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)

Two IgG1 type monoclonal antibodies ALT-01 and ALT-04 were prepared by two different immunization schedules. ALT-01 was generated by fusing murine myeloma NS-1 cells with splenocytes from a BALB/c mouse immunized by human lung squamous carcinoma cells, which were coated by antisera to mixed human lymphocytes. For preparation of ALT-04, human lung squamous carcinoma xenograft-bearing nude mice were injected I. P. with the spleen cells of normal BALB/c mice in order to acquire immunofunction. The spleen cells from these tumor-bearing nude mice were fused with NS-1 cells. Then, these hybridomas were screened and cloned for 3 times. Two antibodies were shown to recognize the surface antigen on human lung carcinoma cells and several kinds of tumor cell lines but not those on normal cell lines. ALT-01 reacted to neither human lung carcinoma tissue nor its xenograft. ALT-04 reacted to human lung carcinoma tissue, of which, reaction to adenocarcinoma was the strongest but not to various normal tissues. Immunoprecipitation followed by SDS-polyacrylamide gel electrophoresis and autoradiography was used to detect the associated antigen in 35S-labeled human lung carcinoma cells. Antigens, reacting to ALT-01, show one band of Mr 38,000 but those to ALT-04 reveal two bands of Mr 48,000 and 36,000.
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PMID:[Reactivity of monoclonal antibodies ALT-01 and ALT-04 and identification of lung cancer-associated antigens]. 344 54

The hepatitis B surface antigen (HBsAg) is highly immunogenic and induces an antibody response which is protective in vivo against hepatitis B virus (HBV) infection. Human monoclonal antibodies specific for HBsAg were produced, which could have potential therapeutic applications. Lymphocytes obtained from a vaccinated donor were stimulated in vitro and fused with the human myeloma cell line GM 4672, and eight hybridomas were obtained. Three of these clones, which reacted in an ELISA against the HBsAg vaccine, were expanded, subcloned and further analyzed. The subclones E7C2, C4C10, and D5B2 were able to bind to different HBsAg preparations, which express various subtypes, and recognized the major HBsAg peptides in Western blot analysis. Cross-inhibition experiments showed that E7C2, C4C10 and D5B2 are directed against the same epitope and have an affinity constant ranging from 5 X 10(7) to 3.3 X 10(9) M. Furthermore, these antibodies stained the surface and cytoplasm of the HBsAg-secreting cell lines PLC/PRF/5 and 4.10. The production of immunoglobulins varies from 0.3 to 1.3 micrograms/ml/10(6) and has remained stable over a period of 8 months. These human monoclonal antibodies, which appear to be directed against an antigenic determinant common to all HBsAg subtypes, could be useful in the study of HBV-related liver diseases as well as in their diagnosis and experimental therapy.
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PMID:Preparation and characterization of human monoclonal antibodies directed against the hepatitis B virus surface antigen. 348 52

We have established a new human myeloma cell line from the pleural effusion of a patient with an IgA lambda myeloma, using special tissue culture conditions and selection procedures to prevent the outgrowth of contaminating Epstein-Barr virus (EBV)-carrying normal B-lymphoblastoid cells present in the explant. The myeloma cell line, U-2030, is aneuploid and EBNA-negative and has morphological features, reactivity with cytochemical markers and cell-surface antigen expression typical of plasmablasts. The cell line thus appears to be representative of the malignant clone in vivo. However, functionally the line is a non-Ig-producer and must therefore be derived from a non-secretory variant cell present within the highly aneuploid myeloma cell clone in vivo. The U-2030 differs from previously established human myeloma cell lines in that it has a comparatively high growth rate, is clonable and can be made HAT-sensitive relatively easily. This, together with the facts that it is a non-Ig-producer and mycoplasma-free, suggests that the 6-thioguanine-resistant, HAT-sensitive subline, U-2030 TG, derived from this cell line may be used as a malignant fusion partner for the production of human-human hybridomas. An EBV-carrying lymphoblastoid cell line (U-2031) was also established. This line was diploid and had all the phenotypic properties of lymphoblastoid lines established from normal individuals.
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PMID:Establishment of a new human myeloma cell line (U-2030) and selection of a hat-sensitive subline. 358 53

We have used a monoclonal antibody ESA 152 in fluorescence recovery after photobleaching (FPR) studies of a maturation-dependent surface antigen of ram sperm. The antibody is an immunoglobulin G secreted by a hybridoma derived from NS1 mouse myeloma cells. The ESA 152 antigen is not detectable in testicular sperm. It is localized on the surface of ejaculated sperm where it is present on all regions of the surface, but tends to be concentrated on the posterior region of the head. The ESA 152 antigen can be extracted by detergents or chloroform-methanol. The extracted antigen is sensitive to proteases and migrates with an apparent Mr approximately 30,000 in SDS-containing 10-20% polyacrylamide gradient gels. FPR measurements of ESA 152 lateral mobility in the membrane yield diffusion coefficients in the range 10(-9)-10(-8) cm2/s, values typical of lipids but observed for proteins only at the fluid dynamic limit where diffusion is controlled by lipid fluidity. Immobile fractions, typical of membrane proteins, are observed on all regions. When the antigen is stained by a fluoresceinated Fab fragment of the ESA 152 antibody, the diffusibility is highly regionalized, with particularly low, but rapid, recovery on the midpiece. Cross-linking of the antigen with the intact ESA 152 antibody induces a redistribution in which the antigen is excluded from the posterior head region. This cross-linking is accompanied by increases in ESA 152 diffusibility on both the anterior head and the midpiece.
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PMID:Lateral regionalization and diffusion of a maturation-dependent antigen in the ram sperm plasma membrane. 370 Apr 76

Antibodies to surface IgM and IgD were found to induce increased expression of class II antigens on normal and neoplastic human B cells within 24 h of stimulation. Antigens associated with different class II sub-locus genes (DC, DR and SB) were all found to be increased as determined by monoclonal antibodies (Leu-10 and B 3/4 for DC, D 1/12 for DR and MHM4 for SB-associated antigens). The increased expression of class II antigens was selective as anti-immunoglobulins failed to increase expression of other surface antigens such as B1 and beta 2-microglobulin. The effect of anti-mu and anti-delta could be blocked specifically by corresponding myeloma proteins suggesting that antibodies to surface IgM and IgD, respectively, were responsible for the effect observed. Moreover, antibodies to another surface antigen (B1) failed to induce such changes. Increased class II antigen expression appeared to be dependent on protein synthesis, and early changes in ion fluxes, but could not be elicited by membrane depolarization as reported in murine systems.
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PMID:Antibodies to surface IgM and IgD increase the expression of various class II antigens on human B cells. 387 99

H36 is a species-specific, cell-surface antigen on differentiating newborn rat skeletal myoblasts and myogenic lines. This membrane antigen has been defined by a monoclonal antibody raised by the fusion of SP 2/0-Ag14 myeloma cells with spleen cells from mice immunized with myotubes derived from the myogenic E63 line. H36 antigen, isolated by immunoaffinity chromatography, is comprised of two polypeptides with apparent molecular weights of 98,000 and 117,000. Fluorescence photometry and radioimmunoassays have been used to follow quantitative and topographic changes in the H36 determinant during myogenesis. H36 is present at a basal level on replicating myoblasts; it increases on prefusion myoblasts and persists on myotubes. At or near the time of prefusion, it becomes concentrated between adjacent aligned myoblasts and localized on membrane "blebs". H36 is present on both skeletal and cardiac cells but absent from a variety of cells that include fibroblasts, neuronal cells, and smooth muscle. There are approximately 4 x 10(5) determinants per myoblast, and the Ka of the antibody is 3.8 x 10(8) liters/mol. The distributions of H36 on the top and attached surfaces of myoblasts and myotubes are distinct, which suggests localized specialization of these surfaces. H36 is an integral membrane component and upon cross-linking, it associates with the detergent-insoluble cytoskeletal framework. Inhibition of myogenesis by 5-bromodeoxyuridine or by calcium deprivation prevents the developmentally associated changes in the expression of H36. H36 is also absent or markedly reduced on the fu- and Ama102 developmentally defective mutant myoblast lines. We conclude that H36 is a muscle-specific, developmentally regulated cell-surface antigen that may have a role in myoblast differentiation and that can be used to determine the embryonic lineages of skeletal and cardiac muscle.
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PMID:Expression of a developmentally regulated antigen on the surface of skeletal and cardiac muscle cells. 388 14

Monoclonal anti-actin antibody which is known to stimulate DNA synthesis and cell growth in a murine transformed cell line, L cell, was examined for its ability to modulate the expression of surface antigen on the cell membrane. There was a time dependent increase in the number of cell surface antigen molecules on L cells stimulated by monoclonal anti-actin antibody as measured by indirect immunofluorescence and flow cytometry. For L cells incubated for 12, 24, 48, 72, and 96 hours with monoclonal anti-actin antibody versus a myeloma control supernatant, the percentage of cells exhibiting high intensity immunofluorescence was 29 vs. 13, 13 vs. 10, 34 vs. 1, 52 vs. 11, and 35 vs. 18, respectively. We conclude that monoclonal anti-actin antibody modulates the time dependent surface expression of actin on L cells. It is likely that this modulated expression of surface actin-like molecules plays an important role in the transmission of stimulatory signals to the cells which result in enhanced cellular metabolism and proliferation.
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PMID:Monoclonal anti-actin antibody modulates expression of surface antigen on L cells. 392 44

Female BALB/c mice were immunized with human melanoma (Mewo) cells containing ganglioside GD3 as a surface antigen. Immune splenocytes were fused with syngeneic P3-X63.Ag 8 myeloma cells. Antibodies produced by hybrid clones were analyzed by solid phase immunoassay. B, C, D and Q clones producing antibodies against Raja clavata brain gangliosides were obtained. Monoclonal B and C antibodies bound monosialogangliosides. Monoclonal D antibody bound a number of gangliosides but reacted predominantly with GD1a. Monoclonal Q antibody reacted selectively with GQ1c. It is assumed that ganglioside GQ1c is expressed on the melanoma cell surface and may be found only in the early stage of ontogenesis of high vertebrates.
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PMID:[Isolation and analysis of monoclonal antibodies against various gangliosides]. 394 18

Unlike other hamster phagocytes, hamster pulmonary macrophages (PM) avidly ingest albumin-coated latex particles in the absence of serum. They also possess a highly specific cell surface antigen. To evaluate the relationship between these two characteristics, PM were incubated with mouse monoclonal antibody directed against the PM antigen. After unbound antibody was removed, the amount of bound antibody and the phagocytic capability of PM were measured by flow cytometry and fluorescence microscopy. Maximum antibody binding produced a 25% inhibition of ingestion. Particle attachment was not affected. This effect was antigen specific, since neither a nonspecific mouse myeloma protein of the same subclass nor a mouse antibody that bound to another hamster surface antigen had any effect on binding or ingestion. If antigen-specific F(ab')2 fragments were introduced both before and during the period of phagocytosis, the inhibition of particle ingestion approached 100%. Particle binding increased at low F(ab')2 concentrations but declined at higher concentrations. Because calcium may play a role in the ingestion process, the effect of antibody on 45Ca uptake was evaluated. It was observed that antigen-specific F(ab')2 fragments stimulated 45Ca uptake, whereas control antibodies did not. These results suggest that the antigen reacting with our anti-hamster PM monoclonal antibody is involved in immune opsonin-independent phagocytosis and that calcium participates in this phagocytic process.
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PMID:Inhibition of immune opsonin-independent phagocytosis by antibody to a pulmonary macrophage cell surface antigen. 395 Apr 9

During long-term tissue culture of spontaneously transformed clones from BALB/c 3T3 mouse-embryo cells, some clones spontaneously begin to produce high titers of endogenous murine type-C viruses. The antigenic properties of these viruses have been analyzed by indirect immunoelectronmicroscopy and can be classified into two distinguishable populations: (a) BALB/c murine myeloma-associated extracellular viruses that carry a specific envelope antigen, xVEA, different from the typical murine leukemia viral envelope antigens; and (b) previously uncharacterized type-C viruses that have neither xVEA nor the murine leukemia viral envelope antigens. The former produces PC1 antigen and the latter might induce a new cell-surface antigen. Neither of these two populations of BALB/3T3 endogenous type-C viruses was able to infect BALB/c cells but both could infect NIH Swiss cells. A single BALB/3T3 clone, then, can release infectious endogenous type-C viruses with at least two different antigenic properties. We conclude that BALB/c somatic cells contain preexisting genetic information for production of at least closely related but, nevertheless, distinct type-C viruses.
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PMID:Antigenic properties of endogenous type-C viruses from spontaneously transformed clones of BALB-3T3. 435 Nov 84


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