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)

Hybrid cell lines were prepared by the fusion of BALB/c myeloma NS-1 cells with the lymphocytes of BALB/c mice that were immunized with partially purified androgen receptor (AR) from human prostates. One of the clones, 5F4, was chosen for detailed specificity analysis. The avidin-biotin-peroxidase complex (ABC) procedure was used for immunohistochemical staining of the 5F4 monoclonal antibody. In human benign prostatic hypertrophy (BPH) tissues, cytoplasm and nuclei were stained. Of 16 prostatic cancer tissues, 2 were composed of AR-positive cells exclusively, 7 were composed of AR-negative cells, and 7 contained both AR-positive cells and AR-negative cells (mixed). Of nine cases that were AR-positive or mixed, seven cases responded to the hormone therapy, and two were not determined for responsiveness because the patients died early of other diseases. Of seven AR-negative cases, all but one inestimable case had no response to the hormone therapy. Immunohistochemical analysis of AR by using the monoclonal antibody 5F4, was a useful tool for determining androgen dependency of prostatic cancers.
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PMID:Establishment of monoclonal antibody to human androgen receptor and its clinical application for prostatic cancers. 246 71

We have made monoclonal antiidiotypic antibodies (Ab2) relating to the p97 antigen of human melanoma. This was accomplished by immunizing BALB/c mice with 96.5, a monoclonal antibody (MAb) specific for epitope p97a, hybridizing their spleen cells with NS-1 myeloma cells, and selecting for hybridomas making antibody binding to Fab fragments prepared from MAb 96.5 (Fab 96.5). The Ab2 were tested for binding to Fab 96.5, as well as for their ability to inhibit the binding between MAb 96.5 and p97. Three monoclonal Ab2 were identified which competitively inhibited the binding between p97 and MAb 96.5 when injected into either BALB/c or C3H/HeN mice; two of them induced Ab3 which expressed the same idiotype as MAb 96.5 and which were specific for p97. These two Ab2 thus appear to functionally mimic p97. They were, however, unable to induce delayed-type hypersensitivity to p97 and to protect mice against transplants of p97-positive mouse melanoma cells, suggesting that the epitope recognized by MAb 96.5 may not be a target for cell-mediated rejection of tumors.
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PMID:Monoclonal antiidiotypic antibodies related to the p97 human melanoma antigen. 247 May 2

A new monoclonal antibody, 1C5, was produced by fusion of spleen cells obtained from mice immunized with CAC-1, a human cell line of cervical adenocarcinoma of the uterus, and NS-1 myeloma cell. The objectives of this study were to obtain moAb that can be used for routine histology and cytology, and to examine the histogenesis of cervical adenocarcinoma. 1. 1C5 reacted with 88% of cervical adenocarcinoma of the uterus, but did not react with cervical squamous cell carcinoma of the uterus and other squamous cell carcinoma. However, 1C5 reacted with some adenocarcinomas, such as endometrial carcinoma of the uterus and ovarial carcinoma. 2. The staining pattern by 1C5 was different, in cervical adenocarcinoma from that in endometrial carcinoma of the uterus, and also different in the endocervical type from that in the endometrioid type of cervical adenocarcinoma. Therefore, 1C5 is useful in distinguishing between two types of adenocarcinoma of the uterus. 3. 1C5 did not react with normal squamous cells or normal columnar cells of the uterine cervix, or with normal endometrial cells of the uterus. However, the columnar cells in a limited area of the squamocolumnar junction were strongly stained with 1C5. 4. 1C5 reacted with ethanol-fixed, and routine formalin-fixed and paraffin-embedded tissue. Thus, 1C5 may be used for clinical diagnosis. 5. 1C5 was found to be IgG1. 6. The molecular weight of the 1C5-defined antigen was 26,000 daltons, and the epitope of the 1C5-defined antigen was carbohydrate moiety. 7. We examined the histogenesis of cervical adenocarcinoma of the uterus by utilizing the reactivity of 1C5.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:[The production and characterization of monoclonal antibody, 1C5, reactive with cervical adenocarcinoma of the uterus]. 247 40

By comparison, it was shown that ascaris protein as carrier was far more effective than BSA and mouse serum albumin to make human c-peptide (HCP) immunogenicity in mice. Twelve monoclonal antibodies (McAb) were obtained after fusion of NS-1 myeloma cells with spleen cells from two BALB/c mice immunized with HCP-ascaris protein conjugate. Eight McAb were characterized and all of them were of IgG1 subclass. Affinities of the McAb for HCP were in the range of 0.03-0.85 X 10(9) mol-1. Although all 8 McAb reacted with both HCP and human proinsulin (HPI), they could specifically recognize human insulin from HPI and were highly species specific without cross-reaction with proinsulin, insulin and c-peptide of other species tested. Through analysis of binding with different HCP fragments, their antigenic determinants were located at either N or C terminal of HCP. The results of plasma HCP radioimmunoassay in 20 normal fasting human adults showed that the value (0.47 +/- 0.16 pmol/ml) determined by rabbit PcAb (R2303) against BSA-HCP was significantly higher than that (0.29 +/- 0.13 pmol/ml) determined by McAb-1.
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PMID:[Studies on monoclonal antibodies directed against human C-peptide]. 247 69

The 78,000-dalton glucose-regulated protein (GRP78) is a stress-inducible protein localized in the endoplasmic reticulum. It has been identified as the immunoglobulin heavy-chain-binding protein. We report here a high level of GRP78 expression in a B-cell myeloma line, NS-1, which produces only kappa light-chain proteins but is unable to secrete them. GRP78 transcription was enhanced in NS-1 cells, resulting in higher levels of GRP78 mRNA and protein than in non-immunoglobulin-producing cells. Furthermore, the nonsecreted light chains in NS-1 cells were found in specific association with GRP78. We hypothesize that in nonsecreting lymphoid cells, the presence of free, unassembled light chains in the endoplasmic reticulum could result in increased transcription of the GRP78 gene and that GRP78 can also bind to immunoglobulin light chains.
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PMID:Enhanced transcription of the 78,000-dalton glucose-regulated protein (GRP78) gene and association of GRP78 with immunoglobulin light chains in a nonsecreting B-cell myeloma line (NS-1). 250 63

The sodium channel blocker, tetrodotoxin (TDT), was conjugated to keyhole limpet hemocyanin (KLH) and used to immunize BALB/c mice. Anti-TDT antibodies were detected in serum by ELISA and reached stable levels 4-5 wk after the first immunization. Spleens from immunized mice were fused with NS-1 mouse myeloma cells and approximately 9,329 resultant hybrids were screened by ELISA for reactivity to TDT. Two stable hybrids were isolated, subcloned, and characterized. These hybrids, termed TD13a1 and TD2C5, secreted specific anti-TDT antibodies that recognized TDT but not the related sodium channel blocker, saxitoxin (STX), as determined by competition ELISA. Both antibodies were of the IgG1k subclass with Ka's approaching 10(7) M-1. The inhibitory ability of these antibodies was tested by a competitive displacement assay for [3H]STX on rat brain membranes. Both antibodies strongly inhibited TDT binding to membranes. A nanomole of TD2C5 was able to bind approximately 1.8 nmol of TDT, whereas a comparable amount of TD13a1 bound half as much. Furthermore, TD2C5 was able to protect against TDT-induced reduction of peripheral nerve action potentials in rat tibial nerve when administered in situ. These antibodies thus represent potentially useful reagents for neurobiologic research, detection of toxin contamination and diagnosis of poisoning, and may provide protection against the toxicity of TDT in vivo.
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PMID:Protection against nerve toxicity by monoclonal antibodies to the sodium channel blocker tetrodotoxin. 254 73

The sodium channel blocker saxitoxin (STX) was conjugated to keyhole limpet hemocyanin (KLH) and used to immunize BALB/c mice. Anti-STX antibodies were detected in serum by an enzyme-linked immunosorbent assay (ELISA) within a week or two after the first immunization. Spleens from immunized mice were fused with NS-1 myeloma cells and approximately 7000 resultant hybrids were screened by ELISA for reactivity to STX. Two stable hybrids were isolated, subcloned, and characterized. These hybrids, termed S1A5 and S3E.2, secreted specific anti-STX antibodies that did not recognize the closely related toxin tetrodotoxin (TDT), as determined by competition ELISA. The S1A5 monoclonal antibody (mAb) was of the IgMk class and S3E.2 of the IgG1k subclass with affinity constants (Ka values) of approximately 10(6) M-1. The protective ability of these antibodies was tested by a competitive displacement assay for [3H]STX binding on rat brain membranes. Purified S3E.2 strongly displaced [3H]STX binding, whereas S1A5 weakly inhibited [3H]STX binding to membranes. One nanomole of S3E.2 or S1A5 was able to bind 0.03 nmol or 0.005 nmol, respectively, of STX. The S3E.2 mAb offered partial protection against STX-induced reduction of peripheral nerve action potential in rat tibial nerve when administered in situ at concentrations 10- to 30-fold greater than STX. The S1A5 mAb, despite its ability to inhibit STX binding in vitro, was completely ineffectual in situ. These antibodies, particularly S3E.2, thus represent potentially useful reagents for neurobiologic research, detection of toxin contamination, and diagnosis of poisoning, and may provide protection against the toxicity of STX in vivo.
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PMID:In vitro and in situ inhibition of the sodium channel blocker saxitoxin by monoclonal antibodies. 254 81

A Balb/c mouse was immunized with chick synaptic plasma membranes and monoclonal antibodies were produced by fusion of spleen cells with NS-1 mouse myeloma cells. One antibody, MAC-L1, immunoprecipitated more than 90% of the [3H]PN200-110-labeled calcium channels but only 20% of the omega -conotoxin receptor solubilized from the chick brain membranes. Thus possibly, a certain portion of the omega -conotoxin receptor in the chick brain is a dihydropyridine-sensitive calcium channel. By the specific immunoprecipitation of 125I-labeled proteins, two large polypeptides of 193kDa and 130kDa under reducing conditions were identified as the major components of the calcium channel.
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PMID:Identification of a dihydropyridine-sensitive calcium channel in chick brain by a monoclonal antibody. 255 Dec 70

Monoclonal antibodies were generated to antigens on human foreskin keratinocytes to identify epithelial-specific molecules. Spleen cells from BALB/c mice, immunized with membrane preparations from primary explants of foreskin epithelial cells, were fused with the NS-1 mouse myeloma line. Hybridoma supernatants were screened for the desired immunological reactivity using enzyme-linked immunosorbant binding assays. Hybridomas secreting antibodies reacting with epithelial cells, but not fibroblasts or lymphocytes, were cloned by limiting dilution, and two stable clones producing immunoglobulin M K antibodies were selected for study. Evaluation of fixed paraffin-embedded human tissue by an indirect immunoperoxidase technique revealed that the antibodies bound most strongly to normal stratified squamous and transitional epithelium, and squamous and transitional cell carcinomas. Antibodies from the cloned hybridomas also reacted with primary cell cultures of foreskin keratinocytes, pulmonary epithelium, fetal liver, and amnion cells, but not with primary cultures of nonepithelial cells. Further testing by enzyme-linked immunosorbent assays revealed that the antibodies reacted with some long-term cell lines derived from epithelial tumors. Nonepithelial cell lines were not stained by the antibodies. Indirect immunofluorescent studies indicated that staining was confined to the cell surface. These antibodies may prove useful in studies of differentiation markers of human epithelial cells.
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PMID:Isolation and characterization of a monoclonal antibody specific for epithelial cells. 257 8

Monoclonal antibodies were generated by immunizing rats with mouse bladder carcinomas, fusing their spleen cells with NS-1 myeloma cells and selecting for antibodies that bound to mouse bladder carcinomas. One of the antibodies, IG5, recognizes an antigenic determinant which is present in mouse bladder carcinoma cytoskeletons and is not detectable in the normal bladder epithelium. Indirect immunofluorescence studies revealed that the antigen is expressed intracellularly and is organized in the form of filamentous arrays. The antigen was detected by peroxidase--antiperoxidase immunocytochemistry in stratified epithelia and glands derived from these, but has not been observed in any tissues of mesenchymal or neuronal origin. Various normal and neoplastic human tissues were subsequently tested for reactivity with antibody IG5. Antigen expression in normal tissues was similar to that in the mouse. Most carcinomas of the bladder and lung were stained, while all of eleven colon carcinomas were negative. Antibody IG5 immunoprecipitated radio-iodinated peptides of 58, 56, 52 and 43 kD molecular weight from mouse bladder carcinomas. Western blotting experiments with antibody IG5 demonstrated bands of 56 and 50 kD in a keratin-enriched fraction of the bladder carcinoma cytoskeleton. Antibody IG5 reacted with molecules which have several properties typical of cytoskeletal keratin peptides. Our findings are discussed in the context of previously described keratin peptides and relevant monoclonal antibodies.
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PMID:A monoclonal antibody recognizing cytoskeletal keratins of stratified epithelia and bladder carcinomas. 257 32


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