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 monoclonal antibodies, M3/31 and M3/38, were obtained by fusion of mouse myeloma cells with rat spleen cells immunized to immunoadsorbent-purified macrophage glycoproteins. Co-precipitation experiments show that antigenic determinants recognized by these two antibodies reside on the same molecular species, termed Mac-2, Mac-2, an antigen of 32,000 Mr, is synthesized by and expressed on the surface of thioglycollate-elicited macrophages as shown by [35S]-methionine and 125I labeling. Saturation binding experiments show that thioglycollate-elicited macrophages express 1.7 X 10(5) Mac-2 sites/cell. Thioglycollate-elicited macrophages are strongly absorptive for 125I-labeled M3/38 MAb. Kidneys are also absorptive; however, evidence is presented pointing to the nonspecificity of this absorption. Lymph node and thymus are negative, whereas spleen and bone marrow are weakly absorptive, probably due to stromal cells. Nonlymphoid tissues, such as lung, liver, heart, and brain, exhibit slight or no absorbing capacity. Cell suspensions from spleen, bone marrow, thymus, and peripheral lymph node are greater than 99% Mac-2- by immunofluorescent flow cytometry. In contrast, thioglycollate-elicited macrophages are greater than 96% strongly positive for Mac-2. Only 20% of peptone-elicited cells are weakly positive, whereas resident peritoneal macrophages and other macrophage elicited by Listeria monocytogenes, Con A, or LPS are greater than 98% negative. SDS-PAGE of [35S]-methionine-labeled Mac-2 shows that thioglycollate-elicited macrophages synthesize 10- to 30-fold more Mac-2 than other peritoneal macrophage subpopulations, whereas all types of peritoneal macrophages synthesize and express on their surfaces similar amounts of the Mac-1 antigen. Mac-2 antigen is therefore induced in macrophages only in response to specific differentiative signals.
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PMID:Mac-2, a novel 32,000 Mr mouse macrophage subpopulation-specific antigen defined by monoclonal antibodies. 617 26

The BALB/c mouse strain represents an excellent model for studying the activation of V genes, because several myeloma proteins share the cross-reactive idiotype with antipolysaccharide antibodies of the same antigenic specificity. In addition, the majority of these antipolysaccharide antibody responses are independent of T help and, therefore, the maturation of helper T cells does not play a role in the study of these responses. Our results, as well as those obtained by other investigators, have shown that immunization of 1-day-old mice elicits an anti-beta 2 leads to 6 fructosan, 384Id anti-S tranaroa LPS, and X24IdX and X24IdI antigalactan response. T15Id+ phosphocholine, IdX+ anti-Ars, and 460Id+ anti-TNP (in response to immunization with TNP-LPS and TNP-Levan) antibody responses can be induced only in 6-to 8-day-old mice. One can obtain 2.4 SSSIII Id+ of anti-SSSIII and 347Id+ antiflagellin antibody responses only in 2-week-old mice. In 4-week-old mice IdX+ anti-beta 2 leads to 1 fructosan was elicited, and QPC52IdX+ anti-alpha 1-6 dextran in 3-month-old mice. These observations suggest a sequential activation of V genes during postnatal life. The theoretical and practical implications of these observations are discussed.
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PMID:Sequential activation in V genes during postnatal life. 617 32

Several idiotypic (Id) specificities have been identified by immunofluorescence on the membranes of B cells in the spleens of nonimmune mice. These determinants are displayed at frequencies varying from 0.22 to 1.83% of B cells and are entirely immunoglobulin (Ig) in nature. No Id determinants were observed on the membranes of four Slg- Abelson virus-transformed pre-B cell lines that are sensitive to LPS. Under our experimental conditions, we did not observe a significant increase in 3H-thymidine incorporation subsequent to the in vitro incubation of splenic lymphocytes from normal mice with various amounts of anti-Id antibodies specific for several cross-reactive (IdX) or individual Id. Similarly, in utero exposure to anti-Id antibodies against myeloma proteins specific for T-independent antigens displaying B cell mitogenic properties did not alter the proliferation of lymphocytes induced by these mitogens. In contrast, exposure to anti-Id antibodies in vitro as well as in utero had a profound and specific effect on the corresponding antibody responses and maturation of small lymphocytes into plasma cells. When normal B cells were cultured with the B cell mitogen LPS in the presence of anti-Id antibodies directed against the J558IdX, specific suppression of the maturation of IdX+ plasma cells was observed. In mice exposed to maternal anti-Id in utero, we observed a severe inability to mount an immune response to any compound that elicited antibody molecules bearing the Id that was complementary to the maternal anti-Id. These same maternally Id-suppressed mice, however, gave a normal response when the same compound was presented as a mitogen. Our results reinforce the concept that Id on membranes of B lymphocytes are associated only with Ig receptors and do not support the possibility of mitogen-like poly-clonal stimulatory properties of anti-Id antibodies.
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PMID:Idiotypes on B lymphocytes: association with immunoglobulins. 618 21

Immunization of B10.D2 Ign mice against a (BALB/c X NZB)F1 murine B lymphoma cell line (WEHI-5) and subsequent fusion of immune spleen cells with a drug sensitive myeloma (P3 X 63-Ag8) has resulted in the generation of a series of hybridoma cell lines. One of these clones, BD5-334.5, secretes an antibody which reacts with a determinant, designated Lym 7.2, which demonstrates an identical tissue and strain distribution as the conventionally defined Ly 7.2 antigen. Furthermore, anti-Ly 7.2 alloantiserum significantly blocks reaction of the anti-Lym 7.2 monoclonal antibody with BALB/c splenocytes. Lym 7.2 is present on a majority of splenocytes, peripheral blood leukocytes, and lymph node cells. However, B cells express considerably higher cell surface density of this antigen than peripheral T lymphocytes. This antigen was not detected on erythrocytes, kidney, liver, or brain. Moreover, Lym 7.2 is present on approximately 15% of normal thymocytes, and 15% of bone marrow cells, and is expressed on cortisone resistant thymocytes. Quantitative flow cytometry analysis demonstrated that the antigen is present at approximately half the cell surface density on spleen cells from F1 mice between Lym 7.2 positive and Lym 7.2 negative mice, but on the same percentage of cells as Lym 7.2 positive inbred strains. Data from backcross analysis suggest that a single locus is encoding this antigen. Mitogen blasts, induced with PHA, ConA, and LPS, all express the Lym 7.2 marker.
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PMID:Lym 7.2: monoclonal antibody defining an alloantigen similar or identical to Ly 7.2. 620 26

Monoclonal antibodies were prepared by the fusion of murine myeloma NS1 cells with spleen cells of BALB/c mice immunized with Formalin-killed elementary bodies of the Chlamydia trachomatis L2 serovar. The specificity of these monoclonal antibodies was determined with a solid-phase immunoassay in which HeLa 229 cells infected with C. trachomatis serovars D, G, H, I, L2 and the Chlamydia psittaci meningopneumonitis strain Cal-10 were used. An immunoglobulin G3 monoclonal antibody (L2I-6) was identified that reacted with both C. trachomatis- and C. psittaci-infected HeLa cells. The immunoreactivity of the genus-specific epitope was heat resistant (100 degrees C, 10 min) but was destroyed by sodium metaperiodate treatment. Further characterization of the chlamydial specificity of monoclonal antibody L2I-6 by microimmunofluorescence showed that it was reactive with all 15 C. trachomatis serovars and seven C. psittaci strains isolated from five different animal species. We undertook studies to identify the biochemical nature of the chlamydial component on which the genus-specific epitope was located. The immunoreactive component was isolated by hot phenol-water extraction of dithiothreitol-reduced chlamydial elementary bodies. The component was positive in the Limulus amoebocyte lysate test (results of Limulus amoebocyte lysate assay were identical with those of Salmonella typhimurium LT2 SAI 377 Re lipopolysaccharide [LPS]), contained 8.8% 2-keto-3-deoxyoctulosonic acid, was resistant to proteinase K, and possessed electrophoretic mobility and silver-staining characteristics in sodium dodecyl sulfate-polyacrylamide gel electrophoresis consistent with a rough LPS or glycolipid. On the basis of these findings, we conclude that the genus-specific epitope recognized by monoclonal L2I-6 is located on chlamydial LPS. We further characterized the antigenic properties of the chlamydial LPS epitope by examining the immunoreactivity of monoclonal antibody L2I-6 by immunoblotting analyses against isolated LPSs extracted from Neisseria gonorrhoeae, S. typhimurium, and Escherichia coli. Monoclonal antibody L2I-6 did not bind LPS of these organisms, demonstrating that the chlamydial genus-specific LPS epitope is apparently not shared by these gram-negative bacteria. We were able, however, to show that the chlamydial LPS does share antigenic determinants with LPS of gram-negative organisms. Polyclonal rabbit antisera raised against S. typhimurium Re LPS or lipid A showed intense immunological cross-reactivity with chlamydial LPS by immunoblotting.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:Monoclonal antibody against a genus-specific antigen of Chlamydia species: location of the epitope on chlamydial lipopolysaccharide. 642 19

Detergent-solubilized plasma membranes of Con A-activated mouse spleen cells were absorbed with Sepharose-coupled rat antibodies against resting mouse lymphocytes. The unbound fraction was used to immunize a rat, and the immune spleen cells were fused with the rat myeloma Y3 . All seven rat monoclonal antibodies produced in this way strongly reacted with mitogen-activated spleen cells but only weakly or insignificantly with unstimulated spleen cells. One of the antibodies, YE3 /19.1, was studied in detail. The antibody strongly reacted with Con A- or LPS-stimulated spleen cells, but not significantly with normal adult thymocytes, spleen cells, or bone marrow cells. Unlike the transferrin receptor, which is expressed on virtually all dividing cells, the antigen defined by YE3 /19.1 was not detected on erythroblast-enriched populations or some non-T, non-B cell lines. Therefore, the antigen, termed MALA-1, seems to be specific for activated murine lymphocytes of the T and B cell lineages. Over 25% of normal adult lymph node cells were also found to express the antigen, although the antigen densities on lymph node cells were lower than those on mitogen-stimulated spleen cells. Kinetic studies of the expression of MALA-1 and the transferrin receptor on Con A-activated spleen T cells showed that both antigens are detectable within 24 hr of Con A stimulation. Although the density of the transferrin receptor on Con A blasts declined as the cell proliferation ceased, MALA-1 expression persisted. Immunoprecipitation of MALA-1 from surface-iodinated Con A blasts revealed its m.w. to be approximately 14,000 to 18,000.
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PMID:MALA-1: a surface antigen expressed on activated murine T and B lymphocytes. 660 86

Monoclonal antibodies to murine lymphocyte differentiation antigens were generated by fusing the mouse myeloma cell line X63-Ag8.653 with spleen cells derived from Lewis rats hyperimmunized with lymphoid cells from nude (C57BL/6) mice. One of these antibodies--designated 3MB1--recognizes a previously undescribed cell surface antigen. This antigen is expressed on 62% of spleen cells, 9% of thymus cells, and 98% of peritoneal macrophages. Virtually all LPS- and Con A-induced lymphoblasts carry this newly found antigen. The 3MB1 determinant is limited in its expression to leukocytes. It is not found in other tissues such as brain, liver, kidney, or on erythrocytes. Biochemical analysis reveals that the 3MB1 target antigen consists of a single chain glycoprotein with an approximate m.w. of 90,000.
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PMID:A new murine cell surface differentiation antigen (Leugp90) defined by a rat monoclonal antibody: cellular distribution and biochemical characterization. 697 11

Amphotericin B at the concentration normally used for routine suppression of fungal infection in tissue culture strongly inhibits the proliferation of NS1/1 myeloma cells and the LPS-induced activation of B lymphocytes from mouse spleen. The proliferation of T lymphocytes induced by concanavalin A (Con A) was less affected by the antibiotic, indicating that B-lymphocyte proliferation was preferentially inhibited. The unexpected sensitivity of B-lymphoid cells to amphotericin B precludes its use as an anti-fungal agent in the production of hybridomas from fusions between these cells.
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PMID:Inhibition of proliferation of a murine myeloma cell line and mitogen-stimulated B lymphocytes by the antibiotic amphotericin B (Fungizone). 698 85

Somatic cell hybrids were prepared between the TK-deficient variant of murine pre-B cell line, 70Z/3, cells and the HGPRT-deficient variant of non-secreting myeloma cells. Several hybrid clones which secreted IgM but did not express surface IgM were isolated. LPS stimulation did not induce the expression of surface IgM. SDS-PAGE analysis indicated that the IgM secreted by one of the hybrid clones was a 19S pentamer and that the size of its mu-chains was the same as that of mu-chains from MOPC 104E myeloma IgM. Two-dimensional gel electrophoresis of biosynthetically labeled immunoglobulin showed that the same pattern was obtained with kappa-chains from two hybrid clones and from the LPS-induced 70Z/3 cells. The result showed that cell hybridization could induce L-chain synthesis in the pre-B cell line. Anti-idiotypic antibody against the secreted IgM was prepared and it was shown that the surface IgM expressed on all LPS-stimulated 70Z/3 cells bore the same idiotype. Those results indicated that the specificity commitment has already occurred in 70Z/3 cells.
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PMID:Induction of 19S IgM secretion in a murine pre-B cell line, 70Z/3, by cell hybridization with non-secreting myeloma cells. 698 54

Using an anti-idiotypic antibody previously characterized as specific for the hapten binding site of the 2,4-dinitrophenyl (DNP)-binding BALB/c myeloma protein MOPC-460, we have detected substantial amounts of this idiotype (Id-460) in the serum of normal mice. Whereas the idiotypic material in DNP-immune serum binds to DNP, the Id-460-positive material in normal mouse serum is not specific for DNP. The material in normal serum appears to be immunoglobulin. Furthermore, Id-460-positive, non-DNP-binding monoclonal immunoglobulins that completely inhibit our assay for Id-460 are repeatedly isolated when hybridomas are prepared from LPS-activated normal spleen cells. These data are interpreted in the context of Jerne's network hypothesis. It is our conclusion that the non-DNP-binding form of Id-460 is the inherited form and that this form establishes an idiotypic network favoring the production of anti-DNP bearing Id-460. Thus, the paradox of finding an inherited idiotype in the antibody response to the nonpathogen DNP may be resolved by proposing that the true form of Id-460 is specific for an environmental pathogen and that Id-460 dominance in the anti-DNP response is simply a consequence of idiotype-specific regulatory events preconditioned by Id-460-bearing immunoglobulin specific for antigenic determinants unrelated to DNP.
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PMID:Expression of an idiotype (Id-460) during in vivo anti-dinitrophenyl antibody responses. III. Detection of Id-460 in normal serum that does not bind dinitrophenyl. 729 44


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