Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UMLS:C0026764 (multiple myeloma)
 36,148 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Spleen cells from BALB/c mice previously immunized with B-lymphoblastoid cell line RPMI-1788 were fused with P3-X-63-Ag8.653 myeloma cells. Monoclonal antibodies (Ab) IPO-4 were screened on 18 cell lines by the indirect immuno-fluorescence method. Cryostat sections of tissues were stained according to the PAP technique. The Mab IPO-4 were tested for reactivity with blood cells of 17 healthy persons and 102 patients with chronic lymphocytic leukemia, acute lymphoblastic and myeloblastic leukemias, hairy cell leukemia, multiple myeloma, non-Hodgkin's lymphomas and Hodgkin's disease and mitogen stimulated lymphocytes. MAb IPO-4 were found to be directed against antigen expressed on activated T and B cells.
 ...
PMID:[Monoclonal antibodies IPO-4 recognizing antigen-activated human T and B lymphocytes]. 234 19

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.
 ...
PMID:[Alpha 1-antitrypsin in clinical diagnosis of primary hepatic carcinoma--an appraisal of monoclonal antibody-rate nephelometry]. 236 69

Spleen cells of Biozzi-HR mice immunized with human thyroglobulin (hTg) were fused with P3-X63-Ag8.653 mouse myeloma cells. Twenty monoclonal antibodies (MAbs) selected by an enzyme immunoassay (indirect ELISA) were produced, purified and characterized. The equilibrium association constant (Ka) of one of the MAbs, determined by Scatchard analysis of the ELISA data, was found to be 2 X 10(9) M-1; the Ka of the other MAb, estimated from titration curves by comparison with the aforementioned MAb, ranged from 8 X 10(9) M-1 to 6 X 10(7) M-1. The reaction between the MAb and hTg was not inhibited by thyroxin (T4), triiodothyronine (T3) and triiodothyropropionic acid (DT3). Species specificity of the MAb was studied using bovine and porcine Tgb. The topology of the MAb was investigated by competitive inhibition immunoassays. Seven distinct antigenic regions were identified.
 ...
PMID:Production and characterization of monoclonal antibodies against human thyroglobulin. 241 47

Spleen cells from hamsters immunized with recombinant mouse interferon-gamma (IFN-gamma) were fused with mouse myeloma cells, resulting in the production of four anti-IFN-gamma monoclonal antibodies. Binding of 125I-IFN-gamma by these protein A-bound antibodies was specifically blocked by cold IFN-gamma. Binding by three of these antibodies was also blocked by a synthetic peptide corresponding to the N-terminal 1-39 amino acids of IFN-gamma, whereas a corresponding C-terminal (95-133) peptide had no effect on binding. The N-terminal specificity of these three antibodies was confirmed by their specific binding of 125I-N-terminal (1-39) peptide. One of the N-terminal specific monoclonal antibodies inhibited both antiviral and macrophage priming (for tumor cell killing) activities of IFN-gamma, whereas the other two had no effect on either biologic function. The selectivity of the inhibition of IFN-gamma function was not due to a differential ability of the N-terminal specific antibodies to bind IFN-gamma. Blocking experiments with cold IFN-gamma and N-terminal peptide suggest that the epitope specificities of the monoclonal antibodies could be determined by the conformational or topographic structure of IFN-gamma. An exact determination of the epitope specificity of the monoclonal antibody that inhibited IFN-gamma function could provide insight into the structural basis for the role of the N-terminal domain in the biologic function of IFN-gamma. Polyclonal antibodies to either the N-terminal or the C-terminal peptides also inhibited both the antiviral and the macrophage-priming activities of IFN-gamma. All of the antibodies that inhibited IFN-gamma function also blocked binding of IFN-gamma to membrane receptor on cells, whereas antibodies that did not block function also did not inhibit binding. The data suggest that both the N-terminal and the C-terminal domains of IFN-gamma play an important role in its antiviral and macrophage-priming functions, possibly in a cooperative manner.
 ...
PMID:Epitope and functional specificity of monoclonal antibodies to mouse interferon-gamma: the synthetic peptide approach. 242 Aug 86

Spleen cells of Biozzi HR mice immunized with formolized, lyophilized Candida albicans serotype A cells were fused with P3-X63-Ag8.653 mouse myeloma cells. Twenty-one monoclonal antibodies (mAb) selected by an indirect ELISA technique were produced and partially characterized. All mAb reacted with a C. albicans cell wall extract. Five of the mAb were directed against C. albicans serotype A, but not against serotype B. These mAb also recognized C. tropicalis. The 16 other mAb cross-reacted with several yeast species. The immunoreactivity profiles of 5 representative anti-Candida mAb were confirmed in most cases by inhibition studies.
 ...
PMID:Production and partial characterization of anti-Candida monoclonal antibodies. 242 14

Monoclonal antibodies to different domains of the porcine intestinal 1,25-dihydroxyvitamin D3 [1,25-(OH)2D3] receptor have been produced. A nuclear extract enriched in the 1,25-(OH)2D3 receptor was prepared from small intestinal mucosa of young pigs. The receptor was purified an additional 6600-fold by chromatography on DNA-cellulose, ammonium sulfate precipitation, gel filtration high-performance liquid chromatography, and DEAE-Sepharose chromatography, with an overall yield of 23% and an average purity of 24%. A BALB/c mouse immunized with this material developed serum polyclonal antibodies to the 1,25-(OH)2D3 receptor, as demonstrated by a change in sedimentation of the porcine receptor on sucrose gradients. Spleen cells from this animal were fused with mouse myeloma cells (P3-NSI/1-Ag4-1, SP2/0-Ag14), and 24 hybridomas secreting antibodies to the 1,25-(OH)2D3 receptor were identified by both a radiometric immunosorbent assay and an immunoprecipitation assay. Twenty-one hybridoma lines were cloned by limiting dilution and further characterized as subclass IgG1 antibodies with the exception of one which is an IgA. All but two of the antibodies cross-react with the 1,25-(OH)2D3 receptor from both mammalian (human, monkey, and rat) and avian (chicken) intestine; two antibodies recognize only porcine intestinal receptor. All antibodies are unreactive to the vitamin D serum transport protein. Eight of the antibodies bind denatured receptor on an immunoblot. A solid-phase competition assay was used to identify four groups of antibodies that bind to distinct epitopes on the 1,25-(OH)2D3 receptor. One antibody from each of the four groups was used to examine the effect of antibody binding on the DNA-binding activity of the receptor-hormone complex. One antibody completely inhibited the binding of the 1,25-(OH)2D3 receptor complex to DNA-cellulose, suggesting that the epitope for this antibody may be located in the polynucleotide binding domain of the protein. Antibodies from two additional groups only slightly perturbed DNA binding, while one had no effect, suggesting that these antibodies bind to receptor epitopes distant from the region of the polypeptide directly involved in polynucleotide binding. These antibodies that are directed to several different binding sites on the 1,25-(OH)2D3 receptor provide important new tools to probe the biochemistry and topology of the 1,25-(OH)2D3 receptor and to investigate its role in mediating target tissue response to hormone.
 ...
PMID:Monoclonal antibodies to the porcine intestinal receptor for 1,25-dihydroxyvitamin D3: interaction with distinct receptor domains. 242 89

Spleen cells from Balb/c mice immunized with human breast cancer cells (MCF-7) were fused with murine myeloma SP2/0 cells. Screening of the monoclonal antibodies produced was carried out on glutaraldehyde fixed cells coated on microtiterplates. An initial evaluation of the specificity was obtained by comparing the binding of the monoclonal antibodies to MCF-7 cells with the binding to human peripheral blood lymphocytes. Eight monoclonal antibodies reacting with different epitopes on the MCF-7 cells were obtained. On the basis of their clonal origin, isotype and reaction pattern towards the MCF-7 cells these monoclonal antibodies were subdivided into two classes. Both groups of antibodies reacted with fixed and unfixed MCF-7 cells. The cellular distribution of the antigens recognized by the monoclonal antibodies was determined. To check for specificity a panel of different cells (of human and animal origin) was evaluated by immunocytochemical techniques.
 ...
PMID:Specific monoclonal antibodies reacting with human breast cancer cells. 243 33

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.
 ...
PMID:Monoclonal antibodies to rat plasma kininogen. 243 8

Thirteen monoclonal antibodies (MAbs) were produced against Lol p I (Rye I), the major Lolium perenne (rye grass) pollen allergen. Spleen cells from A/J and SJL mice immunized with highly purified Lol p I (Lol I) were allowed to fuse with cells from the non-secreting Sp2/0-Ag14 myeloma cell line. Each MAb was analyzed for antigenic specificity by radioimmunoassay (RIA) using 125I-Lol I. The epitope specificities of seven of the MAbs were examined by competitive binding against a labelled standard MAb for the Lol I antigen (Ag). The dissociation constant, Kd, of one MAb (No. 3.2) that was studied most extensively was determined by double Ab RIA to be 3.5 X 10(-6) L/M. This MAb recognized the related 27,000-30,000 Group I glycoproteins found in the pollens of nine other species of grass pollens tested, including weak binding to Bermuda grass Group I (Cyn d I), which by conventional analysis using polyclonal anti-Lol I serum shows no detectable binding. Monoclonal antibody No. 3.2 was coupled covalently to Sepharose 4B and used to prepare highly purified Lol I from a partially purified rye pollen extract. Finally, an RIA was developed which permitted the analysis of the Group I components in rye grass and nine other grass pollen species. The latter assay is likely to prove useful in the standardization of grass pollen extracts according to their Group I contents.
 ...
PMID:Monoclonal antibodies to the major Lolium perenne (rye grass) pollen allergen Lol p I (Rye I). 243 41

To avoid the exclusive use of rodent monoclonal antibodies (MAbs) in patients for the detection of tumors by immunoscintigraphy and for radioimmunotherapy, swine MAbs were produced that are directed against carcinoembryonic antigen (CEA). Spleen cells from 2 pigs immunized with purified colon carcinoma CEA were fused with a nonsecreting mouse myeloma cell line by conventional methods, except that a particularly long immunization protocol and large amounts of spleen and myeloma cells were used. Of 1,200 growing hybrids tested, 20 were found initially to produce antibodies binding to radiolabeled CEA. Seven stable clones producing anti-CEA MAbs for more than 6 months were derived from these hybrids by repeated subcloning. The pig origin of the seven MAbs was demonstrated in a solid-phase CEA enzyme immunoassay where anti-pig immunoglobin (Ig) antibodies coupled to peroxidase gave a positive reaction while anti-mouse Ig antibodies were entirely negative. All swine MAbs were of the IgG isotype. Three anti-CEA MAbs showed no cross-reactivity with granulocytes, while four others gave various degrees of reactivity with different granulocyte glycoproteins. Competitive binding to CEA performed for two purified swine MAbs showed that they recognized two different epitopes. The affinity constants measured for these two MAbs by Scatchard plot on purified CEA were high (1.2 X 10(9) and 1.2 X 10(10) liter/mol). One of the MAbs was tested in vivo for tumor localization by injection, after radiolabeling, in nude mice bearing human colon carcinoma xenograft. High ratios of tumor to normal tissue were obtained with mean values of 10.5 for intact MAbs and of 26.8 for F(ab')2 fragments of the porcine MAb. The results showed that heterofusion with this particular protocol can be used to produce swine MAbs of high affinity and specificity for a well-defined tumor marker. These reagents may have an important clinical utility, particularly in patients who became sensitized to mouse immunoglobulins.
 ...
PMID:Swine monoclonal antibodies of high affinity and specificity to carcinoembryonic antigen. 243 34


<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>