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)

Fusion of spleen cells from autoimmune NZB/NZW female mice with drug-resistant myeloma cells (clones NSI/1, X63-Ag8.653 and NSO/1) produced hybrid clones which secreted antibodies to various nuclear components. Roughly 50% of the anti-nuclear hybridomas produced antibodies reacting with DNA, 20% with RNA and 30% reacted with other nuclear antigens. Two hybridomas of the latter group were cloned and studied in detail. They secreted antibodies which produced bright fluorescence staining of nuclei and metaphase chromosomes. The specificity of the antibodies was determined by testing them in an enzyme-linked immunosorbent assay and a radioimmunoassay against individual acid- and salt-extracted histones, against histones mixed two and three at a time and against histone complexes isolated as such from chromatin. One of the monoclonal antibodies was specific for histone H2B and reacted with the histone free in solution or when present as a H2A-H2B complex. The second monoclonal antibody recognized a specific conformation in the H3-H4 complex that was present only when the complex was obtained from chromatin by salt extraction. The same conformation, however, could be induced by adding histone H2B to a mixture of acid-extracted H3 and H4. Our findings show that the autoimmune syndrome in NZB/NZW mice resembles human systemic lupus erythematosus not only in the incidence of antibodies to DNA and RNA, but also in the production of autoantibodies to histones.
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PMID:Monoclonal autoantibodies to histones from autoimmune NZB/NZW F1 mice. 619 84

Two monoclonal antibodies against the B subunit (Mr 108 000) of chick oviduct progesterone receptor (PgR) were produced by immunizing rats and fusing spleen cells with NS-1 mouse myeloma cells. The hybridoma lines designated 9G10 and 3E8 produce rat IgG2a and IgG2b, respectively. Antibody-receptor interactions were demonstrated under protein denaturing conditions. Previous studies by Weigel et al. [Weigel, N. L., Tash, J. S., Means, A. R., Schrader, W. T., & O'Malley, B. W. (1981) Biochem. Biophys. Res. Commun. 102, 513-519] have shown that chick PgR can be phosphorylated in vitro. Both antibodies, 9G10 and 3E8, were shown to displace partially denatured 32P-labeled PgR from its characteristic 4S position on high salt sucrose density gradients to a form with a higher sedimentation coefficient. Further specificity and sensitivity were demonstrated by protein immunoblotting experiments. In partially purified as well as electrophoretically pure receptor B subunit preparations antibodies reacted with the Mr 108 000 receptor B band. By immunoblot assay 9G10 was 20-fold more sensitive than 3E8, the former detecting down to 5 ng of receptor and the latter 100 ng. Because of its sensitivity 9G10 was able to detect the Mr 108 000 receptor as a single band in a crude oviduct fraction and did not cross-react with any other contaminating proteins. Receptor antigenic determinants were localized by immunoblot assay of receptor proteolytic digests.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Structural analysis of chicken oviduct progesterone receptor using monoclonal antibodies to the subunit B protein. 620 57

Cryostat sections of human central nervous system (CNS) tissue absorbed sheep erythrocytes (E) sensitized with rabbit IgG antibody (A). The indicator cells bound to the choroid plexus, to the leptomeninges covering the brain and spinal cord, to the arachnoid granulations and to the perivascular tissue of the neural parenchyma. Unsensitized E or E sensitized with F(ab')2 fragments of IgG were not bound. The reactions were inhibited by pooled human IgG, human IgG1 and IgG3 myeloma proteins, and Fc fragments of pooled human IgG. Whole human IgG2 myeloma protein, IgM, IgA, F(ab')2 fragments of pooled human IgG and albumin did not inhibit. Experiments with reduced and alkylated IgG, EDTA, iodoacetamide, 2-mercaptoethanol, various pHs and salt concentrations, formaldehyde, periodic acid and neuraminidase did not reveal any differences between the Fc gamma receptors in the separate anatomical areas. The Fc gamma receptors in human CNS are thus apparently very similar.
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PMID:Properties of Fc gamma receptors in the human central nervous system. 628

Monoclonal antibodies (mAB) were raised to be used as probes to identify cytoplasmic components associated with intermediate filaments (IF). Four hybridomas (B27, B76, B78, and B100) secreting mAB were generated by fusing mouse myeloma cells with the spleen cells of mice immunized intraperitoneally with Triton-high salt insoluble materials from BHK-21 cells. This insoluble material consists mostly of IF, a small number of microfilaments, and some polyribosomes. Biochemical studies show that the Triton-insoluble materials contain many proteins, including vimentin (decamin) and desmin. Immunofluorescence microscopy of BHK-21 cells stained with the four mAB showed that these mAB decorate the IF in a dotted pattern. Double staining with polyclonal antibody to vimentin confirmed the reactivity of the mAB with the IF. These mAB also stained the vimentin-containing filament system in a variety of other cells including epithelial cells (PTK1 and HeLa) and cells of astroglial origin. Histological studies showed that mAB-B100 stained many types of tissue including epidermis, smooth muscle, and subdermis pericytes, but not the white matter nor the gray matter of the cerebellum and spinal cord. Immunoelectron microscopy with colloidal gold has shown that the mAB-B100 decorated the IF in clusters or aggregates around proteinaceous materials associated with the filaments. Results of immunoprecipitation indicate that mAB-B100 reacted with a protein of 50,000 daltons. These findings suggest that the mAB-B100 we have developed recognizes one of the many components of what appears to be an integrated cytoskeletal structure connected with intermediate filaments.
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PMID:An intermediate filament-associated protein, p50, recognized by monoclonal antibodies. 635 21

BALB/c mice were repeatedly immunized with a galactosyl transferase-rich microsomal fraction of rat myeloma cells. Spleen cells were subsequently fused with Sp2/0 mouse myeloma cells, the resulting hybridomas were cloned, and their secreted Ig was screened for reactivity with antigens belonging to the Golgi complex. One such monoclonal antibody, 6F4C5, gave especially intense immunofluorescent staining of the Golgi area of myeloma cells and fibroblasts. It recognized two proteins bands on immunoblots of gel-fractionated cell lysates: a major one with an estimated Mr of 54,000 and a minor one at 86,000. Both proteins were concentrated in microsomal fractions isolated at low ionic strength. They were hydrophilic judging from partitioning of a Triton X-114 cell lysate. Both were cytoplasmically oriented as demonstrated by protease and high KCl treatments of postmitochondrial supernatants and microsomal fractions. Neither was retained by columns of insolubilized wheat germ agglutinin or concanavalin A, which suggests that they are not glycoproteins. Their more detailed location in the Golgi complex was studied by immunoelectron microscopy, using a saponin permeabilization procedure and peroxidase-conjugated reagents. The observed staining was restricted to two or three cisternae in the medial part of the stack. Nevertheless, differential centrifugation experiments indicated that the two antigens may be recovered in distinct subcellular fractions: this may be related to the unexpected observation that rather low salt concentrations strip the antigens from microsomal fraction.
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PMID:Characterization of cytoplasmically oriented Golgi proteins with a monoclonal antibody. 643 14

Fusion of human myeloma cell line GM 4672 and tonsillar lymphoid cells from a normal donor resulted in 13 primary hybridomas, which produced IgM anti-single-stranded DNA (ssDNA) antibodies, as determined in enzyme-linked immunosorbent assay. Nine of these primary hybridomas have been cloned and a total of 34 clones were obtained. Supernatants of these cloned hybridomas were tested for binding to ssDNA, native DNA, RNA, low molecular weight supernatant DNA, polydeoxyguanylate-polydeoxycitidylate, polydeoxyadenylate-thymidylate sodium salt, and cardiolipin. Supernatants from all clones but one showed polyspecificity when reacting with the antigens tested. That the clones were true hybridomas rather than transformed lymphoid cells was evidence by IgM anti-DNA antibody secretion, karyotype analysis, and HLA typing. These studies imply that immunoglobulin genes encoding for anti-DNA autoantibodies with a spectrum of nucleic acid specificities similar to systemic lupus erythematosus, exist among normal B lymphocytes.
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PMID:Anti-DNA autoantibody-producing hybridomas of normal human lymphoid cell origin. 647 Jan 43

A mouse was immunized with purified rabbit uterine cytosolic progesterone receptor (specific activity: 3 nmol of steroid bound per mg of protein). After fusion of its spleen cells with Sp2-OAg myeloma cells, supernatants of 11 hybrid cultures were found to react in both an immunoenzymatic test and a double-immunoprecipitation test with the progesterone receptor. Clones were obtained from the five hybrid cells that gave the strongest response in both tests. Antibodies from cell culture supernatants and ascitic fluids were characterized. Three are of the IgG1 and two of the IgG2a isotype. Their apparent affinity for the progesterone receptor was measured by immunoprecipitation in physiological salt conditions. The equilibrium dissociation constants were between 0.1 and 4 nM. All five monoclonal antibodies crossreacted with the rabbit nuclear receptor, the human cytosolic receptor, and other mammalian (rat, guinea pig) but not avian (chicken) cytosolic progesterone receptors. There was no interaction with the glucocorticoid receptor and corticosteroid binding globulin.
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PMID:Monoclonal antibodies to rabbit progesterone receptor: crossreaction with other mammalian progesterone receptors. 657 31

In order to improve the yield of hybridomas for monoclonal antibody production, 8 different sources and molecular weights of polyethylene glycol (PEG) were compared as fusing agents. Sp2/0 myeloma cells were fused with murine splenic lymphocytes immunized with sheep red blood cells. The Kodak 1450 PEG produced the maximum number of hybridomas. The optimal technique consisted of slowly adding 1 ml of freshly prepared fusogen (5 g Kodak 1450 PEG, 0.5 ml dimethylsulfoxide, and 5 ml of phosphate-buffered saline, pH 7.0) to the cells over a 1 min period, incubating the mixture at 37 degrees C for 90 s, then gradually diluting the mixture in 50 ml of Hanks' buffered salt solution. After 10 min, the cells are centrifuged, resuspended in selective medium with feeder macrophages and cultured. This procedure routinely produces between 600-3,000 hybridomas per fusion.
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PMID:Comparison of polyethylene glycols as fusogens for producing lymphocyte-myeloma hybrids. 674 7

Hybridoma cells have been produced by fusing SP2/O-Ag14 mouse myeloma cells with spleen cells from a mouse immunized with a purified preparation of estrogen receptor from calf uterus. The antibodies, all of the immunoglobulin G (IgG) class, interact with different forms of calf receptor as well as with rat and human receptors. The equilibrium dissociation constant of the antibody-receptor complex was measured in solid phase and in solution. With immobilized antibodies the Kd is 0.06 nM whereas in solution it is 0.5 nM. Only one antigenic determinant is present per molecule of receptor with the antibodies tested. The antibodies JS34/32 are able to form only a 1:1 complex with the 8S form of the receptor, whereas a 2:1 receptor-IgG complex is formed at low antibody concentration with the high-salt or nuclear form of receptor. The antibodies JS34/32 and JS28/32 prevent neither the nuclear uptake of the receptor nor the extraction of the translocated receptor from the nuclei.
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PMID:Monoclonal antibodies against estrogen receptor: interaction with different molecular forms and functions of the receptor. 715 74

Staphylococcal neutral phosphatase (NPtase) was purified from two Staphylococcus aureus strains by sequential high salt extraction, ultracentrifugation and ion exchange chromatography. The enzyme showed maximum phosphatase activity at neutral pH, appeared as two bands in SDS-PAGE (31 and 32 kDa), and the isoelectric point was > 10. No close similarity between NPtase and other known bacterial proteins in respect of their N-terminal amino acid sequences was found. Purified NPtase bound rat and human polyclonal IgG [intact and F(ab')2 fragments], IgM, IgA, intact myeloma immunoglobulins, myeloma light chains, gamma heavy chain and, with a much lower affinity, Fc fragments. Furthermore, NPtase can bind serum albumin. Heparin, a highly negatively charged molecule, significantly inhibited NPtase binding to immunoglobulins and HSA, but did not inhibit the binding of specific antibodies to NPtase; this indicates that charge interactions are important. The newly characterized staphylococcal phosphatase with binding properties for immunoglobulin is an interesting bacterial protein that could be involved in post-infectious sequelae.
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PMID:Staphylococcal neutral phosphatase. A highly cationic molecule with binding properties for immunoglobulin. 788 57


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