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 monoclonal antibody, RGL-1, was produced by fusion of NSI myeloma cells with spleen cells of a mouse immunized with isolated rat intraepithelial lymphocytes (IEL). SDS-PAGE analysis revealed that RGL-1 precipitated two major noncovalently bound chains of about m.w. 100,000 and 125,000, and a minor component of m.w. 200,000. Examination of both tissue sections and isolated cells indicated that RGL-1 stained the majority of the lamina propria lymphocytes and IEL but only very few cells (less than 2%) in the lymphoid organs and small numbers of lymphocytes in other mucosae. In the small intestine, RGL-1 stained lymphocytes with the helper (W3/25) as well as the cytotoxic/suppressor (OX8) phenotype. The antibody reacted with 95% of the granular IEL but with less than 0.1% of the blood large granular lymphocytes. Although mature IgA plasma cells in the lamina propria were RGL-1-, some large IgA-containing cells were weakly positive. In the gut-associated lymphoid tissues (GALT), studies combining immunofluorescence and autoradiography indicated that 56 and 73% of rapidly dividing cells of mesenteric lymph nodes and of thoracic duct lymph (TDL) stained with RGL-1, respectively. In addition, 90 to 100% of the IgA-containing blasts of MLN and 75% of those of TDL were labeled by RGL-1. In contrast, rapidly dividing cells of spleen and of peripheral lymph nodes did not stain with RGL-1. Because RGL-1 can be demonstrated on both intestinal lymphocytes and their immediate precursors in the GALT, its expression may be related to the homing of lymphocytes into the gut mucosa.
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PMID:A monoclonal antibody specific for rat intestinal lymphocytes. 241 31

Mouse monoclonal antibodies directed against nerve growth factor (beta NGF) from bovine seminal plasma have been isolated and characterized. They are produced by hybridomas derived from Sp2/0.Ag14 myeloma cells and spleen cells from BALB/c mice immunized with beta NGF which was purified by the method of Harper et al. [J. biol. Chem. 257, 8541-8548 (1982)]. Five of these hybridomas can be grown in ascites tumor form and secrete antibodies of the IgG1 or IgG2a subclass. When used to probe the components of seminal plasma extracts or purified beta NGF as separated electrophoretically on SDS gels, the antibodies react with the beta NGF band at Mr = 15,000. The antibodies bind to native bovine beta NGF, but bind very poorly to mouse beta NGF. Antibody exclusion and additive-binding experiments indicate that these antibodies bind to the 1 antigenic domain. The cell receptor binding site is probably not close to this domain, as the antibodies fail to block the biological activity of bovine beta NGF on cultures of dissociated neurons from sensory ganglia. These monoclonal antibodies define a region in which bovine beta NGF is structurally different from the closely related molecule mouse beta NGF.
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PMID:Monoclonal antibodies to nerve growth factor from bovine seminal plasma. 241 11

We have produced a monoclonal antibody against myelin basic protein that reacts with astrocytes, oligodendrocytes, and Schwann cells. This antibody was generated by fusion of mouse myeloma cells with spleen cells from BALB/c mice immunized with delipidated white matter from adult rat corpus callosum. The antibody was characterized via solid-phase radioimmunoassay, immunoblot of SDS-PAGE, and by indirect immunofluorescence staining of monolayer cultures containing oligodendrocytes, astrocytes, and Schwann cells. Myelin basic protein (MBP) was shown previously to be present only in myelin producing cells in CNS and PNS (oligodendroglia and Schwann cells) and not in astrocytes. The binding of this monoclonal antibody to all 3 cell types suggests that these cells share a common epitope. This epitope may be related to a common progenitor cell.
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PMID:Astrocytes, oligodendrocytes, and Schwann cells share a common antigenic determinant that cross-reacts with myelin basic protein: identification with monoclonal antibody. 242 23

For production of monoclonal antibodies (McAbs), hybrid cells were prepared by fusion of spleen cells of BALB/c mice immunized with the human prostatic cancer cell line PC-82 and the P3-X6(3)Ag8.653 murine myeloma cell line. Supernatants of approximately 500 hybrid clones were screened for prostate specific antibodies using an ELISA on PC-82 cells. A selection of antibodies was further tested for their specificity on a large series of different tissues. A broad cross reactivity pattern was obtained. Most cross reactivity was with pancreatic tissue, kidney, and bowel. One antibody turned out to react with prostate stromal cells. Two McAbs (ER-Pr 1 and ER-Pr 2) reacted solely with prostatic epithelium. Monoclonal antibody affinity chromatography combined with SDS-PAGE showed that both antibodies were directed against a 35-kD protein. Immunoblotting revealed that this protein is identical to prostatic antigen (PA). The epitope detected by ER-Pr 1 and ER-Pr 2 was largely preserved after formalin-fixation of prostatic tissues which renders these antibodies very suitable for routine examination of tissue sections.
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PMID:Characterization of monoclonal antibodies raised against the prostatic cancer cell line PC-82. 242 90

Spleen cells from Balb/c mice immunized with purified rat plasma kininogen were fused to P-3 mouse myeloma cells. Positive clones were identified by enzyme linked immunosorbent assay (ELISA), cloned successively two times with limiting dilution and expanded as ascites tumors. Five hybridomas were developed that produced monoclonal antibodies against plasma kininogen. Two of the secreted antibodies were of the IgG1 (k) isotype and the remaining three were of the IgG1(lambda), IgG2A(k) and IgM(k) isotypes respectively. The specificity of the monoclonal antibodies was confirmed by the immunoprecipitation of kininogen with the antibodies coupled to Sepharose-4B followed by SDS-polyacrylamide gel electrophoresis. These monoclonal antibodies recognize at least two distinct epitopes on rat plasma kininogen.
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PMID:Monoclonal antibodies to rat plasma kininogen. 243 8

Two mouse monoclonal antibodies (MoAbs), B10 and 1H5, were generated by fusing mouse myeloma NS-1 cells with spleen cells from a BALB/c mouse immunized with Ueda-1 cells derived from human squamous cell carcinoma (SCC) of the floor of the mouth. Immunohistochemical analysis revealed that these MoAbs recognize the filamentous components of cytoplasm which were protein in nature. While the pattern of antigen distribution in various cell lines was not cell-type specific, reactivity of these antibodies with tissue sections was informative. MoAb 1H5 was preferentially reactive with well-differentiated squamous cell carcinoma, however, reaction with adenocarcinoma was observed infrequently. This antibody also preferentially reacted with the spinous layer of normal stratified squamous epithelium. MoAb B10, however, was reactive with nonepithelial tissues as well as with epithelial ones, and its level of binding bore no relationship to the grade of histologic malignancy. SDS-PAGE and Western blotting analysis, using cytokeratin extracts of Ueda-1 cells and human epidermis, demonstrated that MoAb B10 reacted with a wide range of keratin proteins of 65-67K, 58K, 56.5K, 56K, 52K, 50K, 48K, 45K, 40K, 38K, 36K, and 34K molecular weight (MW), while MoAb 1H5 reacted with keratin proteins of 65-67K, 58K, 56.5K, 56K, 52K, 48K, and 34K MW. These results suggest that MoAb 1H5 may recognize keratin subfamilies related to squamous differentiation, whereas MoAb B10 recognizes a wide range of keratin proteins, and may even react with other kinds of intermediate filament proteins (IFPs).
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PMID:Monoclonal antibodies against human oral squamous cell carcinoma reacting with keratin proteins. 244 66

Monoclonal antibodies against human and bovine 2':3'-cyclic nucleotide 3'-phosphodiesterase (CNPase) were generated by fusing FOX-NY myeloma cells with spleen cells from RBF/Dn mice previously immunized with the purified brain antigens. The enzyme isolated from bovine brain was quite basic, with an isoelectric point of 9.71 and both the bovine and human enzymes consisted of a closely spaced doublet at approximately 44 and 46 kDa on SDS-PAGE. Six monoclonals were were identified as strongly recognizing the enzyme on both ELISA plates and on immunoblots of whole brain protein. Four monoclonals very weakly cross-reacted with guinea pig myelin basic protein. In contrast with two previous reports, some of our monoclonal antibodies did immunostain 2 or 3 protein bands in peripheral nerve, two bands closely corresponding to those immunostained in central nervous system (CNS) myelin, the Wolfgram protein fraction and in acetone powders of whole brain. Each of the 6 monoclonals reacting strongly on immunoblots recognized the enzyme in from 2 to 5 of the species examined (human, bovine, rat, mouse and rabbit). In addition, all 6 monoclonals that immunostained the enzyme in whole brain, myelin and Wolfgram protein immunoblots recognized both CNP1 (44 kDa) and CNP2 (46 kDa). The two closely spaced protein bands observed on SDS-PAGE and previously stained on immunoblots of CNS CNPase using polyvalent rabbit anti-bovine CNPase antisera, and now different monoclonal antibodies, appear to be immunologically related and to contain highly conserved sequences.
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PMID:Monoclonal antibody production to human and bovine 2':3'-cyclic nucleotide 3'-phosphodiesterase (CNPase): high-specificity recognition in whole brain acetone powders and conservation of sequence between CNP1 and CNP2. 244 13

Nerve growth factor (NGF) was isolated from the venom of Vipera lebetina and was purified to homogeneity as judged by SDS gel electrophoresis. The biologically active NGF was used to immunize BALB/c mouse, and the spleen cells from immunized mouse were fused with mouse PAI myeloma cells. Forty-seven hybrid cell lines, secreting monoclonal antibodies to V. lebetina NGF, were isolated and nine of them purified from ascitic fluids. The isolated antibodies define two partially overlapping epitopes of the V. lebetina NGF which are not involved in the biological activity of the molecule. Both epitopes are also present on the beta-NGF from the mouse salivary gland and on the NGFs from the following snake venoms: V. lebetina, V, ursini, V, berus berus, Echis carinatus, Bungarus caeruleus, Agkistrodon halys, Naja naja oxiana, Naja naja atra and Naja naja, but not on the bovine seminal plasma NGF. The mol. wts of the NGFs in these snake venoms were determined by Western immunoblot with monoclonal antibodies. The mol. wts of the NGFs from V. ursini (37,000), E. carinatus (36,000, 44,000) and A. halys (29,000) were determined for the first time.
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PMID:Monoclonal antibodies against Vipera lebetina venom nerve growth factor cross-react with other snake venom nerve growth factors. 244 8

In the present investigation, we have utilized the somatic cell hybridization technique to generate an experimental model for studying the differential expression of membrane (mIg) and secreted (sIg) forms of immunoglobulin that characterize different stages of B cell development. We describe here that fusion of the dextran-binding myeloma, MOPC 104E (mu, lambda 1) and the phthalate-binding B cell hybridoma, 2C3E1 (gamma 1, kappa) results in the formation of antigen-specific, double hybrids (tribrids) that coexpress both parental secreted forms of Ig but express only one of the two possible membrane forms of immunoglobulin (Ig). This segregated expression of membrane Ig is a new and unexpected finding that has been substantiated here by both immunological and biochemical methods. Analysis by SDS-containing polyacrylamide gels (SDS-PAGE) reveals distinct and characteristic migration patterns for each of the four Ig heavy chains in the tribrids (mu membrane, mu secreted, gamma 1 membrane and gamma 1 secreted). Immunochemical analysis of the immunoglobulin from the tribrids confirms the coexpression of both secreted forms of immunoglobulin in most of the tribrid lines tested and indicates that about 30% of the tribrids express only phthalate-specific gamma 1 membrane Ig, while 38% express only dextran-binding mu membrane Ig. About 30% of the tribrids secrete both antibodies but express no membrane form and less than 1% are non-secretors. Approximately 2% initially express both membrane forms of Ig, as determined by immunocytoadherence assay using appropriate target cells but subsequently express only one membrane form during propagation in vitro. SDS-PAGE analysis of surface labeled tribrids confirms that in tribrids expressing membrane Ig, only a single mIg is synthesized. These results suggest that the expression of the secreted and membrane forms of immunoglobulin are separately regulated and the tribrids represent a model with which to study the mechanisms involved in the regulation of each structurally distinct immunoglobulin form.
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PMID:Expression of mu and gamma 1 membrane forms of immunoglobulin segregate in somatic cell hybrids. 244 9

The Engelbreth-Holm-Swarm mouse tumor has been found to produce at least two molecular species of heparan sulfate proteoglycan, a low density one (LD) and a high density one, which differ not only in core proteins but also in glycosaminoglycan structures (Kato, M., Y. Koike, Y. Ito, S. Suzuki, and K. Kimata. 1987. J. Biol. Chem. 262:7180-7188). With aim at investigating their distribution and possible functions in tissues, monoclonal antibodies were produced. Hybridomas obtained by fusion of NS-1 mouse myeloma cells with spleen cells from the rat immunized with a mixture of these proteoglycans were selected by their ability to react with the antigen. Two of them secreted monoclonal antibodies (IgG2a), designated HK-84 and HK-102, that recognize specifically the core protein moiety of LD. Immunofluorescent staining of various tissues (skeletal muscle, cardiac muscle, lung, brain, and kidney) with these monoclonal antibodies has demonstrated that the antigen molecules were present in all basement membranes of these tissues. SDS-PAGE of heparitinase-treated proteoglycan fractions prepared from these tissues and subsequent immunoblotting using these monoclonal antibodies have confirmed that the antigen molecule was LD, and further suggested that there was a tissue-specific variation in the core molecular size. Based on these results, we propose that LD may be an essential component in all basement membranes.
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PMID:Basement membrane proteoglycan in various tissues: characterization using monoclonal antibodies to the Engelbreth-Holm-Swarm mouse tumor low density heparan sulfate proteoglycan. 245 34


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