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Target Concepts:
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Query: UMLS:C0026764 (
multiple myeloma
)
36,148
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Monoclonal antibodies (MAbs) were obtained from hybridoma clones established by cell fusion between P3X63Ag8.653 mouse
myeloma
cells and spleen cells of mice or rats hyperimmunized against human bladder cancer tissue or BC47 rat bladder cancer cells. RBS-31 and RBS-85 mouse MAbs and
RBA
-1 rat MAb were raised against BC47 cells and HBP-1 MAb was raised against human bladder cancer tissues. Urinary antigens detected by these MAbs were quantitatively assayed by means of ELISA using 50 microliters of 1:2 diluted urine samples. The cut-off value of the assay was set up as the mean + 4 X SD of the mean using data from the healthy individual urine samples. The reactivity of all healthy control urine samples were under the cut-off value (negative). By contrast, urine from bladder cancer patients reacted positively with the RBS-31 MAb at 72%, with the RBS-85 MAb at 63%, with the
RBA
-1 MAb at 51% and with the HBP-1 MAb at 35%. The urine samples from some patients with renal calculi, acute cystitis or complicated urinary tract infections showed only a weak reactivity with our MAbs. As for extra-bladder cancers, some patients with renal, renal pelvis, prostate or ureter cancer, but no patients with esophageal, gastric, colon or liver cancer or leukemia, had reactive urinary antigens.
...
PMID:Increase in murine monoclonal-antibody-defined urinary antigens in patients with bladder cancer and benign urogenital disease. 267 68
The Mr 52,000 glycoprotein is regulated by estrogen and released by breast cancer cells in culture (B. Westley and H. Rochefort, Cell, 20: 352-362, 1980). This rare protein was partially purified from 25 liters of medium conditioned by MCF7 cells and injected into Biozzi's selected mice. The spleen lymphocytes of one immunized mouse was fused with the murine
myeloma
P3-X63-Ag8-653. Sixteen hybridomas producing monoclonal antibodies to the Mr 52,000 protein were isolated, and seven of them were cloned and purified. The seven monoclonal antibodies were all of the immunoglobulin G1 isotype, and their dissociation constants ranged from 0.35 to 2.3 nM. The antibodies specifically recognized the secreted Mr 52,000 protein as evidenced by double immunoprecipitation and by immunoblotting after electrophoretic separation and transfer. Double-determinant immunoradiometric assay indicated that the seven purified monoclonal antibodies recognized three distinct regions of the Mr 52,000 protein, and it was used to assay the Mr 52,000 protein in biological fluids. These antibodies did not react with the external plasma membrane of MCF7 cells, as shown by immunofluorescence analysis. By contrast, the cytoplasm of MCF7 cells (but not T47D and
RBA
cells) was stained by the peroxidase-immunoperoxidase complex after plasma membrane permeation, indicating that the protein is secreted by exocytosis rather than shed from the plasma membrane.
...
PMID:Characterization of monoclonal antibodies to the estrogen-regulated Mr 52,000 glycoprotein and their use in MCF7 cells. 388 Nov 71