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)

We have synthesized three peptides with amino acid sequences corresponding to amino acids 533-547, 597-611, and 765-779 of the human progesterone receptor (hPR). These peptides were conjugated to keyhole limpet hemocyanin and injected into mice and rabbits to develop antibodies to hPR. Antibodies to the undenatured form of PR were elicited only by the peptide with amino acid sequence 533-547. Fusion of SP2/0 myeloma cells with spleen cells from mice immunized with this peptide produced several active clones. Rabbit sera from immunized animals produced one antiserum that reacted with the undenatured form of PR. One monoclonal antibody (PR-AT 4.14) and one antiserum (PR-AT533) raised against peptide-(533-547) were characterized. Binding of these antibodies to the undenatured form of PR was demonstrated by analysis of the antibody-receptor complexes on sucrose density gradients and by immunoprecipitation techniques. Binding of PR to the antibodies was inhibited by excess peptide. The antibodies did not react with estrogen, glucocorticoid, or androgen receptors, but recognized PR from human breast cancer as well as calf, rabbit, mouse, and rat uteri, indicating that this epitope was conserved among these species. Based on sucrose density gradient analysis of PR prepared and labeled in the presence of proteolysis inhibitors and sodium molybdate, the antibodies bound to a site on the intact undenatured PR, but failed to bind to partially degraded steroid-binding form of the receptor, suggesting that the antibody-binding domain is at or near a site sensitive to proteolysis.
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PMID:Monoclonal and polyclonal antibodies to human progesterone receptor peptide-(533-547) recognize a specific site in unactivated (8S) and activated (4S) progesterone receptor and distinguish between intact and proteolyzed receptors. 220 32

Spontaneous fusion between lymphoid and carcinoma cells in vivo has been described previously. Splenocytes from mice treated with LPS or mitogen have been reported to fuse better with myeloma cells using PEG as fusion agent than splenocytes from untreated mice. We report a phenomenon where immunization of mice with formalin treated, whole Haemophilus paragallinarum bacteria induced spontaneous fusion of splenocytes with myeloma cells in vitro, without the aid of any fusion agent. Co-immunization of mice with H. paragallinarum and an unrelated antigen (hen's egg white lysozyme), followed by co-culturing of the immune splenocytes with SP2/0 myeloma cells, yielded stable hybridoma cell lines producing anti-lysozyme antibodies. H. paragallinarum may be used in adjuvants to simplify the production of monoclonal antibodies, and the discovery of a promotional activity of a gram negative bacterium on cell fusion and hybridoma formation may shed new light on spontaneous fusion as a natural immune phenomenon in cancer.
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PMID:Spontaneous fusion between splenocytes and myeloma cells induced by bacterial immunization. 225 87

N-acetyl-aspartyl-glutamate (NAAG) is a putative neuromodulator/neurotransmitter in the mammalian nervous system. Immunohistochemical studies with polyclonal NAAG antisera have revealed immunoreactive neurons and processes in several brain regions. However, these antisera crossreact to some degree with N-acetyl-aspartate (NAA), which is present in mM concentrations in brain, prompting the development of monoclonal antibodies (MAb) more specific for NAAG. By fusing spleen lymphocytes obtained from BALB/c mice pre-immunized with NAAG covalently linked to bovine serum albumin by carbodiimide with SP2/0-Ag 14 mouse myeloma cells, we produced three IgG2a (kappa) MAb which specifically reacted with NAAG. These MAb exhibited negligible crossreactivity with NAA or with structurally similar peptides, as shown by solid-phase radioimmunoassay. Antibody activity was absorbed out selectively by both NAAG-thyroglobulin conjugate and free NAAG. These MAb stained many nuclei of the medulla-pons and midbrain, mitral cells in the olfactory bulb, pyramidal neurons in sensorimotor cortex, locus ceruleus, and several cholinergic cranial nuclei. The staining pattern strongly correlated with NAAG levels determined by HPLC. Monoclonal antibodies significantly enhanced sensitivity of staining, allowing visualization of dorsal horn neurons in spinal cord, which were not readily detectable with polyclonal antiserum. Availability of these MAb now facilitates further clarification of the role of NAAG in the brain.
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PMID:Production and characterization of monoclonal antibodies to N-acetyl-aspartyl-glutamate. 231 20

Mouse monoclonal antibodies (Mabs) against the human breast cancer cell line MCF-7 were obtained by fusing spleen cells from immunized mice with SP2/0 myeloma cells. The Mabs obtained show a high degree of specificity for epithelial cells. They react in a heterogeneous way with neoplastic and non-neoplastic tissues. Mabs 5D10, 2B4, and 3B7 recognize the same antigen (MW 80,000-90,000) in fresh tissue and in paraffin embedded sections. Mab 11F9 recognizes another antigen which can only be detected in unfixed tissue and not in paraffin sections. A preliminary study suggests a glycolipid nature of all recognized antigens. At least one of the monoclonal antibodies (5D10) developed can be used in an in vitro and in vivo model for the study of the invasiveness of MCF-7 cells.
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PMID:Production of immunohistochemical reactivity of mouse anti-epithelial monoclonal antibodies raised against human breast cancer cells. 233 39

Splenocytes derived from mice inoculated with a commercial cellulase preparation or purified cellulases were fused with a stable myeloma cell line (SP2/0). Specific monoclonal antibodies to cellobiohydrolases I and II and endoglucanases I and II were established. In addition to specific monoclonal antibodies, we were also able to establish stable hybridoma cell lines which produced monoclonal antibodies that recognized similar epitopes possessed by two or more of the above cellulases. By obtaining monospecific antibodies for all four individual cellulases, the role and function of the individual cellulases can thus be studied in greater detail.
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PMID:Cross-reactive and specific monoclonal antibodies against cellobiohydrolases I and II and endoglucanases I and II of Trichoderma reesei. 233 71

The polyclonal antibodies to juveniles of Paragoniums westermani (PwJ-PcAbs) from sera of Wistar rats infected with Paragoniums westermani (P.w.) were purified by Sephadex G 200 chromatography. Next the shared serological antigens of P.w. metacercaria and juveniles (PwMJ-SAg) from the crude antigens of the metacercariae (M-NS-Ag) were purified with immuno-affinity chromatography on cyanogen bromide-activated cross-linked Sepharose 4B beads coupled with PwJ-PcAbs. PwMJ-SAg, a group of glycoprotein molecules shown by the staining test, were specific serological antigens of P.w. metacercariae and juveniles, identified by the immunoabsorb test and immunoelectrophoresis. By SDS-PAGE, PwMJ-SAg were fractionated to seven bands, including major bands A (27.5 K) and Bi (19.5 K), the two major serological antigen molecules. 20 sera samples from the patients with the nonpulmonary type of P. w. paragonimiasis were detected using PwMJ-SAg and M-NS-Ag by Dot-ELISA, and the difference of sensitivity between two antigens was highly statistically significant (P less than 0.001). BALB/c mice, in the early stage of infection with P. w. metacercaria, were immunized with PwMJ-SAg. The spleen cells of the mice were isolated and fused with SP2/o, a murine myeloma cell line. After three subclonal cultures, eight cell lines secreting monoclonal antibodies (McAbs) to PwMJ-SAg were prepared from 384 wells of hybridoma cells. All McAbs were IgG1 subclass.
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PMID:Studies on specific serological antigens in metacercariae and juveniles of Paragoniums westermani and its monoclonal antibodies. 234 88

This study was undertaken to evaluate the use of serum alpha 1-antitrypsin (alpha 1AT) in clinical diagnosis of primary hepatic carcinomas with monoclonal antibody-rate nephelometry. BALB/c mice were injected with human alpha 1AT. Spleen cells of the immunized mice and SP2/0 myeloma cells were hybridized in vitro. Monoclonal antibodies against alpha 1AT so obtained were used as detection agents in immuno-chemical monitor system (ICS). In 50 healthy individuals, serum alpha 1AT was 209 +/- 46.04 mg/dl. Serum alpha 1AT was determined in 49 patients with primary hepatic carcinoma, 26 with chronic active hepatitis and 26 with cirrhosis. Their positive rates were 43%, 3.8% and 0, respectively. Serum alpha 1AT level was significantly higher in primary hepatic carcinoma than in chronic active hepatitis and cirrhosis patients (P less than 0.001). No difference was found in alpha 1AT between patients with benign liver diseases and healthy adults (P greater than 0.05). The results indicate that alpha 1AT is useful in the diagnosis of primary hepatic carcinomas.
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PMID:[Alpha 1-antitrypsin in clinical diagnosis of primary hepatic carcinoma--an appraisal of monoclonal antibody-rate nephelometry]. 236 69

BALB/c mice were infected per os with the infective larvae (L1) of Trichinella spiralis, and challenged by injecting 0.2ml soluble L1 antigen 3 days before cell fusion. SP2/0 myeloma and immune spleen cells were fused at the ratio of 1:5 in the presence 30%PEG (MW 4,000). The fusion rate and antibody positive rate were 92.1% and 16.6% respectively using ELISA. Among these the chromosomes of 4 strains were 2n greater than 100 and that of the SP2/0 myeloma cells 2n less than or equal to 70. The titer of McAb in the ascites was found to be 1/640 or 1/1,280. Eight strains were of IgG1, 1 IgG2a and 3 IgM in an agar system. Three strains of McAbs, which could recognize specifically the L1 antigen fractions by immuno-blotting technique, were used as probes to localize the target antigens in sections of T. spiralis L1. Staining was performed using an indirect technique consisting of goat anti-mouse IgG-conjugated horseradish peroxidase on de-paraffin sections, and substrate DAB. The results revealed that the antigens reacted most strongly with the specific McAbs were located in the cuticle and stichosome, followed by the lining of gut. Among the 3 strains of McAbs used, 2E5F11A5 reacted most strongly with the antigen, followed by 2E5E9E4. 2E5E9G5 was the weakest.
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PMID:[Preparation of monoclonal antibodies against Trichinella spiralis and localization of antigens]. 236 31

BALB/c mice were immunized with the purified p30 antigen. SP2/0 myeloma cells and immune spleen cells were fused with 50% PEG (Sigma, MW 3,350-4,000). The cell fusion rate was 93.95%, and the antibody producing rate 21.01%. The technique of limiting dilution was used for cloning of the hybridoma cells. Two hybridoma cell lines E8 and G1 secreting McAb against p30 antigen were obtained. The number of chromosome of both E8 and G1 cell lines was 98.7 +/- 6.54 and 97.7 +/- 7.77, respectively. Results of the PAGE of the ascites generated by the hybridoma cell lines E8 and G1 showed a thick protein band at the gamma-region which was absent from the ascites generated by the SP 2/0 myeloma cells. The immunoglobulin of the McAb E8 and G1 belonged to IgG2 subclass. The results of the immunohistochemical method using the horseradish peroxidase conjugated antibody showed that both E8 and G1 McAb only reacted with epithelial cells of the normal human prostatic glands and their ducts, but did not cross-react with other thirty-four different kinds of normal human tissues. The results of inhibiting ELISA test showed that both E8 and G1 McAb were only inhibited by the human seminal plasma and p30, weakly inhibited by the adult male's urine, but were not inhibited by other eight different kinds of human body fluids and secretions as well as semen from eight different species of animals. It was concluded that McAb of E8 and G1 were organ and species specific.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:[Establishment of hybridoma cell lines producing monoclonal antibodies against-p30 antigen]. 236 36

Five different hybridoma clones secreting anti-HBeAg antibody were constructed by fusing cells of mouse myeloma line SP2/0 with splenocytes from BALB/c mice immunized with recombinant HBeAg. The monoclonal antibodies obtained were characterized immunologically and one was used to develop ELISA for detection of HBeAg and anti-HBeAg antibody. These monoclonal assays enabled the detection of 3 U HBeAg/ml and 1 U anti-HBeAg/ml with reference to standards of the Paul Ehrlich Institute, Frankfurt, F.R.G. Both assays compared well with a commercially available kit (Abbott Laboratory) and were used for detection of HBeAg and anti-HBeAg antibody in clinical serum samples.
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PMID:Monoclonal antibodies against hepatitis B e antigen: production, characterization, and use for diagnosis. 237 Feb 87


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