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)

Hybridization of a non-secreting mouse myeloma cell line NSO with splenocytes from a BALB/c mouse hyperimmunized with the anti-CD4 monoclonal antibody (mAb) HP2/6 generated the anti-idiotypic (anti-id) mAb F11-2113, F11-2302 and F11-2444, which recognize idiotope(s) (id) that are the same or spatially close to each other and are located outside the antigen-combining site of the immunizing mAb. Binding and inhibition assay showed that id are not expressed either on other mouse anti-CD4 mAb or polyclonal immunoglobulins (Ig). Western blotting analysis showed that the id defined by anti-id mAb F11-2113, F11-2302 and F11-2444 are similarly expressed on separated heavy and light chains of mAb HP2/6 and suggested they are likely to be 'sequence-dependent' since their expression is conserved following SDS and reducing reagents treatment. This finding is unique inasmuch as 'sequence-dependent' id similarly expressed on heavy and light chains have been described only on a mouse monoclonal auto-antibody with immunoregulatory properties.
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PMID:Anti-idiotypic monoclonal antibodies reacting with idiotope on isolated-denatured chains of an anti-CD4 monoclonal antibody. 178 32

Immunization of BALB/c mice with the mouse anti-CD4 monoclonal antibody (mAb) HP2/6 resulted in the production of anti-idiotypic antibodies. Analysis of the kinetics of the development of anti-idiotypic antibodies showed a homogeneous response among the immunized animals. Cross-blocking assays performed with anti-CD4 mAbs OKT4, OKT4c and OKT4d showed that syngeneic anti-idiotypic antiserum elicited with mAb HP2/6 recognizes idiotope(s) expressed only on the immunizing mAb. The idiotope(s) is (are) located within or closely related to the antigen-combining site of mAb HP2/6. Hybridization with the myeloma cell line NSO of splenocytes from a BALB/c mouse hyperimmunized with mAb HP2/6 generated the anti-idiotypic mAbs F11-2113, F11-2302 and F11-2444 which recognize idiotope(s) outside the antigen-combining site of mAb HP2/6. Although the anti-idiotypic mAbs cross-inhibit each other in their binding to mAb HP2/6, they differ in the ability to elicit anti-anti-idiotypic antisera. Furthermore, mAb F11-2113 enhances CD4 down-regulation in the presence of mAb HP2/6 to a larger extent than mAbs F11-2302 and F11-2444. The latter results suggest an additional mechanism by which anti-idiotypic antibodies may induce functional abnormalities of CD4+ T cells in human immunodeficiency virus-infected T cells.
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PMID:Immunochemical and functional characterization of anti-idiotypic antibodies to a mouse anti-CD4 monoclonal antibody. 181 63

Spleen cells of BALB/c mice immunized with human pulmonary adenocarcinoma cell LTEP-a2 were fused with murine myeloma cell SP 2/0, from which 4 hybridomas (2 A7, 2 E9, 4 F2 and 5 F11) were obtained. Indirect immunofluorescence test showed that these 4 monoclonal antibodies reacted with human lung cancer cells, but not with 2 BS or the lymphocytes and red blood cells in 4 different ABO groups of 10 persons. Using ABC immunoperoxidase stain technique, these 4 antibodies showed negative reaction with 9 tissue types from the normal subject and fetus but could react with 52-83% of the 29 human lung carcinomas and 64-92% of the 24 non-small cell lung cancers (non-SCLC). When 5 F11 was combined with 2 A7 or 2 E9, the percentage of positive stain was 100% in 24 non-SCLC. The results of indirect immunofluorescence stain showed that strong membrane stain by 5 F11 and membrane stain by 4 F2 were obtained, indicating that these antibodies could recognize antigens on cancer cell membrane. It is suggested that a mixture of 5 F11 and other antibodies be useful in the diagnosis and treatment of lung cancer. Molecular weight of the antigens recognized by the 4 antibodies was determined by SDS-PAGE and immunoblot technique to be 47 KD (2 A7), 67 KD (2E9), 40 KD (4F2) and 56 KD (5 F11).
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PMID:[Monoclonal antibody against human lung carcinoma]. 217 66

The Escherichia coli P fimbriae F71, F72, F9, and F11 from four cloned strains were purified, and polyclonal antisera were raised in rabbits. Cross-reactions of these antisera with eight different cloned and purified fimbriae were measured in an enzyme-linked immunosorbent assay. These antisera showed a reaction with the homologous fimbriae and also with most heterologous fimbriae. Monoclonal antibodies (MAbs) directed against the same four native fimbriae were produced by the fusion of spleen cells from immunized BALB/c mice with SP2/0 myeloma cells. The resulting four series of MAbs were also screened in an enzyme-linked immunosorbent assay with eight different cloned and purified fimbriae. Four different F71 hybridomas produced MAbs which recognized only epitopes on F71 fimbriae. Two F72 MAbs recognized epitopes on F72 and F9 fimbriae, whereas another F72 MAb recognized an epitope on only F72 fimbriae. Three MAbs raised against F9 reacted only with epitopes on F9 fimbriae. Six MAbs against F11 fimbriae could be divided into two groups: on the one hand two MAbs recognizing F11, pyelonephritis-associated pilus, Pap, and F72 fimbriae and on the other hand four MAbs recognizing F11 and "Clegg" fimbriae. None of the MAbs reacted with 1A or 1C fimbriae. In a hemagglutination inhibition assay it was shown that none of the MAbs produced inhibited the adhesive properties of homologous cloned strains.
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PMID:Monoclonal antibodies that recognize the P fimbriae F71, F72, F9, and F11 from uropathogenic Escherichia coli. 241 58

We have previously reported that a group of monoclonal antibodies (MAbs) to carcinoembryonic antigen (CEA), designated Group F MAbs, are able to discriminate CEA in tumor tissues from the CEA-related normal antigens and that CEA assay systems utilizing at least one Group F MAb show the improved cancer diagnosis. In this study, we cloned the genes coding for two Group F MAbs (F11-35 and F11-39) and deduced the amino acid sequences of the variable regions for their heavy and light chains. The variable region for the heavy chain of F11-35 contained a possible N-glycosylation site (Asn/Asp/Thr) at amino acid positions 89-91. Then, we constructed two mouse-human chimeric antibodies by using the F11-35 and F11-39 variable region genes of heavy and light chains (VH and V kappa) and human heavy and light chain constant region genes (gamma 1 and kappa) derived from a human plasma cell leukemia line (ARH77). The chimeric gene constructs were sequentially co-transfected into murine non-Ig-producing myeloma (P3-U1) or hybridoma (Sp2/0) cells by electroporation. The resulting chimeric heavy chain of F11-35 showed a slightly but significantly higher molecular weight than that of F11-39, but the molecular weights of their unglycosylated peptides synthesized in the presence of tunicamycin were similar, indicating the glycosylation at the possible N-glycosylation site in the variable region of the Ch F11-35 heavy chain. Both chimeric antibodies exhibited the same specificity and affinity for CEA as those of the parental murine hybridoma antibodies, respectively. Ascites production of Sp2/0 transfectomas is sufficiently high (600-900 micrograms/ml) for initial clinical studies with the chimeric antibodies.
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PMID:Construction and expression of two mouse-human chimeric antibodies with high specificity and affinity for carcinoembryonic antigen. 824 16

Axonal surface glycoproteins, composed of repeated immunoglobulin-like and fibronectin-type-III(FNIII)-like domains, mediate adhesion between axons or between axons and non-neuronal cells or extracellular matrix proteins. Several representatives of this group promote neurite outgrowth, when presented as substratum to neurons in culture, and have been implicated in axonal guidance mechanisms. TAG-1 and axonin-1 are presumptive species homologues of the rat and the chick, respectively; together with F11/F3, they form a subgroup of Ig/FNIII-like molecules containing a glycosyl-PtdIns membrane anchor. Recent reports on tumor suppressor genes encoding Ig-like and FNIII-like sequences prompted us to isolate the human homologue to TAG-1 and axonin-1. Polymerase chain reaction (PCR) primers were designed to regions conserved in both TAG-1 and axonin-1 using deoxyinosine at ambiguous positions. An expected 1000-bp fragment was obtained from cDNA derived from adult human cerebellum. Using this PCR fragment as a probe, several clones were isolated from a human fetal brain cDNA library. Nucleotide sequence analysis of a full-length clone, as expected, revealed a high degree of similarity to rat TAG-1 (91% identity) and chicken axonin-1 (75% identity) at the amino acid level. The encoded protein was then transiently expressed in monkey COS1 cells, and a stable mouse myeloma cell line was established expressing human TAG-1/axonin-1. The transfected COS1 and myeloma cells showed immunoreactivity on the cell surface with polyclonal anti-(chicken axonin-1) serum. On Western blots, the same antibodies recognized the recombinant protein migrating slightly slower on SDS/PAGE than chicken axonin-1. A comparison of chicken and human brain-tissue proteins by Western-blot analysis revealed a similar apparent molecular mass difference between the two species, which might be due to three additional N-glycosylation sites present on human TAG-1/axonin-1. Immunostaining of cryostat sections of embryonic retinas with polyclonal anti-(axonin-1) serum showed similar expression patterns in chicken and human samples at corresponding developmental stages. An additional shared feature of human TAG-1/axonin-1, rat TAG-1 and chick axonin-1 is their attachment to the cell membrane with a glycosyl-PtdIns anchor.
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PMID:cDNA cloning, structural features, and eucaryotic expression of human TAG-1/axonin-1. 842 42

Abstract Mammalian target of rapamycin (mTOR) is a serine/threonine kinase that plays a critical role in the regulation of basic cellular functions, including cellular growth and proliferation. In this study we describe the generation and characterization of novel monoclonal antibodies directed against mTOR protein kinase. A GST-tagged fragment of mTOR expressed in bacteria was used as an antigen. Antibody-producing hybridoma cells were obtained by fusing SP2/0 myeloma cells with splenocytes from immunized mice. Anti-mTOR antibody-producing hybridoma cell lines were first identified by enzyme-linked immunosorbent assay and then subcloned by limiting dilution. Antibodies produced by selected clones were further tested for their reactivity towards the GST/mTOR 1334-1504 recombinant protein. Furthermore, antibody produced by F11 clone was shown to recognize specifically mTOR in different tissues and cell lines in Western blotting, immunoprecipitation, and immunohistochemistry. In addition, mTOR F11 antibody was suitable for immunoprecipitating and testing mTOR activity in in vitro kinase assay. In summary, generated antibodies will be useful for investigating mTOR signaling complexes in normal and pathological states.
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PMID:Generation and characterization of monoclonal antibodies to mTOR kinase. 1880 7

We newly cloned the gene encoding the human aspartyl (asparaginyl) beta-hydroxylase (HAAH) from the surgical tissue of a patient with hepatocellular carcinoma. This study was designed to generate HAAH-specific monoclonal antibody (MAb) for further exploration of its structure and function. Mice were co-immunized with naked plasmid DNA containing N-terminal domain of encoding HAAH gene and recombinant HAAH polypeptide. Hybridomas were developed by the electrofusion of the splenocytes from mice immunized with plasmid DNA to Sp2/0 myeloma cells in vitro. Three hybridoma cell lines (designated G3, G9, and F11, respectively) stably secreting HAAH-specific MAbs were obtained. The specificity and sensitivity of MAbs were assessed by indirect enzyme-linked immunosorbent assay (ELISA) and Western blot analysis. Results showed that the three MAbs belong to IgG1 kappa isotype, the titer of MAbs reached was 5 x 10(4) - 1 x 10(5), and the affinity constant (k(aff)) of MAbs ranged between 2.5 x 10(8) - 1.1 x 10(9). MAb G3 was preliminarily applied to detection expression of HAAH for seven tumor tissues, including hepatocellular carcinoma, lung cancer, kidney cancer, cholangiocarcinoma, prostate cancer, breast cancer, and glioblastoma by immunohistochemical stain. Our studies demonstrated that co-immunization of naked DNA containing encoding gene of target antigen and recombinant target protein, and combined with in vitro electrofusion, is an effective and simple method to raise MAbs.
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PMID:Monoclonal antibodies against human aspartyl (asparaginyl) beta-hydroxylase developed by DNA immunization. 1966 97