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)

Splenocytes from mice immunized either with bradykinin conjugated with carbodiimide to keyhole limpet hemocyanin or ovalbumin were fused using polyethylene glycol with the mouse myeloma cell line SP2/o. Nine monoclonal antibodies reactive with kinins were obtained from two fusions. All of the antibodies were of the IgG1k isotype, except for one, which was an IgG2ak. Based on their reactivities with biologically active kinins and biologically inactive degradation products, the antibodies were separated into three groups. The first group, which had the highest affinities for bradykinin, displayed about equal reactivities for bradykinin and des-Arg9-bradykinin, but little reactivities for the kinin fragments, des-Arg1-bradykinin and des-Phe8-Arg9-bradykinin, or for lysyl-bradykinin and methionyl-lysyl-bradykinin. The second group was similar to the first except that it showed about a 2.5- to 3.5-fold greater reactivity for des-Arg9-bradykinin than for bradykinin. The third group, which had the lowest affinities for bradykinin [50% inhibition of antibody binding to an enzyme-linked immunosorbent assay (ELISA) plate occurring with bradykinin concentrations ranging from about 8 to 39 nM], showed little reactivities with des-Arg1-bradykinin, des-Arg9-bradykinin and des-Phe8-Arg9-bradykinin, but 50-100% cross-reactivities with lysyl-bradykinin and methionyl-lysyl-bradykinin. The useful ranges for bradykinin detection (ng/well, 50 microL assay volume) using the highest affinity antibody in each group in ELISAs were: 0.01 to 0.5, 0.03 to 3, and 0.1 to 3 for groups 1, 2, and 3, respectively.
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PMID:Enzyme-linked immunosorbent assays for kinins using high-affinity monoclonal kinin antibodies. 237 67

The present study is designed to investigate the regulatory effect of mammalian erythroblasts, prior to naturally-occurring denucleation, on malignancy of mouse plasmocytoma cells and the possibility of reactivation of the pyknotic late erythroblast nuclei in hybrid cells crossed between rat intermediate or late erythroblasts of 15-day Wistar rat embryonic livers, and mouse plasmocytoma (SP2/O) cell lines. Results indicated that: (i) Suppression of tumorigenicity and reversion of the malignant phenotype were observed in hybrid cells in a similar way as those of cybrid cells crossed between reticulocytes and myeloma cells as we reported previously, thus providing further evidence to support the hypothesis that some regulatory substances already existed in mammalian intermediate and late erythroblasts long before nuclear extrusion. (ii) Appearance of positive histochemical reaction for hemoglobins in cytoplasm and electrophoretic bands of rat and mouse globin chains in hybrid cell lysate were identified. The transcripts of mouse globin genes could be readily detected by nucleic acid hybridization technique with mouse beta-globin gene probes. (iii) Reassuming of rat chromosome and globin gene products synthesis in hybrid cell indicates that the originally pyknotic nuclei of late erythroblasts could be reactivated to assume functional activity after cell hybridization. The mechanism of regulatory effect and its possible relation to naturally occurring denucleation in developing mammalian red blood cells were discussed.
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PMID:Studies on the cell phenotype characteristics of hybrid cells crossed between rat nucleated erythroblasts and mouse plasmocytoma (SP2/O) cell line. 239 Jan 64

Three McAb were produced against an outer envelope preparation from Leptospira, interrogans, serovar Lai by fusion of SP2/0 myeloma cells with immune BALB/c mice spleen cells. The fusion rate was 96% and the antibody positive rate was 50%. One of the hybridomas, E4B11C9, reacted with 13 of the 13 serovars of the Icterohaemorrhagiae serogroup in microscopic agglutination test (MAT) but did not react with the 18 representative serovars of L. interrogans and L. biflexa serovar patoc and Leptonema illini. For all non-reactive serovars the MAT titres were greater than 1:25. The McAb, E4B7G5, reacted similarly with all serovars except smithi and tonkini. E4B7D4 reacted also similarly with all serovars except serovars birkini, ndambari, bogvere, smithi and tonkini. Therefore, 3 McAb showed serogroup specificity and partial serogroup specificity by agglutination. The agglutination titres were high and hybridomas were stable, so it might be useful in providing a simple, rapid method for the classification and identification of clinical isolates such as pathogenic L. interrogans in place of the complicated and time-consuming conventional methods.
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PMID:[Study on the characteristics of agglutination reaction of McAb with Leptospira interrogans outer envelope]. 239 Oct 93

We had demonstrated that the NK cell mediated cytotoxicity of murine spleen cells could be augmented by in vivo priming and subsequent in vitro challenge with a streptococcal preparation OK432, and the cell surface phenotype of induced killer cells was Thy-1+, asialo GM1+, suggesting that the activated cells were of NK lineage (OK-NK cell). We had also clarified that IL-2 played a major role in inducing the OK-NK cells via the production of IFN-gamma. In this study, we examined the effect of adoptive transfer of OK-NK cells on syngeneic tumors in mice. Mice were implanted with SP2 myeloma cells intraperitoneally (i.p.), or C26 colon adenocarcinoma cells subcutaneously to make the models of peritonitis carcinomatosa or solid tumor, and the OK-NK cells were transferred i.p. or intratumorally, adoptively. By the adoptive transfer of OK-NK cells, 92% of mice bearing SP2-tumor had be cured. The tumor growth of C26-solid tumor was inhibited, and the survival rate of mice bearing C26-tumor was significantly increased. The intratumoral remnants of 125I-labelled OK-NK cells were 61, 27 and 8% at 4, 12 and 36h after intratumoral transfer, respectively. By multiple transfer of OK-NK cells, the antitumor effect was more effectively augmented than that of a single transfer. Results in this study suggested that OK-NK cells could be useful for the therapy of cancer patients.
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PMID:Successful adoptive immunotherapy with OK432-inducible activated natural killer cells in tumor-bearing mice. 240 Jun 28

Gamma seminoprotein (gamma Sm), a glycoprotein isolated from human seminal plasma with a molecular weight of 29,000 and possibly a serine protease, has been demonstrated to be one of the prostate organ-specific antigens. We established a murine monoclonal antibody (MoAb) to gamma-Sm in order to prove the presence and localization of this protein in the prostate. The hybrid clones were obtained by fusing mouse SP2/O-Ag-14 myeloma cells with splenocytes from Balb/c mouse immunized with the major fractions of gamma-Sm. The enzyme-linked immunosorbent assay was done for antibody screening. After cloning twice in soft agarose, the stable clone, termed 43-21-1-1, was finally chosen. This MoAb, IgG1(kappa), recognized gamma-Sm specifically, which was verified by an immunoblotting assay. The specificity of the MoAb was further evaluated by immunohistochemical study by the avidin biotin complex method. Periodate-lysine-paraformaldehyde-fixed surgical specimens, including the prostate associated with fibromuscular hyperplasia, seminal vesicles, bladder, testis and epididymis, were examined. Formaldehyde (10%)-fixed surgical specimens from patients with adenocarcinoma of the prostate and primary transitional cell carcinoma arising from the periurethral prostatic ducts were also examined. Positive reactions of gamma-Sm were recognized only in the cytoplasm of prostatic glandular epithelial cells and along the luminal surface. Fibrous and muscular tissues always given negative staining. Neither nonprostatic tissues nor transitional cell carcinoma of the prostate were stained positively for gamma-Sm. These results show that this MoAb (43-21-1-1) is quite specific to gamma-Sm and may be useful for the immunohistochemical study with prostatic tissue.
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PMID:[Preparation and characterization of monoclonal antibody to gamma seminoprotein]. 240 88

Twenty-nine independent hybridomas producing monoclonal antibodies to the matrix (M) protein of vesicular stomatitis virus (Indiana serotype) were prepared by fusion of SP2/0 myeloma cells with spleen lymphocytes obtained from BALB/c mice which had been immunized with the purified M protein. The specific reactivity of each monoclonal antibody was determined by an enzyme-linked immunosorbent assay and a competitive binding assay. Most of the antibodies were of the immunoglobulin G2a and G2b isotypes, although some were immunoglobulin M. By measuring the competitive binding of 125I-antibody, we identified four antigenic determinants in the M protein of the virus; two of these determinants, however, exhibited a large degree of overlap. Western blot analysis revealed little or no cross-reactivity of the antibodies with other viral proteins or with the M protein of the New Jersey serotype. Prolonged trypsin proteolysis removed the first 43 amino acids from the amino-terminal region of the M protein, but it retained its reactivity with monoclonal antibodies to each epitope, except for diminished reactivity with one. To aid in future mapping of these epitopes, we inserted a cDNA clone of the mRNA encoding the M protein of vesicular stomatitis virus into an inducible lac expression vector; the M protein produced in the JM103 strain of Escherichia coli under induced conditions was found to be approximately the same size as native M protein and was recognized by the monoclonal antibodies. These monoclonal antibodies and the cDNA clone should be useful for studying the role of M protein in virus maturation and the regulation of viral transcription.
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PMID:Monoclonal antibodies to the M protein of vesicular stomatitis virus (Indiana serotype) and to a cDNA M gene expression product. 241 Jun 27

Tyrosinase (EC 1.14.18.1) is the enzyme essential to pigment formation in mammals; this enzyme is specifically localized in melanocytes, which occur primarily in the skin, hair bulbs, and eyes. Three hybridomas, TMH-1, TMH-2, and TMH-3, which produce monoclonal antibodies directed against tyrosinase, were obtained by fusion of SP2/0 myeloma cells and lymphocytes of rats hyperimmunized with purified melanosomal tyrosinase. These three monoclonal antibodies bound specifically to the mature, T4 form of tyrosinase, and did not bind to either of the precursor forms (T1 or T2) of the enzyme, which demonstrates that further posttranslational modifications of this enzyme occur which had not previously been detected. Epitope mapping studies have shown that at least two different immunologic determinants on tyrosinase are recognized by these antibodies. All three antibodies showed positive immunofluorescence staining of pigmented murine melanocytes from various sources, including B16 melanoma growing in vivo and in vitro, epidermal melanocytes, and retinal melanocytes. The antibodies did not cross-react with unpigmented cells, including K1735 amelanotic melanoma cells, albino murine skin or eye tissue, fibrosarcoma cells, rat fibroblasts, or epidermal keratinocytes. These monoclonal antibodies are sensitive, highly specific probes for pigmented mammalian melanocytes.
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PMID:Anti-T4-tyrosinase monoclonal antibodies--specific markers for pigmented melanocytes. 241 67

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

Monoclonal antibodies against human prostatic acid phosphatase (PAPase) were produced by immunization of human primary spleen cell cultures. Dissociated spleen cells were cultured for 5-8 days in the presence of 100 ng/ml of PAPase and pokeweed mitogen (1:5000). Following immunization, B cells were isolated and infected with Epstein-Barr virus (EBV). Two weeks after EBV-transformation, cells were fused with either mouse myeloma cells (SP2/OAg14) or human/mouse heteromyeloma cells (SHM-D33). Hybrid clones were screened for anti-PAPase production. In 7 independent immunizations, the average fusion frequency was 3.6 per 10(6) lymphocytes. 18-32% of the hybridomas produced anti-PAPase; approximately 75% of these secreted IgM and 25% secreted IgG. Antibody specificity was determined by immunoassay and immunohistological studies. The procedures described here may be suitable for the production of human monoclonal antibody of a useful specificity.
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PMID:Production of monoclonal antibodies against prostatic acid phosphatase by in vitro immunization of human spleen cells. 241 32

We have developed a murine hybridoma cell line that secretes a monoclonal antibody directed to the serum human vitamin D binding protein (hDBP), a 58,000-dalton alpha-globulin with a high avidity for 25-hydroxycholecalciferol and globular actin. This immunoglobulin G1 kappa-light chain antibody was produced by the fusion of the spleen cells from BALB/c mice, immunized with purified hDBP, with SP2/0-AG4 myeloma cells. The antibody was easily removed from the supernatant of hybridoma cultures or mouse ascites fluid by Protein A affinity chromatography. Apparent serum monospecificity was demonstrated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and isoelectric focusing gels transblotted to nylon membranes and overlayed with purified MAK 89 antibody and radioiodinated Protein A. The affinity of the antibody is high [dissociation constant (Kd) = 2.6 X 10(-11) M]. Parallel displacement of tracer by hDBP and human serum was observed. The sera from various species displaced the hDBP tracer in the following potency: monkey more than cat more than dog more than guinea pig. RIAs for DBP from several species are feasible with this antibody. This antibody does not, in contrast to polyclonal anti-hDBP antiserum, bind to viable monocytes. However, the MAK 89 antibody does bind to the membranes of well washed, fixed, and permeant circulating monocytes. Surface membrane radioiodination of monocytes and immunoprecipitation of the detergent lysates with the antibody demonstrates a protein with molecular weight equivalent to hDBP. The epitope recognized, therefore, appears to be hidden in the viable cells, suggesting an intimate and intricate association of the hDBP and monocyte plasma membrane.
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PMID:Characterization of a monoclonal antibody to human serum vitamin D binding protein (Gc globulin): recognition of an epitope hidden in membranes of circulating monocytes. 242 47


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