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)

A rapid and efficient procedure for isolating homogeneous beef liver phenylalanyl-tRNA synthetase (EC.6.1.1) was developed that enables to purify the enzyme 5000 fold and to achieve the activity of 8 e.a.u. per mg of protein. The molecular mass of the native enzyme was estimated to be 260 kDa, for alpha subunit - 59 kDa, and for beta - 72 kDa. Two cellular clones were derived by means of hybridization of immunised splenocytes with myeloma cells. They secrete monoclonal antibodies, designated P6 and P1 2, that bind to human placental and bovine liver phenylalanyl-tRNA synthetases but not to the same enzymes from E. coli and T. thermophilus. P6 and P1 2 antibodies do not affect the aminoacylation capacity of human or bovine phenylalanyl-tRNA synthetases. By immunoblotting, it was shown that P6 antibodies recognize the alpha subunit of the enzyme.
Mol Biol (Mosk)
PMID:[Express method of isolation of mammalian phenylalanine-tRNA-synthetase and preparation of monoclonal antibodies against this enzyme]. 220 92

Murine monoclonal antibodies against human/rat corticotrophin-releasing factor-41 (CRF-41) were produced and characterized for use in the immunological and biological characterization of CRF-41. Spleen cells from BALB/c mice immunized with CRF-41 conjugated to bovine gamma-globulin were fused with a BALB/c-derived non-secretor X-63 myeloma line. Hybridomas were selected for CRF antibody production by enzyme-linked immunosorbent assay, and positive hybridomas cloned twice. Three monoclonal antibodies were obtained (KCHMB001, KCHMB002 and KCHMB003) and characterized as IgG1, IgG1 and IgG2a isotypes respectively, with affinity constants for rat CRF-41 of 30, 53 and 34 nmol/l respectively. All three monoclonal antibodies recognize an epitope contained between residues 34 and 41 of the human/rat sequence. The antibodies were able to neutralize the ACTH-releasing activity of rat CRF-41, applied to rat pituitary fragments in vitro, in a dose-dependent manner. Isoelectric focusing showed that KCHMB003 detected bands of synthetic rat CRF-41 and rat [Met(O)21,38]-CRF-41 at pH 7.1 and 6.8 respectively. Use of KCHMB003 in a two-site enzyme-amplified immunoassay showed that this antibody recognizes both synthetic rat CRF-41 and immunoreactive CRF-41 in rat hypothalamic tissue extracts.
J Mol Endocrinol 1990 Oct
PMID:Production and utilization of monoclonal antibodies to human/rat corticotrophin-releasing factor-41. 224 88

Recently, the failure of interleukin 4 (IL4) autocrine growing CT4S cells to grow in vivo has been demonstrated. Because it could not be excluded that the cells produce insufficient amounts of IL4 to support their growth in vivo, subclones were established which are unresponsive to exogenous IL4 and therefore have acquired full growth autonomy. From the fact that the subclones likewise did not give rise to tumors when injected into nude mice, one may conclude that the IL4 production of autocrine growing CT4S prevents their growth in vivo. To test this hypothesis, a retroviral vector containing the IL4 gene under the control of the immunoglobulin heavy chain (Igh) enhancer/promoter was constructed and used to infect the myeloma cell line J558L. An IL4 producing clone was established (J558L-XEPIL4) and the tumor progression in comparison to the parental clone J558L was monitored in nude mice. The IL4 production significantly delayed the growth of J558L-XEPIL4 in vivo. Tumor suppression was much more evident when J558L-XEPIL4 cells were injected into syngeneic BALB/c mice. These results may explain why autocrine growing CT4S do not grow in vivo and suggest the involvement of functional T lymphocytes in the effectiveness of the host dependent anti-tumor action of IL4.
Mol Immunol 1990 Dec
PMID:Lack of tumorigenicity of interleukin 4 autocrine growing cells seems related to the anti-tumor function of interleukin 4. 227 62

Murine myeloma cell lines are noted for the instability of their immunoglobulin genes and the production of nonsynthesizing variants. In this study, the synthesizing line P3-X63-Ag8 (P3) and its nonsynthesizing subline X63-Ag8-653 (653) were karyotyped and rearrangements of the immunoglobulin carrying chromosomes were investigated. Loss of immunoglobulin synthesis was associated with a reduction in the number of immunoglobulin-carrying chromosomes. When these findings were analyzed in light of published molecular data, it appeared that loss of immunoglobulin synthesis in 653 probably occurred as a result of immunoglobulin gene loss. An unusual finding was the absence of the t(12;15) chromosome in both P3 and 653 cell lines. It was concluded that the t(12;15) chromosome, carried by MOPC 21, has evolved into an unrecognizable form.
Somat Cell Mol Genet 1990 Jan
PMID:Chromosomal evolution in secretory and nonsecretory subline of MOPC 21. 230 43

The major aim of this study was to further investigate the fine specificity of myeloma proteins recognizing epitopes on fructans. Our studies showed that UPC 61, EPC 109, and a hybrid antibody composed of the heavy chain from UPC 61 and the light chain from EPC 109, UPC 61H:EPC 109L, not only bind to inulin which is a linear fructan of beta (2----1) fructofuranosyl linkages, but also bind to sinistrin, a branched molecule consisting of a beta (2----1) fructofuranosyl backbone with beta (2----6) branch points. The fine binding specificity of these three antibodies for the beta (2----1) fructofuranosyl linkages found in inulin-BSA can be further studied by their binding to fructan oligosaccharides isolated from asparagus roots. From a comparative analysis of the amino acid sequences and the apparent affinity constants (aKa) of UPC 61, EPC 109, and the hybrid for various fructan oligosaccharides, it appears that the light chain of the immunoglobulin molecule makes an important contribution to the binding specificity. Finally we report for the first time that a monoclonal antibody specific for beta (2----6) fructans can also bind specifically to inulin-BSA with a lower affinity. This antibody derives its VH and VL from the VHX24 and Vk10b gene families, respectively, which are different from the gene families utilized by UPC 61 and EPC 109 (VHJ606 and Vk11 gene families).
Mol Immunol 1990 Apr
PMID:Binding specificities of inulin-binding immunoglobulins for sinistrin and oligosaccharides isolated from asparagus roots. 235 13

alpha 1-Microglobulin (alpha lm), a glycoprotein heterogeneous in charge, was reported to occur both as a 31-kilodalton (kd) monomer [low mol. wt alpha lm (LMW-alpha lm)] and as polymers or complexes formed with other plasma proteins including IgA [high mol. wt alpha lm (HMW-alpha lm)]. The present study was designed to characterize HMW-alpha lm in normal human serum and in myeloma sera. The following sera were selected: five IgG, 16 IgA and four Bence-Jones protein myelomas. alpha lm was identified by specific monoclonal antibodies in competitive radioimmunoassay and solid-phase ELISA. HMW-alpha lm was found to be associated almost exclusively with monomeric IgA and possibly in very small proportion with dimeric IgA. Ever in cases of predominantly dimeric IgA myelomas, alpha lm was associated with the monomeric form of the monoclonal IgA. The molar ratio of HMW-alpha lm to monomeric IgA never exceeded 3.5% and it was estimated to range from 0.5 to 1.4% in normal serum. No association with other proteins than IgA and no alpha lm polymers were found in IgA myeloma. Two types of HMW-alpha lm-IgA complexes were found: (a) those that were dissociable into IgA and LMW-alpha lm after mild reduction, and (b) those which were dissociated only after complete reduction of the complexes into IgA and an 88-90-kd component bearing alpha lm but no IgA epitopes. It was concluded that either of the two molecular species of alpha lm bearing common epitopes, with apparent mol. wts of 31,000 and 88,000-90,000, respectively, could form stable complexes with monomeric IgA. The association is likely to be performed through disulfide bridges. Nearly all the 88-90-kd but only a small proportion of the 31-kd component is associated with IgA.
Mol Immunol 1985 Jun
PMID:Complexes of alpha 1-microglobulin and monomeric IgA in multiple myeloma and normal human sera. 241 Jul 80

Eleven mouse monoclonal antibodies directed against epitopes on CNBr peptides of the major sialoglycoconjugate of the human red blood cell, glycophorin A, have been produced by hybridomas derived from P3-X63-Ag8.653 myeloma cells and spleen cells from BALB/c mice immunized with purified glycophorin. The monoclonal antibodies could be divided into four groups according to their reactivities with CNBr peptides in a direct ELISA assay: one antibody (6B5) that binds solely to the aminoterminal octapeptide (CNBr3); two antibodies (8F10 and 9C3) that bind to CNBrl (residues 9-81); two antibodies (3D2 and 4C6) that are reactive with CNBr2, The C-terminal portion of the molecule (residues 82-131); six antibodies (1B4, 4C3, 4E7, 7B10, 7C11 and 9D6) which are cross-reactive with an epitope on both CNBr1 and CNBR3 glycopeptides. This cross-reactive epitope(s) appears to involve both carbohydrate and protein residues.
Mol Immunol 1985 Apr
PMID:Monoclonal antibodies to cyanogen bromide fragments of glycophorin A. 241 8

Radioiodinated human secretory IgA (sIgA) injected intravenously into mice was rapidly cleared from the circulation by the liver. A portion of the sIgA was transported as an intact molecule into the bile. However, this transport was less efficient than that of human serum polymeric IgA (pIgA). The clearance of sIgA from the circulation was inhibited by prior injection of asialofetuin, suggesting that its uptake is mediated by the hepatic binding protein (HBP) specific for asialoglycoproteins. Mouse pIgA did not inhibit the hepatic clearance of sIgA. Results of in vivo studies were confirmed by in vitro experiments. The binding of 125I-asialoorosomucoid to either the particulate fraction (2000 g pellet of the homogenate) or the plasma membrane fraction of mouse liver was inhibited by sIgA. When polypeptide components of sIgA were used as inhibitors, significant inhibition was obtained with secretory component (SC), while inhibition with light and J-chains was not statistically significant. Examination of the inhibitory activity of IgA1 and IgA2 myeloma proteins and heavy chains isolated from these proteins revealed that binding of polymeric IgA1 and alpha 1 heavy chains can also be mediated by HBP. However, these interactions appear to be of lower avidity than those with SC. The inhibitory activity of human IgA2 and alpha 2 heavy chains was not significant. The involvement of HBP in binding of sIgA was also confirmed by measuring the inhibition of binding of 125I-sIgA. The binding of this protein by the particulate fraction of the mouse liver homogenate was inhibited by asialoglycoproteins and SC while inhibition with IgA1 and alpha 1 heavy chains was not significant. These results suggest that the carbohydrate moieties recognized by HBP reside primarily in the SC portion of sIgA.
Mol Immunol 1985 Aug
PMID:Carbohydrate-mediated clearance of secretory IgA from the circulation. 241 48

Mouse monoclonal antibodies directed against nerve growth factor (beta NGF) from bovine seminal plasma have been isolated and characterized. They are produced by hybridomas derived from Sp2/0.Ag14 myeloma cells and spleen cells from BALB/c mice immunized with beta NGF which was purified by the method of Harper et al. [J. biol. Chem. 257, 8541-8548 (1982)]. Five of these hybridomas can be grown in ascites tumor form and secrete antibodies of the IgG1 or IgG2a subclass. When used to probe the components of seminal plasma extracts or purified beta NGF as separated electrophoretically on SDS gels, the antibodies react with the beta NGF band at Mr = 15,000. The antibodies bind to native bovine beta NGF, but bind very poorly to mouse beta NGF. Antibody exclusion and additive-binding experiments indicate that these antibodies bind to the 1 antigenic domain. The cell receptor binding site is probably not close to this domain, as the antibodies fail to block the biological activity of bovine beta NGF on cultures of dissociated neurons from sensory ganglia. These monoclonal antibodies define a region in which bovine beta NGF is structurally different from the closely related molecule mouse beta NGF.
Mol Immunol 1985 Sep
PMID:Monoclonal antibodies to nerve growth factor from bovine seminal plasma. 241 11

Two IgG mouse monoclonal antibodies (MAbs), Abs 242 and 463, were prepared by fusion of spleen cells from mice immunized with human C4b with a myeloma cell line, P3/ X 63-Ag 8.653. They were assessed for their effect on the activation and stability of the cell-bound classical-pathway C3 convertase, EAC14b2a and on the binding of C2 and C4bp to EC4b. Ab 242 recognized a conformational neoantigen which appeared upon activation of C4 with C-1s and disappeared after chain separation of C4b, while Ab 463 recognized a linear epitope in the beta-chain of C4b. Ab 242 was found to be a C4bp-like MAb: it accelerates the decay-dissociation of C3 convertase and interferes with the binding of C2 to C4b. It also interfered with the binding of C4bp to C4b. These results suggest that Ab 242 recognizes an epitope which is closely related to the C2- and C4bp-binding sites in C4b. Ab 463, on the other hand, was found to be a nephritic factor like MAb: it prolongs the half-life of C3 convertase from 8 to 30 min at 37 degrees C.
Mol Immunol 1986 Feb
PMID:Monoclonal anti-human C4b antibodies: stabilization and inhibition of the classical-pathway C3 convertase. 242 44


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