibitors sphingosine and H-7 and completely blocked by cytochalasin B and cytochalasin D, which inhibit microfilament formation. Regarding biological function, IM-9 cells bearing surface IgG (sIgG) effectively promoted IgG-secreting activity underlying the homotypic cell aggregation induced by mNKES. The surface antigen recognized by mNKES has a molecular size of about 55 kDa, as determined by immunoblotting analysis. These findings indicate that mNKES recognizes a novel adhesion-associated antigen distinct from any previously reported adhesion-associated antigens in terms of pattern of cellular distribution and biological function and that mNKES is the first human mAb found that rapidly induces homotypic cell aggregation and effectively promotes the IgG-secreting activity of human B lymphoblastoid cell line IM-9.
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PMID:A novel human monoclonal antibody rapidly induces homotypic cell aggregation and promotes antibody-secreting activity by human B lymphoblastoid cell line IM-9. 908 89


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