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)

Nerve growth factor (NGF) was isolated from the venom of Vipera lebetina and was purified to homogeneity as judged by SDS gel electrophoresis. The biologically active NGF was used to immunize BALB/c mouse, and the spleen cells from immunized mouse were fused with mouse PAI myeloma cells. Forty-seven hybrid cell lines, secreting monoclonal antibodies to V. lebetina NGF, were isolated and nine of them purified from ascitic fluids. The isolated antibodies define two partially overlapping epitopes of the V. lebetina NGF which are not involved in the biological activity of the molecule. Both epitopes are also present on the beta-NGF from the mouse salivary gland and on the NGFs from the following snake venoms: V. lebetina, V, ursini, V, berus berus, Echis carinatus, Bungarus caeruleus, Agkistrodon halys, Naja naja oxiana, Naja naja atra and Naja naja, but not on the bovine seminal plasma NGF. The mol. wts of the NGFs in these snake venoms were determined by Western immunoblot with monoclonal antibodies. The mol. wts of the NGFs from V. ursini (37,000), E. carinatus (36,000, 44,000) and A. halys (29,000) were determined for the first time.
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PMID:Monoclonal antibodies against Vipera lebetina venom nerve growth factor cross-react with other snake venom nerve growth factors. 244 8

The monoclonal antibody to the epidermal growth factor (EGF) receptor was generated after fusion of PAI myeloma cells with immunized BALB/c mouse spleen cells, using intact A431 epidermoid carcinoma cells as an immunogen. The antibody, denoted 5A9, is an IgG, which recognizes a protein with molecular mass 170 kDa during immunoblot analysis, immunoprecipitates phosphoprotein with molecular mass 170 kDa from the membrane preparations of A431 cells, and, according to immunofluorescence experiments, is distributed in the cell similar to the EGF-rhodamine conjugate. It is concluded that the produced antibodies are specific to EGF-receptor. At the same time the 5A9 (50 nM) do not compete with EGF for binding with high and low affinity receptors. They fail to induce internalization of the EGF-receptor and do not exert influence on intracellular degradation of EGF-receptor. Monoclonal antibodies 5A9 are also unable to inhibit the EGF-induced protein kinase activity of the receptor and do not stimulate protein kinase activity by themselves. Thus, the prepared monoclonal antibodies can be used to register the EGF-receptor cellular localization without affecting biologic activity of the receptor.
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PMID:[Isolation and characteristics of monoclonal antibodies to the external domain of the EGF receptor in human A431 epidermoid carcinoma]. 247 49

Fusions were performed between the mouse PAI myeloma cell line and spleen cells from Balb/c mice immunized with intact erythrocytes from 1-day Cornell K-strain White Leghorn chickens. Following single cell cloning, four hybridoma clones were found to secrete erythroid specific monoclonal antibodies. Based on its pattern of reactivity, the antibody (IgG2a, kappa) secreted by clone 10C6 detects a specific avian oncodevelopmental antigen associated with the hematopoietic system: chicken fetal antigen (CFA). Two other clones, designated as 3F12 and 4C2, produced antibodies (IgM, kappa) that recognize another avian developmental antigen: chicken adult antigen (CAA). A fourth clone, 9F9, produced an antibody (IgM, kappa) that reacts with all peripheral erythrocytes from both Japanese quail and chicken regardless of age. Clone 10C6 antibody apparently detects an erythrocyte specific (ES) determinant of CFA associated with determinant #8 while antibodies of clones 3F12 and 4C2 recognize a chicken specific determinant of CAA. Analysis by complement mediated microcytotoxicity indicated that the epitopes detected by 10C6 vs 3F12 and 4C2 antibodies were expressed on erythrocytes in a reciprocal fashion during development. Furthermore, strain variations in the incidence of erythrocytes carrying these epitopes were observed. The usefulness of these monoclonal antibodies for the study of erythroid populations is discussed.
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PMID:Chicken developmental antigens: analysis of erythroid populations with monoclonal antibodies. 405 82

Pyelonephritis-associated P-pili (PAP) of Escherichia coli O6,H(-),K1(-),F12,haemolysin(-) were purified by salt precipitation and affinity chromatography using Synsorb P1. Purified PAP showed a single band with a molecular weight of 18 kDa by electrophoretic analysis. A monoclonal antibody (mAb) was produced by fusion of the PAI myeloma cell line with splenic lymphocytes from BALB/c mice immunised with the purified PAP. The mAb was of IgM class with kappa light chains and reacted with a 18-kDa moeity of the salt precipitate; the epitope was present near the apical part of the pilus filaments. The mAb reacted with PAP in both immunofluorescence and haemagglutination tests when 108 strains isolated from urine samples were tested; the two tests were in agreement for 202 of 204 strains isolated from faecal samples.
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PMID:Production and characterisation of monoclonal antibodies against pyelonephritis-associated P-pili of Escherichia coli. 791 47

The application of immunoassays in pesticide residue analysis is of increasing interest due to the sensitivity, simple handling and fast throughput of samples. For a wide application of these assays, a sufficient supply of standardized antibodies over a long period of time is necessary. The monoclonal antibody technology is solving this problem with an increasing number of cell lines which produce antibodies against different pesticides. Hybridomas were produced by cell fusion of spleen cells from mice immunized with dichloroatrazine conjugated to bovine serum albumin and mouse myeloma cells (PAI-B3 Ag8I). After screening with a competitive enzyme immunoassay, a monoclonal antibody that was specific for terbuthylazine and was produced by a permanent hybridoma cell line was selected for immunoassay development and optimization. For this purpose, an antigen- and antibody-immobilized ELISA technique was improved by varying the test parameters. Comparing both methods, the latter turned out to be superior (50% binding = 0.8 microgram/l, detection limit = 0.14 microgram/l).
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PMID:Optimization of a monoclonal antibody-based enzyme immunoassay for the detection of terbuthylazine. 847 76

Eight species of murine monoclonal antibodies against human ST2 protein, which is highly similar in protein sequence to the interleukin 1 receptor, were produced. The fusion was carried out between the murine myeloma cell line PAI and murine lymph node or spleen cells from mice immunized with the recombinant ST2 protein produced in Escherichia coli. Characterization of these monoclonal antibodies by immunoblot analysis revealed that they all reacted with recombinant, N-glycosylated ST2 protein that was secreted from COS7 cells transiently transfected with a mammalian expression vector carrying ST2 cDNA. The recombinant N-glycosylated ST2 protein could be immunoprecipitated by 5 out of 6 species of the IgG class monoclonal antibodies. Furthermore, these antibodies were also able to detect, by immunofluorescence, the membrane-bound chimeric molecule possessing an extracellular portion of human ST2 and a transmembrane and cytoplasmic portion of murine receptor type ST2L expressed on COS7 cells, indicating that these monoclonal antibodies were useful for detecting the natural membrane-bound ST2 in human cells. Combining immunoprecipitation and immunofluorescence with the aid of these monoclonal antibodies, together with the reverse transcriptase-polymerase chain reaction method, the human leukemic cell line UT-7 was demonstrated to express human ST2 mRNA and protein. The identification of the ST2 gene product in UT-7 cells may help investigators elucidate the function of the human ST2 gene.
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PMID:Studies on natural ST2 gene products in the human leukemic cell line UT-7 using monoclonal antihuman ST2 antibodies. 857 90

Two hybridoma clones have been produced by hybridization of murine myeloma cell line PAI and splenocytes from BALB/c mice immunized with cells from a transplantable sarcoma induced in rat by SR-RSV. The antibody produced by hybridoma clone 2C2 was of subclass IgG3 and recognized a cell surface antigen of 52 kD. It only cross-reacted with cells from SR-RSV-induced sarcoma in hamster, but not with cells from the chicken RSV-induced sarcoma, nor with a number of methylcholanthrene sarcomas and various other tumors of viral or other etiology developed in rats, mouse, hamsters or chickens. The antibody produced by hybridoma clone 5G2 was of subclass IgG2A and recognized an antigen of 28 kD which was located under the plasma membrane, particularly in the cell protrusions and microvilli. Cross-reactions were found with all sarcoma cells tested, indicating that this antigen might represent a common sarcoma antigen of comparatively low molecular mass.
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PMID:Two tumor-associated membrane antigens defined by monoclonal antibodies in a transplantable sarcoma induced by Rous sarcoma virus in rat. 893 54

Human caliciviruses (HuCVs) are classified into the Norwalk-like viruses (NLV) and Sapporo-like viruses (SLV) as genera within the family CALICIVIRIDAE: The NLV genus is further classified into genogroups I and II, based on sequence similarities. To study the antigenic determinants on the HuCV capsid protein and develop new diagnostic tools for field samples, we established and characterized monoclonal antibodies (MAbs) against baculovirus-expressed recombinant HuCV virus-like particles (VLPs). Hybrid clones producing MAbs were obtained from cultures of PAI myeloma cells fused with spleen or mesenteric lymph node cells from mice immunized orally with either a single type of recombinant Norwalk virus (rNV), Kashiwa 47 virus (rKAV), Snow Mountain agent (rSMA), or Sapporo virus (rSV) VLP or with mixtures of two types of VLPs from different genogroups. Twenty MAbs, obtained as mouse ascites, were characterized and classified into six groups according to their enzyme-linked immunosorbent assay (ELISA) and Western blotting (WB) cross-reactivity patterns to VLPs. Five groups of MAbs reacted by both WB and ELISA and were classified as follows: common cross-reactive MAbs for four genogroup I and six genogroup II VLPs (group A), genogroup I-specific MAbs (group B), genogroup II-specific MAbs (group C), and strain-specific MAbs (groups D and E). One MAb group (group F) reacted only by ELISA. The group A MAbs, which showed broad cross-reactivity with VLPs of both NLV genogroups, were obtained from mice immunized orally with a single type of VLP (either rNV or rKAV). Two MAbs, which were obtained from mice immunized with rSV, reacted with rSV but not with any NLV VLP. These are the first MAbs to be reported for any SLV. These strain-, genogroup-, and genus-reactive MAbs will be useful tools for further study of the antigenic and structural topography of the HuCV virion and for diagnostic assays for HuCVs.
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PMID:Cross-reactivity among several recombinant calicivirus virus-like particles (VLPs) with monoclonal antibodies obtained from mice immunized orally with one type of VLP. 1208 62

Sapovirus (SaV), a member of the family Caliciviridae, is an important cause of acute epidemic gastroenteritis in humans. Human SaV is genetically and antigenically diverse and can be classified into four genogroups (GI, GII, GIV, and GV) and 16 genotypes (7 GI [GI.1-7], 7 GII, [GII.1-7], 1 GIV and 1 GV), based on capsid sequence similarities. Monoclonal antibodies (MAbs) are powerful tools for examining viruses and proteins. PAI myeloma cells were fused with spleen cells from mice immunized with a single type of recombinant human SaV virus-like particles (VLPs) (GI.1, GI.5, GI.6, GII.3, GIV, or GV). Sixty-five hybrid clones producing MAbs were obtained. Twenty-four MAbs were characterized by ELISA, according to their cross-reactivity to each VLP (GI.1, GI.5, GI.6, GII.2, GII.3, GII.4, GII.7, GIV, and GV). The MAbs were classified by this method into: (i) MAbs broadly cross-reactive to all GI, GII, GIV and GV strains; (ii) those reactive in a genogroup-specific; and (iii) those reactive in a genotype-specific manner. Further analysis of three broadly cross-reactive MAbs with a competitive ELISA demonstrated that at least two different common epitopes are located on the capsid protein of human SaVs in the four genogroups. The MAbs generated and characterized in this study will be useful tools for further study of the antigenic and structural topography of the human SaV virion and for developing new diagnostic assays for human SaV.
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PMID:Novel monoclonal antibodies broadly reactive to human recombinant sapovirus-like particles. 2292 83