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 murine Hybridoma, CEB9, which stably produces monoclonal antibody against human uterine cervical carcinoma is described. CEB9 was obtained by fusing splenic cells from a BALB/c mouse immunized with human uterine cervical carcinoma cell line CC-801 cells with mouse myeloma cell line SP2/0 -Ag14 cells, followed by cloning and subcloning. The antibody is identified as IgG. The results of immunocytochemistry and fluorescence analysis show that the antibody reacted strongly with human uterine cervical carcinoma cells only among the following tested cell lines: PLC/RF/5, 7402, LETP-78, Scle, Hep-2, 2BS, as well as primary cultured human fibroblast cells. Pancreatic carcinoma cells were reactive.
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PMID:[Preparation and characterization of monoclonal antibody against human uterine cervical carcinoma]. 183 11

A monoclonal antibody (mAb), KA8 that interacts with the kappa-opioid receptor binding site was generated. BALB/c female mice were immunized with a partially purified kappa-opioid receptor preparation from frog brain. Spleen cells were hybridized with SP2/0AG8 myeloma cells. The antibody-producing hybridomas were screened for competition with opioid ligands in a modified enzyme-linked immunosorbent assay. The cell line KA8 secretes an IgG1 (kappa-light chain) immunoglobulin. The mAb KA8 purified by affinity chromatography on protein A-Sepharose CL4B was able to precipitate the antigen from a solubilized and affinity-purified frog brain kappa-opioid receptor preparation. In competition studies, the mAb KA8 decreased specific [3H]ethylketocyclazocine ([3H]EKC) binding to the frog brain membrane fraction in a concentration-dependent manner to a maximum to 72%. The degree of the inhibition was increased to 86% when mu- and delta-opioid binding was suppressed by 100 nM [D-Ala2,NMe-Phe4,Gly-ol]-enkephalin (DAGO) and 100 nM [D-Ala2,L-Leu5]-enkephalin (DADLE), respectively, and to 100% when mu-, delta-, and kappa 2-sites were blocked by 5 microM DADLE. However, the mu-specific [3H]DAGO and the delta-preferring [3H]DADLE binding to frog brain membranes cannot be inhibited by mAb KA8. These data suggest that this mAb is recognizing the kappa- but not the mu- and delta-subtype of opioid receptors. The mAb KA8 also inhibits specific [3H]naloxone and [3H]EKC binding to chick brain cultured neurons and rat brain membranes, whereas it has only a slight effect on [3H]EKC binding to guinea pig cerebellar membranes.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:A monoclonal antibody recognizing kappa- but not mu- and delta-opioid receptors. 185 Dec 5

Rabbits were immunized with the Fab fragment of a murine monoclonal antibody (McAb) PD4 against human gastric cancer to produce anti-PD4-idiotypic antibody (alpha PD4-Ab2). The alpha PD4-Ab2 could not only competitively inhibit binding of McAb PD4 to gastric cancer cell MGC803, but also induce delayed-type hypersensitivity (DTH) to MGC803 in mice. Spleen cells of mice immunized with alpha PD4-Ab2 were fused with myeloma cell SP2/0 to form hybridoma secreting Ab3 which could be bound to target cell MGC803. McAb C7-Ab3, one of the Ab3, could selectively react with a 40 kD tumor-associated antigen located on MGC803 cell membrane, as well as McAb PD4. The results indicate that alpha PD4-Ab2 possesses determinants (internal image antigen) similar to those on MGC803, and could mimic human gastric cancer-associated antigen.
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PMID:Anti-FD4 idiotypic antibody mimicking human gastric cancer-associated antigen. 193 49

Actinobacillus actinomycetemcomitans produces a cytolytic peptide leukotoxin which kills susceptible target cells, including human neutrophils, monocytes, lymphocytes, and HL-60 promyelocytic leukemia cells. Cell death occurs as a consequence of colloid osmotic lysis. In the present investigation early leukotoxin-induced changes in membrane permeability were studied by flow cytometry and quantitative spectrofluorimetry in leukotoxin-susceptible and resistant targets. Within 5 s toxin-susceptible cells exhibited concentration-dependent, sustained increases in systolic free Ca2+, and this was rapidly followed by a progressive fall in membrane potential. These early manifestations of membrane injury occurred approximately 10-15 min before cell death, as reflected by flow cytometric analysis of propidium iodide stained cells. The rise in cytosolic Ca2+ was almost entirely due to an influx of extracellular Ca2+. The results of Hill plots for the action of leukotoxin on Ca2+ permeability in human neutrophils or HL-60 cells suggested that two or more toxin molecules participate in the assembly of an ion conducting pore in the plasma membrane. Changes in membrane permeability or cell viability were not observed in response to heat-inactivated toxin. Under appropriate conditions toxin-induced membrane abnormalities were inhibited by leukotoxin-neutralizing mAb or relatively high concentrations (greater than or equal to 2.5 mM) of extracellular Ca2+. Leukotoxin-resistant target cells showed no evidence of membrane injury even when exposed to high concentrations of leukotoxin for prolonged periods of time. These included resistant human K562 erythroleukemia cells and murine SP2 myeloma cells which have previously been shown to adsorb the toxin, suggesting that they possess a protective mechanism(s) which impedes toxin insertion or assembly in the lipid bilayer. These data support the concept that A. actinomycetemcomitans leukotoxin acts as a cell-specific, pore-forming protein which permeabilizes the plasma membrane of susceptible target cells.
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PMID:Early changes in cytosolic calcium and membrane potential induced by Actinobacillus actinomycetemcomitans leukotoxin in susceptible and resistant target cells. 194 Mar 58

Hybridomas were generated by fusing the Balb/c SP2/0 myeloma-like cell line with either: (i) splenocytes from Balb/c mice immunized with foot-and-mouth disease virus (FMDV), rinderpest virus (RPV), peste des petits ruminants virus (PPRV), African swine fever virus (ASFV) or pig thymocytes; or (ii) lymph node cells from cattle immunized with FMDV. If the fusion mixtures were plated in cloning medium of methyl cellulose and HAT medium, small hybridoma colonies developed which rarely survived. Fusion mixtures were then plated in liquid HT medium on to 3T3/A31 feeder layers in 75 cm2 flasks, incubated at 37 degrees C for 24 h before adding aminopterin, and incubated for a further 2 to 4 days before cloning in methyl cellulose/HT medium. Without the aminopterin in the cloning medium, colonies of hybridomas, which could be cultured, developed from the majority of fusions. These colonies were isolated in HT medium over feeder layers and given two subcultures in HAT medium as a precaution against any reversion to aminopterin sensitivity during the cloning. No evidence of such reversions were seen, and recloning results suggested that the initial cloning was highly efficient at generating monoclonal cultures.
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PMID:Rapid isolation of monoclonal hybridoma cultures by a 'fusion-cloning' method: the requirement for aminopterin. 195

Luteinizing hormone-releasing hormone (LHRH) was conjugated to bovine thyroglobulin and used to immunize a BALB/c mouse. Spleen lymphocytes were subsequently fused to SP2/0 myeloma cells and two of the resulting hybridoma clones were found to produce high titer antibodies to LHRH (HU4H and HU11B); both belonged to the IgG1 subclass. Characterization of the monoclonal antibodies revealed that HU4H and HU11B have conformational and sequential specificity to LHRH, respectively, and that neither one shows significant immunoactivity with pro-LHRH. The value of these antibodies in immunocytochemical applications is demonstrated by their ability to cause intense specific staining of LHRH neuronal cell bodies and fibers in brain sections from several mammalian species.
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PMID:Monoclonal antibodies to luteinizing hormone-releasing hormone: production, characterization, and immunocytochemical application. 204 38

Comparison of amino acid sequences of the alpha-chain fragment of human C4, C4d, has shown C4A- and C4B-specific sequences at residues 1101-1106 in which the aspartic acid-histidine substitution at position 1106 may be related to the amide and ester bond forming properties of these molecules. Peptides containing twelve amino acid residues of the C4A- or C4B-specific sequences were synthesized and injected into female Balb/c mice. Serum from 2 mice, one immunized with the C4A-specific peptide and the other with the C4B-specific peptide, gave strong isotype-specific responses in an enzyme-linked immunosorbent assay against affinity-purified C4A3 and C4B2B1. Spleen cells from these mice were fused with the mouse myeloma SP2/0-Ag 14, and two cloned cell lines, AII-1 and BII-1, were established from hybrids. Enzyme-linked immunosorbent assay and western blotting of monoclonal antibodies AII-1 and BII-1 show that the former reacts with the C4A but not with the C4B alpha-chain and the latter with C4B but not with the C4A alpha-chain. Furthermore, immunoblotting of C4 allelic variants showed that AII-1 reacted with all C4A allotypes tested, including A6, A4, A3 and A2, whereas BII-1 reacted with all C4B allotypes tested, including B5, B3, B2, and B1.
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PMID:Monoclonal antipeptide antibodies against amino acid residues 1101-1106 of human C4 distinguish C4A from C4B. 204 34

Monoclonal antibodies (mAbs) to sperm specific antigens were generated by fusion of mouse myeloma cells (SP2/0) with splenocytes of female BALB/c mice hyperimmunized with washed human spermatozoa. The resultant hybridomas producing antisperm antibodies were first screened by ELISA. Out of these, one of the mAbs (D2G4) which recognized target antigens restricted to the acrosomal cap was chosen for these studies. The mAb D2G4 was found to be an agglutinating antibody and was also found to cross-react with mouse epididymal spermatozoa in ELISA and indirect immunofluorescence. The origin of antigens reacting with monoclonal antibody D2G4 was investigated. When frozen sections of murine testis and various regions of epididymis were reacted with mAb D2G4, only the cauda epididymal region was stained. Western blot of proteins from the epididymal spermatozoa and fluid indicated the presence of two bands of mol. wt 45 and 26 kd. These bands were identical under reducing and non-reducing conditions. These observations suggest that the two proteins are structurally similar or at least have a common epitope. These data indicate that the proteins recognized by D2G4 are acquired by spermatozoa during their passage and storage in the cauda epididymis.
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PMID:Immunochemical localization and characterization of proteins from mouse cauda epididymis using human sperm specific monoclonal antibody. 205 23

BALB/c mice were immunized intraperitoneally with outer envelopes of serogroup icterohaemorrhagiae lai serovar strain 017 leptospires. Monoclonal antibodies against outer envelopes (IgG, agglutinating titre 1:25,600) were produced by hybridoma technique. The monoclonal antibodies ascites (diluted 1:100) 1 ml administered intraperitoneally 1 hour before the intraperitoneal injection of 2 x 10(8) leptospires of strain 017 and the subsequent daily administration of McAb in similar doses for five days protected 80% of guinea pigs. Survival rates of three control groups which received physiological saline, ascites of BALB/c mouse myeloma cell lines SP2/0, and monoclonal antibodies against Pseudomonas aeruginosa in place of monoclonal antibodies against outer envelopes of strain 017 leptospires were 10%, 20% and 10% respectively. When killed 20 days after challenge, guinea pigs of experiment group were normal at autopsy. Old pulmonary haemorrhage were present in the animals of three control groups. Passive immunoprotection experiments have demonstrated immunoprotection of monoclonal antibodies against outer envelopes of strain 017 leptospires. It will be valuable for separating protective antigen fraction of outer envelopes and studying new vaccine of leptospira.
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PMID:[Investigation on the immunoprotection of monoclonal antibodies against outer envelopes of serogroup Icterohaemorrhagiae serovar lai strain 017 leptospires]. 209 58

A monoclonal antibody-based immunoenzymometric assay (IEMA) for the measurement of human serum growth hormone is described. Two high-affinity and complementary monoclonal antibodies were selected from a panel of 9 obtained upon fusion of SP2/O myeloma cells with spleen cells from a Balb/c mouse immunized against human growth hormone of pituitary origin. One monoclonal antibody was immobilized by attaching it to the walls of microtiter wells and the second was biotinylated. The reaction was quantitated by the addition of streptavidin-peroxidase. The sensitivity of the assay was 0.2 mIU/l and the intra- and interassay coefficients of variation for 4.6 to 46 mIU/l were less than 8.3 and 17.3%, respectively. Cross-reaction with human placental lactogen, human prolactin and rat growth hormone was less than 0.1% (w/w). Comparison of results obtained for 180 routine serum assays by radioimmunoassay and the assay described here had a correlation coefficient of 0.94 with a mean value of 16.3 +/- 1.3 (mean +/- SEM) and 13.3 +/- 1.2 mIU/l, with the IEMA providing values 18% lower than the RIA. The discrepancy emphasizes the necessity of redefining normal ranges before immunometric assays, like the one described, can be used routinely.
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PMID:Monoclonal antibody-based immunoenzymometric assay for serum human growth hormone. 209 41


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