Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0153470 (Spleen)
 4,015 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Relatively small liposomes (d less than 200 nm) composed of dioleoylphosphatidylethanolamine (DOPE) and cholesterol (Chol) and containing dioleoyl-N-(monomethoxypoly(ethylene glycol)succinyl)phosphatidylethanolamine (PEG-PE), with PEG of M(r) 5000 (PEG5000-PE), accumulate in the spleen (approximately 40% i.v. injected dose), unlike dioleoylphosphatidylcholine (DOPC)/Chol/PEG5000-PE liposomes of similar size, which show prolonged circulation in the blood. Spleen accumulation was dependent on the injection dose, PEG-PE concentration, and the PEG chain length. The DOPE/Chol/PEG5000-PE liposomes are plasma stable and morphologically indistinguishable from DOPC/Chol/PEG5000-PE liposomes. These results reveal the significance of the matrix lipid in determining the circulation time of PEG-PE-containing liposomes, and are relevant to the design of liposomes which avoid or accumulate in the spleen.
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PMID:Amphipathic poly(ethylene glycol) 5000-stabilized dioleoylphosphatidylethanolamine liposomes accumulate in spleen. 151 Oct 2

Production of monoclonal antibodies against human chorionic gonadotropin (hCG) has been studied using hCG as an immunogen. Spleen cells of BALB/c mice immunized with hCG were fused with NS-1 mouse myeloma cells. This study reports the successful isolation of a hybrid clone secreting a monoclonal antibody specific for hCG. By using PEG 4,000 as a fusion agent, the fusion rates were between 42.0 and 50.2%. In total 842 hybridomas were produced. Among them, 403 hybridomas had hCG antibody production. After cloning twice by limiting dilution and alternately screening by enzyme immunoassay and by radioimmunoassay, there were 39 cell lines having specific antibody production. Among them, the No. 57-42-2 had the highest reactivity. By Ouchterlony test, the monoclonal antibody was shown to be IgG1. The affinity constant of the antibody to hCG was 0.6 x 10(9) 1/mole. In radioimmunoassay, the cross reactivity of the antibody to human luteinizing hormone (LH) and human follicle-stimulating hormone (FSH) was 1.5% and 0.7%, respectively. There was no cross reaction with human thyrotropin-stimulating hormone (TSH).
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PMID:Production of monoclonal antibodies to human chorionic gonadotropin. 324 19

1. This paper describes the production and characterization of monoclonal antibodies against bovine parathyroid hormone (bPTH)-(1-84). 2. Spleen cells from A/J mice successfully immunized with bPTH-(1-84) were fused with SP2/O myeloma cells using PEG 4000 as fusogen. The screening method employed microtiter plates coated with sheep antimouse IgG and the presence of specific monoclonal antibodies was demonstrated by the binding of 125I-bPTH-(1-84). 3. A detailed study of the specificity of the three viable monoclonals with highest affinity showed that two (6FH6 and 6CD4) were amino-terminal specific and the other (5BG9) carboxyl-terminal specific. The two amino-terminal monoclonal antibodies appear to recognize the same antigenic site. 4. The monoclonal antibodies produced are potentially useful reagents for the development of new methods for the measurement of PTH in biological fluids, studies on the interaction of PTH with its receptor, as well as localization of PTH producing cells.
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PMID:Monoclonal antibodies to bovine parathyroid hormone: production and characterization. 324 28

During our studies on human kidney tubular antigens we have applied the technique of cell fusion for the preparation of monoclonal antibodies. For this purpose, plasma membranes were prepared from human kidney cortex by homogenization, fractionated on density gradients and selected according to brush border marker enzyme activity. Spleen cells from Balb/c mice hyperimmunized with plasma membranes were fused (PEG) with NS1 plasmocytoma cells by standard procedure. Culture supernatants were tested for presence of specific antibodies by indirect immunofluorescence with fluorescein-conjugated rabbit anti-mouse Fab antibodies on human kidney slices. In two fusions (210 wells), 70 positive hybrids were found secreting antibodies for a variety of antigens in the kidney. Most of them were directed against tubular antigens. In addition, as a by-product, we detected hybridomas which secreted antibodies specific for antigens in other parts of the nephron, such as glomeruli, blood cloning, and monoclonal antibodies were produced in large amounts from ascitic fluid. Some of these antibodies are specific for antigens of the basement membrane, others for antigens of the mesangium. Some recognize antigens present on glomeruli alone, others recognize antigens present on glomeruli and tubules or on glomeruli and blood vessels. We are convinced that the new immunological technique will yield better information on the antigenic microstructure of the nephron. In addition, the monoclonal and, by definition, monospecific antibodies might be useful for diagnostic purposes: recognition and quantitation of the corresponding antigens in the serum and/or urine of patients suffering from kidney diseases.
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PMID:The production of monoclonal antibodies against glomerular and other antigens of the human nephron. 702 87

This is a communication on the introduction of the first monoclonal marker at Graz University Medical School. Human peripheral blood mononuclear cells were used for immunisation of BALB/c mice by injecting 4,5 X 10(6) cells s. c. Boosting consisted of i.p. injection of 5 X 10(6) cells 4 times in monthly intervals. Spleen cells were taken 4 days after the last boost, fused with NS-1 myeloma cells, using PEG as fusogenic agent. After growth in HAT selective medium, antibody secreting clones were identified by testing the supernatants. Cultures with activity against lymphocytes were closed on normal BALB/C peritoneal cell feeder layers. One of them secreted IgG 1 with strong activity against all lymphoid cells and was named HLy D 1. Further testing showed activity with band cells, polymorphs, eosinophils, macrophages but not with tissue sections from anaplastic undifferentiated cancers and erythroid leukaemias. Since he was named H Le D 1 and introduced for differentiating rare undifferentiated carcinomas from malignant tumors of the lymphoid system.
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PMID:[Cell hybridization: a monoclonal marker as a diagnostic help in haematology and oncology (author's transl)]. 727 18

TDRD7 is a scaffold protein whose specific function is unknown. It has been identified in complexes with proteins that regulate cytoskeleton dynamics and centrosomal movements, mRNA transport, and protein translation apparatus. Here we report the generation and characterization of monoclonal antibodies against TDRD7 protein. Bacterially expressed His-tagged fragments of TDRD7 were used as antigens. Spleen cells from immunized mice were collected and fused with SP2/0 myeloma cells using PEG 2000. High titer anti-TDRD7 antibody-producing hybridoma cell lines were identified by enzyme-linked immunosorbent assay (ELISA) and then subcloned by limiting dilution. Antibodies produced by E6 clone were further tested for their reactivity with the TDRD7 recombinant proteins. The results obtained clearly indicate that E6 anti-TDRD7 antibodies recognize specifically recombinant 6His-tagged TDRD7 proteins and endogenous TDRD7 in Western blotting, immunoprecipitation, and immunocytochemistry. In summary, these antibodies will be useful for researchers investigating TDRD7 and molecular complexes involving this protein.
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PMID:Generation and characterization of monoclonal antibodies to TDRD7 protein. 1858 16

As IgM is the first isotype of antibody which appears in blood after initial exposure to a foreign antigen in the pattern of primary response, detection, and quantification of this molecule in blood seems invaluable. To approach these goals, generation, and characterization of a highly specific mAb (monoclonal antibody) against human IgM were investigated. Human IgM immunoglobulins were used to immunize Balb/c mice. Spleen cells taken from the immunized animals were fused with SP2/O myeloma cells using PEG (polyethylene glycol, MW 1450) as fusogen. The hybridomas were cultured in HAT containing medium and supernatants from the growing hybrids were screened by enzyme-linked immunosorbent assay (ELISA) using plates coated with pure human IgM and the positive wells were then cloned at limiting dilutions. The best clone designated as MAN-1, was injected intraperitoneally to some Pristane-injected mice. Anti-IgM mAb was purified from the animals' ascitic fluid by protein-G sepharose followed by DEAE-cellulose ion exchange chromatography. MAN-1 interacted with human IgM with a very high specificity and affinity. The purity of the sample was tested by SDS-PAGE and the affinity constant was measured (K(a) = 3.5 x 10(9)M(-1). Immunoblotting and competitive ELISA were done and the results showed that the harvested antibody recognizes a conformational epitope on the mu chain of human IgM and there was no cross-reactivity with other subclasses of immunoglobulins. Furthermore, isotyping test was done and the results showed the subclass of the obtained mAb which was IgG(1)kappa.
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PMID:Generation of a novel high-affinity monoclonal antibody with conformational recognition epitope on human IgM. 2016 78

Objective To prepare human anti-Mullerian hormone (AMH) immunomagnetic beads and HRP-labeled antibodies and establish a rapid double-antibody sandwich ELISA based on nanometer magnetic beads. Methods The expression vector of human AMH protein was constructed, and the recombinant AMH protein was expressed and purified. BALB/c mice were immunized with the recombinant protein to prepare the polyclonal antibody. Spleen cells were fused with myeloma Sp2/0 cells by PEG. Hybridoma cell lines which could stably secret monoclonal antibodies against AMH were screened out by ELISA. Monoclonal antibodies were produced from the ascites fluid of mice injected intraperitoneally with hybridoma cells and evaluated by Western blotting. Polyclonal antibodies purified from protein A were coupled to nano-magnetic' beads and used as capture antibodies, while HRP-labeled monoclonal antibody was prepared by sodium periodate method and used as probe antibody. A double antibody sandwich ELISA based on the nano-magnetic beads was established and optimized. Results A monoclonal antibody with good specificity for AMH was obtained,' and its subtype was IgG2b. The titers of purified polyclonal antibodies and monoclonal antibodies were up to 1:51 200. The capture antibody coupled with magnetic beads and the probe antibody labeled with HRP kept their good activity. The established method could detect AMH antigen within 1 hour and the detection limit was 50 ng/mL. Conclusion The prepared AMH immunomagnetic beads can be used for the fast and visualized detection of recombinant AMH.
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PMID:[Preparation and application of anti-Mullerian hormone immunomagnetic beads]. 3251 68