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)

A hybridoma-derived monoclonal antibody, produced by immunization with the Burkitt's tumor-derived B-lymphoblastoid cell line, B35M, was previously shown to detect a 68,000 dalton surface membrane protein, BL2, on the surface of peripheral blood B cells, which is absent from thymocytes, T cells, and granulocytes. In this study, we investigated the expression and distribution of BL2 on benign and malignant human lymphoid cells. Indirect immunofluorescent assay with this monoclonal antibody demonstrated that BL2 is expressed by cells within the fetal liver and by a variable proportion of lymph node, tonsil, and spleen B cells, but not by T cells. The neoplastic cells isolated from 18 T-cell malignancies were BL2- . BL2 was was heterogeneously expressed by a variable proportion of the malignant cells in 29/32 cases of B-chronic lymphocytic leukemia and 33/38 cases of B-cell lymphomas, but appeared to be lost in the terminal stages of B-cell differentiation, as myeloma plasma cells were BL2- . BL2 expression was not limited to B cells of a particular surface immunoglobulin isotype. Immunofluorescent staining for BL2 in cryostat tissue sections demonstrated that the majority, but not all, germinal center and interfollicular Ia+ (non-T) cells are BL2+. These findings suggest that BL2 is a B-cell lineage-specific differentiation marker that may be useful in the study of B-cell ontogeny and in defining subgroups of the B-cell malignancies.
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PMID:A new human B-lymphocyte surface antigen (BL 2) detectable by a hybridoma monoclonal antibody: distribution on benign and malignant lymphoid cells. 619 May 20

Four mouse monoclonal antibodies directed against the red cell membrane protein glycophorin A have been isolated and characterized. They are produced by hybridomas derived from SP2/0 myeloma cells and spleen cells from Biozzi mice immunized with a mixture of human erythrocytes from homozygous blood group M and N individuals. These antibodies recognize and bind to purified glycophorin A and to glycophorin on the red cell surface. All are of the IgGl, kappa light chain subclass and bind to determinants presented on the 39 amino acid, trypsin-sensitive, N-terminal peptide of glycophorin A. Three display differential specificities for the two allelic forms of glycophorin A; two are exquisitely specific for the M-form and one preferentially binds the N-form. Treatment of red cells with neuraminidase, which removes N-acetylneuraminic acid from glycophorin A, abolishes the binding of these three antibodies. The binding of the N-specific antibody is also sensitive to modification of the amino-terminal residue of the antigen. The fourth antibody binds equally well to both the M- and N-forms as well as to neuraminidase-treated red cells; thus it recognizes a public, N-acetylneuraminic acid independent glycophorin A determinant.
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PMID:Monoclonal antibodies specific for the M- and N-forms of human glycophorin A. 619 36

We used the hybridoma technique to characterize further the platelet glycoprotein abnormality in Glanzmann's thrombasthenia. Spleen cells from Balb/c mice immunized with human platelets were fused to mouse myeloma cell line Sp2/0-Ag14. Hybridoma lines producing a variety of antiplatelet antibodies were isolated by hypoxanthine-aminopterin-thymidine selection and cloned, and purified monoclonal IgG from six lines was prepared. One of these lines, 8aB5-9, produced an antibody, Tab, that binds to a protein on normal but not thrombasthenic platelets. We isolated this protein from Triton X-100 solubilized normal platelet membranes by affinity chromatography on Tab-Sepharose. As determined by SDS polyacrylamide gel electrophoresis, the isolated protein is a complex of glycoproteins IIb and IIIa, because the two subunits comigrate with glycoproteins IIb and IIIa of whole platelets and show identical changes in mobility after disulfide bond reduction. We prepared (125)I-Tab to determine the number of glycoprotein IIb-IIIa complexes on normal and thrombasthenic platelets by a direct binding assay. Platelets from 17 normal donors bound 39,000+/-4,600 (SD) Tab molecules/platelet. Platelets from four patients with thrombasthenia lacked Tab binding sites (<5%). Five obligate and four presumed heterozygotes for thrombasthenia bound 24,500+/-5,800 Tab molecules/platelet. The platelet alloantigen, Pl(Al), is not that recognized by Tab, because platelets from three Pl(Al)-negative subjects bound Tab normally. Studies with the Tab antibody have (a) enabled quantitation of the number of glycoprotein IIb-IIIa complexes on normal platelet membranes, (b) demonstrated that thrombasthenic homozygotes lack and heterozygotes have a partial deficiency of this complex, and (c) made possible the isolation of this membrane protein which may be required for normal platelet aggregation and clot retraction.
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PMID:Isolation and quantitation of the platelet membrane glycoprotein deficient in thrombasthenia using a monoclonal hybridoma antibody. 644 21

The nicotinic acetylcholine (ACh) receptor probe alpha-bungarotoxin (alpha-Butx) binds with high affinity to a membrane protein of the vertebrate central nervous system. To characterize further this putative neuronal ACh receptor, we have prepared monoclonal antibodies (mAbs) against the alpha-Butx-binding protein of chick optic lobe. Mice were immunized with affinity-purified protein preparations which were estimated to be 10 to 20% pure. Spleen cells from an immunized mouse were fused with the mouse myeloma cell line X63-Ag 8.653. From this fusion, 14 stable hybridoma lines were isolated which produce mAbs against the chick neuronal alpha-Butx-binding protein. Most of the antibodies inhibited alpha-Butx-binding to membrane fractions and/or detergent extracts of chick optic lobe. Some of the mAbs cross-reacted with the alpha-Butx-binding protein of the rat pheochromocytoma cell line PC12. However, none of the mAbs bound to a significant extent to the nicotinic ACh receptor of chick skeletal muscle or of Torpedo californica electric organ. All antibodies specifically isolated a polypeptide of Mr = 57,000 (+/- 2,000) from radiolabeled neuronal protein preparations. The present data show that these mAbs constitute useful tools for the further molecular and functional characterization of the neuronal alpha-Butx-binding protein.
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PMID:Monoclonal antibodies against the alpha-bungarotoxin-binding protein of chick optic lobe. 647 Jul 69

Stable somatic cell hybrids were obtained by fusing Xenopus lymphocytes with mouse myeloma cells. These hybrids contained one to four Xenopus chromosomes and expressed Xenopus gene products, one of which was a lymphocyte membrane protein of 85,000 daltons precipitated by a monoclonal antibody.
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PMID:Somatic cell hybrids from frog lymphocytes and mouse myeloma cells. 678 84

Nineteen independent hybrid cell lines that produce monoclonal antibodies to Chlamydia trachomatis surface antigens were prepared by the fusion of mouse myeloma cells with lymphocytes of mice that were immunized with C. trachomatis immunotypes B, C, and L2. Seven serologically distinct reaction patterns were detected by microimmunofluorescence (micro-IF) of elementary body (EB) preparations when culture fluids were tested against a panel of 18 chlamydial serotyping reference strains. These reaction patterns demonstrated genus-, species-, subspecies-, and type-specific distributions. Additionally, these antibodies were tested in parallel against reticulate body (RB) preparations of several chlamydial strains. Monoclonal antibodies that reacted with genus-specific antigens reacted preferentially with RB, whereas antibodies that reacted to species-, subspecies-, or type-specific antigens reacted equivalently to both RB and EB. Physiochemical characterization of antigens recognized by the different monoclonal antibodies was assessed by heat treatment, pronase digestion, periodate oxidation, and immuno-blot techniques. The genus-specific antigen was a heat-stable, pronase-resistant, and relatively periodate-sensitive component of less than 10,000 m.w. The species-, subspecies-, and type-specific antigens were heat stable, pronase sensitive, and periodate resistant. The antibodies that detected species- and subspecies-specific antigens predominantly reacted in immuno-blots with the 40,000 m.w. major outer membrane protein. These monoclonal antibodies now provide a new approach for the precise serologic classification and detection of different C. trachomatis strains.
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PMID:Monoclonal antibodies to Chlamydia trachomatis: antibody specificities and antigen characterization. 703 57

Rat liver microsomal membranes were purified in order to remove membrane-associated secretory products. Measurements of the decay of the newly synthesized protein of these membranes in vivo were carried out at short time intervals after the protein was labeled by the administration of radioactive leucine. The result of these measurements suggest that the membranes are synthesized and degraded at approximately the same rapid rate as the synthesis and secretion of membrane-associated secretory products. Evidence that the highly dynamic protein of the purified membranes is indeed membrane protein is provided by the observations indicating: that this protein is immunochemically distinct from serum proteins, which are the major secretory product of liver; that many different protein components of the membranes turn over at similarly rapid rates; and that the biosynthesis of these proteins is specifically stimulated by the administration of phenobarbital, which is known to stimulate biosynthesis of hepatic endoplasmic reticulum. These findings suggest that in liver, as had been proposed earlier for the myeloma cell, unidirectional membrane flow, accompanied by rapid synthesis at the origin of flow and rapid degradation of the membranes at or near the terminus of flow, may be the mechanism for the intracellular transport of secretory product.
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PMID:Evidence for rapid turnover of hepatic endoplasmic reticulum and its possible relationship to secretion. 720 94

A panel of monoclonal antibodies was developed for serovar typing of clinical isolates of Chlamydia trachomatis. The panel could distinguish all 15 established serovars from one another, although the hybridomas of the panel were developed by fusions of myeloma cells and spleen cells from mice immunized with antigen derived from the urogenital serovars D to L3. The typing assay was based on a dot enzyme immunoassay, and the monoclonal antibodies that were included in the panel reacted strongly in this assay. A collection of 289 clinical isolates from The Netherlands was typed. The observed serovar frequency distribution was 51 isolates of serovar D (17.6%), 103 isolates of serovar E (35.6%), 62 isolates of serovar F (21.5%), 28 isolates of serovar G (9.9%), 14 isolates of serovar H (4.8%), 2 isolates of serovar I' (0.7%), 20 isolates of serovar J (6.9%), and 9 isolates of serovar K (3.1%). These results were confirmed by typing these isolates with a panel of monoclonal antibodies purchased from the Washington Research Foundation, Seattle. No strain variation was observed within serovar D with both panels. However, restriction fragment length polymorphism analysis of the gene encoding the major outer membrane protein showed that 32 isolates were similar to the prototype D and 17 were similar to the variant D-. The two others showed a new restriction pattern. Our panel of monoclonal antibodies contained one monoclonal antibody that divided the serovar G isolates into two groups. This differentiation was confirmed by restriction fragment length polymorphism analysis, confining this difference to a known sequence variation in variable domain IV. These data support the subdivision of serovar G into serovars G (prototype strain UW-57) and Ga (prototype strain IOL-238).
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PMID:Comparison of two panels of monoclonal antibodies for determination of Chlamydia trachomatis serovars. 788 84

The purified elementary bodies (EBs) of C. pneumoniae ATCC VR1310 were used for primary immunization of male BALB/c mice (8 weeks of age), with the boost following on day 14. Spleen cells were fused with murine myeloma NS-1 cells on day 24 and hybrid cells were cloned by limiting dilution. Two clones, P17C2 & P33C, secreting species-specific monoclonal antibodies (MAbs) and immunoglobulin IgG2a class were obtained after elimination of those clones that produced antibodies against C. trachomatis L1, L2, A, B, C, E serovars, C. psittaci EAE strain and uninfected BGMK cell antigens. It was showed that the two clones of MAbs reacted with the MOMP 39.5 x 10(3) Da major outer membrane protein of all chlamydia species in Western blot and their ascites titers were more than 1:25 600 in Micro-IF test.
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PMID:[Species-specific monoclonal antibodies against Chlamydia pneumoniae]. 798 14

Freshly isolated human peripheral blood mononuclear cells (PBMC) were immunomagnetically depleted of CD56+ cells. When these CD56- PBMC populations were cultured in the presence of autologous donor serum, polyclonal activation with IL-2 and pokeweed mitogen (PWM) generally resulted in exclusive production of IgG antibodies. Fusion with SP2/O-Ag14 mouse myeloma cells was highly efficient and yielded a great number of IgG-producing heterohybridomas. These conditions were used for in vitro immunization with viable human HT29 tumor cells. After fusion, an increase in hybridoma clones producing IgG monoclonal antibodies (MAb) with HT29 specificity showing a higher portion of MAb binding to the surface of viable HT29 cells was recorded. This immunizing efficiency was not observed with HT29 membrane protein fractions or HT29 proteins integrated into ISCOM particles. Investigations with human anti-alpha Gal antibodies showed that the IgG antibodies produced by the human/mouse heterohybridomas did not contain the mouse-specific Gal alpha 1-3Gal epitope.
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PMID:Optimizing production of human monoclonal IgG antibodies by in vitro-primed human PBMC: influence of CD56+ NK cell depletion. 852 52


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