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)

The surface properties of blood lymphocytes from treated myeloma patients and healthy controls were studied in vitro. The patients were tested 6 weeks after the last treatment to allow time for cells to recovery from possible drug toxicity. Peripheral-blood lymphocytes were tested for rosette formation with unsensitized sheep erythrocytes (E rosettes) and with complement and antibody-coated erythrocytes (EAC rosettes). The tests were duplicated using lymphocytes pretreated with trypsin. As others have noted, myelomatosis is associated with increased blood levels of EAC-rosette-forming cells and a marked reduction in E-rosette-forming cells. E-rosette formation was significantly increased by pretreatment of myeloma lymphocytes with trypsin. By contrast, enzyme-treated cells showed no significant change in EAC-rosette formation. These results suggest that the absolute number of circulating T cells is probably not reduced in myelomatosis, but that the surface of T cells is somehow modified so that a proportion of them lose the ability to form E rosettes.
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PMID:Enzyme-induced modification of the surface properties of lymphoid cells in malignant disease. I. Effect of trypsin on rosette formation by lymphocytes in myelomatosis. 696 55

Human IgE was found to bind to the human macrophage line U937. Binding was specific for IgE in that it was inhibited by 3 different human IgE myeloma proteins and by Fc fragments prepared from IgE, but not by IgE Fab fragments or by myeloma proteins representative of the 4 IgG subclasses or by a rat IgE myeloma protein. Dissociation and association rates were rapid, with estimated t1/2 of less than 1 min. The Ka was 4.15 X 10(7) liter/mol. Between 53,000 and 93,000 sites per cell were calculated. The U937 receptor for IgE was trypsin sensitive, whereas the receptor for IgG on the same cell was relatively trypsin resistant.
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PMID:Macrophage receptors for IgE: binding of IgE to specific IgE Fc receptors on a human macrophage cell line, U937. 701 19

Four monoclonal antibodies obtained from the fusion of mouse myeloma cells with lymphocytes of mice immunized with bovine rod outer segment disc membranes were shown to bind to the surface of sealed discs. Radioimmune labeling of rod outer segment membrane proteins separated by sodium dodecyl sulfate gel electrophoresis indicated that two monoclonal antibodies (3D6 and 4B4) were against rhodopsin. Limited proteolysis of rod outer segment membranes with trypsin and Streptomyces griseus protease indicated that the 3D6 antibody bound to the trypsin-sensitive region close to the carboxyl-terminal end of rhodopsin. The 4B4 antibody bound at a trypsin insensitive, but S. griseus protease-sensitive internal region of rhodopsin accessible on the cytoplasmic surface of discs. Two other monoclonal antibodies (3D12 and 4B2) were found to bind to different regions of the Mr = 220,000 concanavalin A binding glycoprotein of rod outer segment disc membranes. Proteolysis studies indicated that these antibodies also bound to a Mr = 140,000 fragment which does not contain the concanavalin A binding site. Immunoferritin-labeling studies for transmission electron microscopy confirm the location of the 3D6 and 4B2 antigens on the cytoplasmic or interdisc surface of disc membranes.
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PMID:Organization of rhodopsin and a high molecular weight glycoprotein in rod photoreceptor disc membranes using monoclonal antibodies. 708 19

Pure secretory immunoglobulin A was isolated from human milk by fractionation in gradients of pH and (NH4)2SO4 concentration followed by gel filtration. The hinge region containing all the O-glycosidically linked oligosaccharides was isolated en bloc after trypsin and pepsin hydrolysis and separated by gel filtration. The mixture of O-glycosidically linked oligosaccharides contained N-acetylneuraminic acid (NeuAc), fucose (Fuc), galactose (Gal), N-acetylglucosamine (GlcNAc) and N-acetylgalactosamine (GalNAc) in the molar ratio of 0.2:0.5:2.5:2:1 respectively. After beta-elimination several oligosaccharides were separated by a combination of ion-exchange chromatography and gel-filtration chromatography. The complete structure of four of these oligosaccharides was determined by methanolysis, methylation and mass spectrometry. The structure of the four oligosaccharides which are linked to serine or threonine residues of the hinge region are as follows: beta-Gal-(1 leads to 3)-GalNAc-ol; alpha-HeuAc-(2 leads to 3)-beta-Gal-(1 leads to 3)-GalNAc-ol; beta-Gal-(1 leads to 3)-[beta-GlcNAc-(1 leads to 6)]-GalNAc-ol; beta-Gal-(1 leads to 3)-[beta-Gal-(1 leads to 4)-beta-GlcNac-(1 leads to 6)]-Gal-NAc-ol. These oligosaccharides are more complex and heterogenous than the oligosaccharides linked to serine residues of the hinge region from myeloma serum immunoglobulin A1.
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PMID:Heterogeneity of the glycans O-glycosidically linked to the hinge region of secretory immunoglobulins from human milk. 721 51

Membrane proteins which selectively bind to the Fc portion of IgG were identified in the Nonidet P-40 extracts of radiolabeled thioglycollate- elicited mouse peritoneal macrophages. Affinity columns of various IgG preparations coupled to Sepharose 4B were used to absorb the Fc-binding proteins. Analysis of the acetic acid or sodium dodecyl sulfate (SDS) eluates from aggregated human IgG or antigen-complexed rabbit IgG columns revealed two Fc(gamma)/-specific proteins with apparent 67,000 and 52,000 mol wt. These proteins were not detected in acid or SDS eluates from F(ab')(2) columns or in eluates from IgG column, over which were passed lysates of Fc receptor-negative cells. With the use of affinity columns that contained aggregated mouse myeloma proteins of different IgG subclasses, we found that the 67,000-dahon protein selectively binds to IgG2a, whereas the 52,000-dalton protein binds to IgG1 and IgG2b. Neither protein was found in SDS eluates from IgG3 columns. Trypsin treatment of the macrophages before detergent lysis removed the 67,000-dalton protein, although it leaves intact the 52,000-dalton protein. These results provide structural confirmation for the existence of separate Fc receptors on mouse macrophages and indicate that the two Fc-binding proteins identified in this study represent all or part of the trypsin- sensitive Fc receptor which binds IgG2a and the trypsin-resistant Fc receptor which binds IgG2b and IgG1.
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PMID:Structural evidence for distinct IgG subclass-specific Fc receptors on mouse peritoneal macrophages. 743 Sep 49

Monoclonal antibodies (MAbs) specific to plum pox virus (PPV) were prepared by fusing myeloma cell lines to spleen cells of mice immunized with purified virus, including virus prepared with protease inhibitors to preserve the integrity of the coat protein (CP). The characterized MAbs could be used in ELISA to differentiate several Mediterranean PPV isolates differing in their geographical origin and CP size. At least seven antigenic sites could be established based on the recognition pattern and competition binding analysis, and the epitopes could be classified in three groups by Western blot analysis of intact and trypsin digested virus particles. By means of electron microscopy the epitopes could be seen to be located on the surface of the virus particles.
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PMID:Production and characterization of monoclonal antibodies to plum pox virus and their use in differentiation of Mediterranean isolates. 752 22

Kidney tubule dysfunction and lesions are frequent complications of myeloma, related to unknown properties of the monoclonal light chain. We have analyzed protease sensitivity and binding properties of urinary light chains from four patients with Fanconi's syndrome, 12 with cast nephropathy, and four control patients without myeloma-associated tubulopathy. All light chains were normal-sized, monomeric and/or dimeric, and none was N-glycosylated. Kinetic studies of light chain digestion by pepsin and the lysosomal enzyme cathepsin B showed the generation of a protease-resistant 12 kDa fragment, corresponding to the V domain of the kappa chain in the four Fanconi's syndrome patients; in two out of four the V domain was also completely resistant to trypsin. Western and dot blots revealed similar patterns of reactivity of light chains from patients with the Fanconi's syndrome towards other light chains. Properties of cast-nephropathy light chains were more heterogeneous but clearly differed from those of Fanconi's syndrome: (i) 9 out of 12 were of the lambda-type; (ii) only four yielded a transient 12 kDa fragment after cathepsin B digestion, but all showed some resistance to proteolysis of the entire molecule or a fragment thereof to at least one protease, at variance with control light chains; (iii) they displayed various patterns of reactivity with other light chains; (iv) 7 out of 12 reacted specifically with Tamm-Horsfall protein (THP) by ELISA, in contrast with those of Fanconi's syndrome. In one patient who presented with cast nephropathy and the Fanconi's syndrome, the light chain exhibited both partial resistance of the V kappa domain to cathepsin B and the highest reactivity with THP.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Protease resistance and binding of Ig light chains in myeloma-associated tubulopathies. 756 94

Protein Fv is found in the normal liver and is released in the stools of patients suffering from viral hepatitis. Protein Fv isolated from five patients stimulated the release of histamine and sulfidopeptide leukotriene C4 from purified and unpurified peripheral blood basophils. Protein Fv absorbed with protein A-Sepharose coated with polyclonal IgG did not induce histamine secretion, whereas removal of putative contaminating Ig did not modify the releasing activity. The characteristics of the release reaction were similar to those of rabbit IgG anti-Fc fragment of human IgE (anti-IgE). There was an excellent correlation (Spearman rank coefficient (rs) = 0.83; p < 0.001) between the maximal percent histamine release induced by protein Fv and that induced by anti-IgE from basophils. Preincubation of basophils with either protein Fv or anti-IgE resulted in complete cross-desensitization to a subsequent challenge with heterologous stimulus. Basophils from which IgE had been dissociated by brief exposure to lactic acid no longer released histamine in response to anti-IgE and protein Fv. A monoclonal IgE purified from a myeloma patient (patient ADZ) blocked both anti-IgE- and protein Fv-induced releases, whereas human polyclonal IgG and a monoclonal IgG purified from another myeloma patient (patient ZEG) selectively blocked protein Fv-induced secretion. Protein Fv also induced the release of preformed (histamine and tryptase) and de novo synthesized mediators (sulfidopeptide leukotriene C4 and/or PGD2) from mast cells purified from human lung parenchyma and skin tissues. There was a significant correlation between the maximal percent histamine release induced by protein Fv and anti-IgE from skin mast cells (rs = 0.63; p < 0.01). There was also an excellent correlation between histamine and tryptase release caused by protein Fv from both lung (rs = 0.80; p < 0.001) and skin mast cells (rs = 0.70; p < 0.01). Thus, we established that protein Fv acts as a novel activator of human basophils and mast cells presumably by interacting with the VH domain of the IgE.
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PMID:Protein Fv produced during vital hepatitis is a novel activator of human basophils and mast cells. 769 15

An effort was made to generate stable swine hybridomas capable of releasing monoclonal antibodies (MAb) with antigenic specificity. Crossbred pigs were immunized with recombinant porcine growth hormone (r-pGH) and the splenic cells were harvested from these animals. B lymphocytes enriched by gradient centrifugation and nylon wool adherence were briefly stimulated in vitro with r-pGH prior to hybridization with murine SP2/0 myeloma cells. The fused hybrids were screened for their ability to produce anti-pGH antibody and the positive ones were subcloned by a limiting dilution procedure. The stable cell lines were maintained by serial passages in cultures for further analysis. One such hybridoma, designated PM20/20, was found to secrete swine IgM. It recognized not only the immunizing r-pGH but also the native pGH extracted from the swine pituitary glands, as demonstrated by Western analysis. It also recognized two smaller fragments with m.w. of 10 kD and 5 kD of r-pGH following trypsin digestion. In addition to pGH, PM20/20 immunoreacted with several other GH species including bovine, chicken, and human origins, but not with ovine prolactin nor rat GH binding protein. The binding association rate constant and dissociation rate constant of PM20/20 to pGH were 5.3 x 10(4) M-1 s-1 and 1.0 x 10(-4) s-1, respectively, thus producing a dissociation constant of 1.9 x 10(-9) M. Therefore, stable swine-mouse heterohybridoma lines have been established and shown to continuously release swine mAb in cultures. These mAb may serve as useful alternatives to murine mAb in certain areas of research.
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PMID:Generation of heterohybridomas capable of releasing swine monoclonal antibody specific to porcine growth hormone. 792 68

Bence Jones proteins purified from urine of patients with multiple myeloma were found to be capable of hydrolyzing carbobenzoxy-L-valyl-glycyl-L-arginine p-nitroanilide (Chromozym TRY) and benzoyl-L-arginine p-nitroanilide (BApNA), synthetic chromogenic substrates for trypsin. The amidolytic activity obeyed classic Michaelis-Menten kinetics, exhibiting optimal activity around pH 8.4 and apparent Km of 140-730 microM and 18-27 microM for Chromozym TRY and BApNA, respectively. No activity was detected with intact IgG or Fab fragment, whereas the activity comparable to those of Bence Jones proteins was found with light chain derived from inactive IgG. Several lines of circumstantial evidence indicate that the observed activity was not due to contaminating enzyme.
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PMID:Amidase activity of human Bence Jones proteins. 794 92


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