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 hybridoma cell line (26-10) derived from the A/J strain of mice secretes an immunoglobulin (IgG2a-k) which binds digoxin with an association constant of 1.2 nM. Such high-affinity antibodies have been utilized in clinical radioimmunoassays as well as in the reversal of toxicity due to excess digoxin. The amino acid sequence of the light chain variable region of this antibody was derived by automated sequencing of the following: the intact chain; a fragment beginning C terminal to the tryptophan residue 40, obtained by cleavage with iodosobenzoic acid; a fragment beginning C terminal to arginine residue 82, obtained by trypsin cleavage on the completely reduced, alkylated, and succinylated chain. Difficulties which had previously prevented the automated Edman sequencing of this chain (and, presumably, similar ones of the same subgroup) were overcome by increasing the duration of the cleavage step at proline residues 8 and 12. The sequences of the first two hypervariable and framework regions of this chain are virtually identical with those of the dinitrophenol- and menadione-binding myeloma light chain MOPC 460 (95% homology). This anti-digoxin hybridoma from the A/J strain makes use of a Vk gene which is similar to that utilized by some BALB/c 2,4-dinitrophenol-binding myelomas.
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PMID:Amino acid sequence of the light chain variable region from a mouse anti-digoxin hybridoma antibody. 640 98

Monoclonal antibodies specific for cell surface antigens on embryonic chick ciliary ganglion neurons (CG) have been obtained at high frequencies by fractionating spleen cells from immunized mice according to their adhesiveness for cell surfaces of the cultured neurons. Spleen cells from mice that had been immunized with live or lightly fixed (0.125% glutaraldehyde) CG neurons were selected for subsequent hybridization with myeloma cells after fractionation on lawns of CG neurons in tissue culture. Immunized spleen cells were cultured with the neurons for 4-7 days prior to fractionation. Three groups of spleen cells were selected for fusion with a myeloma cell line: a non-adherent population of spleen cells, a population of spleen cells that could be removed from the neuronal cells by shaking on a vibratory shaker for 1 h, and a population that could be removed from the neuronal cells only by treatment with low concentrations of trypsin. Of the 3 groups of spleen cells, the population that required trypsin treatment produced the greatest number of hybridomas specific for neurons and for neuronal cell surfaces. Fewer neuron-specific hybridomas resulted from fusion of the group of spleen cells that could be removed from the antigen lawn by shaking. None of these was specific for the CG neurons. No neuron-specific hybridomas resulted from the fusion of the cells that did not adhere to the neuronal cells, and at most only 1 neuron-specific hybridoma resulted from fusions of comparable groups of unselected spleen cells (spleen cells from immunized animals which were not selected on antigen lawns).
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PMID:Differential antigen adhesivity used to select spleen cells for the production of monoclonal antibodies to embryonic neurons. 649 Dec 93

Spleen cells from Balb/c mice given multiple injections of intact human erythrocytes (group O, NN) were fused with NS1 myeloma cells. Culture fluids from the resulting hybrid cells were screened for agglutinating antibody against a panel of erythrocytes. One cell line, 2/23, secreted an IgM antibody which reacted more strongly with NN than with MM cells. Neuraminidase or papain treatment of erythrocytes abolished agglutination whereas trypsin treatment did not. Reactions with U- erythrocytes of different MN phenotypes confirmed the anti-N specificity of monoclonal antibody 2/23. This is the first report of monoclonal anti-N stimulated by the immunization of mice with intact erythrocytes.
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PMID:An interesting monoclonal anti-N produced following immunization with human group O, NN erythrocytes. 672 62

Mouse inflammatory macrophages from C57BL/6N mice were fused with BALB/c mouse-derived myeloma cells (the CANS series). The hybrids in the early period after cell fusion (8 weeks) showed no macrophage functions (chemotaxis, EA and EAC rosette-forming abilities, phagocytosis or lysozyme production). EA rosette-forming ability was observed when these hybrids were treated with trypsin, whereas other macrophage functions were not. After prolonged culture, the hybrids (12 clones of 13 randomly selected) showed all the macrophage functions along with chromosome loss. Myeloma cell functions (kappa light chain production) were found in the young hybrids soon after cell fusion but were absent in the aged hybrids. These results indicated that reexpression of macrophage properties, except for EA rosette-forming abilities, takes place after the loss of chromosomes or genes repressing the expression of macrophage functions.
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PMID:Expression of macrophage functions in hybrids of a myeloma cell line with inflammatory macrophages: evidence for negative control mechanisms in the expression of macrophage functions. 673 48

A calcium binding IgG was isolated and purified by column chromatography from serum of a myeloma patient with asymptomatic hypercalcaemia. The myeloma IgG, characterized as an IgG kappa, revealed a normal sized heavy chain (56 000 dalton), and a light chain of 31 000 dalton. Another population of IgG separated and purified from the same patient's serum did not bind calcium and had a normal 26 000 dalton light chain. Calcium binding activity in vitro is optimal at pH 8.0, and reaches its maximum after 3 h of 45Ca myeloma IgG incubation. Cleavage of the purified IgG by trypsin yielded peptides which were further isolated by column chromatography and characterized as Fab and Fc fragments. Light and heavy chains were obtained by reacting the immunoglobulin with dithiothreitol and iodoacetamide followed by Sephadex G-100 chromatography. Calcium binding activity was proved to be associated with Fab IgG fragment. Preparates containing Fc, heavy or light chains did not bind calcium in vitro.
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PMID:A calcium binding IgG myeloma protein. 676 47

The complete amino acid sequence of an Fc-like fragment designated Fc delta (t) and obtained by limited proteolysis with trypsin of an intact myeloma IgD protein (NIG-65) has been determined. The fragment contains 226 amino acid residues and has a molecular weight of 32,000 per monomeric unit. It has three glucosamine oligosaccharides at asparagine residues 68, 159, and 210. Of these, glucosamine-159 is characteristic of the delta chain and has no counterpart position in any of the other classes. On the other hand, glucosamine-68 is shared by gamma, mu, and epsilon, and glucosamine-210 is shared by alpha and mu. Although the Fc delta (t) has the common framework structure of immunoglobulins, its sequence has many individual characteristics when its two domains are compared separately with the counterpart domain of other heavy chains. Such comparison has shown that the two Fc domains of the delta chain should be placed in an independent branch in topology; for all the other classes, the Fc domains are paired well with their counterparts. The comparison has also shown that there are three prominent gaps by which each domain can be divided into two homologous halves. For each class of immunoglobulin, a moderate degree of internal homology exists between the first half and the second half of each domain of the Fc, suggesting that the primordial gene may have coded for a unit about the size of a half domain. Based on this observation together with sequence comparisons, a possible genetic mechanism is proposed for the origin and evolution of the genes for immunoglobulin domains.
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PMID:Complete amino acid sequence of the Fc region of a human delta chain. 678 54

Sera from 14 patients with an IgA M-component, six of whom had myelomatosis and eight with benign monoclonal gammopathy (BMG) were analysed. All six sera from patients with high IgA (greater than 40 g/l) and total protein (greater than 100 g/l) concentrations were hyperviscous (HV). Four of these six patients also had hyperviscosity syndrome (HVS). There was no correlation between the quantity of IgA dimers or polymers and the presentation of HV and HVS. The binding between IgA and albumin and alpha 1-anti-trypsin was not covalent. Differences in the microenvironment of S-S bonds or of aromatic amino acids between isolated monoclonal monomeric and dimeric IgA were demonstrated with circular dichroism. Besides that, differences in hydrophobicity (exposure of aromatic amino acids) between IgA from normal serum and monomeric and dimeric IgA from a myeloma serum were revealed using hydrophobic interaction chromatography. The significance of hydrophobic interactions involving IgA and the influence of such forces on the circulation of the molecules are discussed.
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PMID:Factors affecting IgA related hyperviscosity. 685 Dec 49

Thirteen IgG monoclonal antibodies to the envelope protein of 17D yellow fever virus (17D YF) were produced. All of the antibodies, whether type-specific to 17D YF or flavivirus cross-reactive, mediated antibody-dependent enhancement (ADE) of virus growth in P388D1 cells. There was no consistent relationship between ADE titres and the degree or pattern of neutralizing and/or haemagglutination inhibition activity. Monoclonal antibodies of different isotypes were used to investigate further the properties of P388D1 Fc receptors. The effects of trypsin treatment of P388D1 on ADE were similar to those previously described in experiments measuring direct binding of IgG proteins or rosetting of sheep red blood cells (SRBC) by macrophages, demonstrating sensitivity to digestion by trypsin of the Fc receptor for monomeric IgG2a but not for IgG2b. Aggregated myeloma proteins of IgG2a and IgG2b isotypes competed equally well with either IgG2a or IgG2b monoclonal antibodies to 17D YF in inhibition of ADE. However, selective inhibition by the homologous isotype was observed when rosetting by P388D1 of SRBC coated with IgG2a or IgG2b monoclonal antibodies was examined. These results may help to explain apparent discrepancies previously reported between experiments utilizing direct binding of IgG proteins and those using rosetting of antibody-coated SRBC to examine Fc receptor properties and indicate that immune complexes of virus and antibody resemble aggregated immunoglobulins with respect to macrophage Fc receptor function and differ from antibody-coated SRBCs.
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PMID:17D yellow fever virus infection of P388D1 cells mediated by monoclonal antibodies: properties of the macrophage Fc receptor. 685 70

The crystallizable myeloma immunoglobulin IgG1 KOL [allotype Gm(-1,4), (gamma 1, gamma)2] which is well characterized in its three-dimensional structure by X-ray diffraction analysis of high resolution has been proved to be homogenous by polyacrylamide gel electrophoresis. The H- and L-chains were separated by gel filtration after complete reduction and carboxymethylation and were characterized by amino acid analysis, end group determination and polyacrylamide gel electrophoresis, respectively. The intact IgG1 KOL was cleaved by cyanogen bromide and all CNBr-fragments were isolated and characterized. The reduced and carboxymethylated H-chain was digested by trypsin and the tryptic hydrolysate was separated by ion-exchange chromatography. Using different procedures of rechromatography 35 out of 37 tryptic H-chain peptides could be isolated in sufficient amounts, the missing 2 peptides were produced by tryptic digestion of 2 CNBr-fragments. The amino acid sequences of all tryptic peptides were determined using a modified Edman degradation method after separation of the enzymatic cleavage products by high-performance liquid chromatography (HPLC). The complete primary structure of the VH-part of the H-chain was established by isolation and partial sequence determination of overlapping peptides obtained from cleavage of the intact H-chain by Staphylococcus aureus proteinase. The gamma 1-H-chain KOL comprises 455 amino acid residues and belongs to subgroup III. The switch from the variable to the constant part occurs at position 126/127, thus making VH-KOL one of the longest variable parts among the yet known immunoglobulin H-chains. This is due to the hypervariable region Hhv4 which is made up by 17 amino acid residues (4-9 residues more compared with other VH-parts). Within this region a so far not described additional intrapeptidal disulfide bridge could be localized (Cys 105-Cys 110) that creates a short loop with antiparallel running peptide strains in beta-pleated sheet conformation. Its role in the three-dimensional structure of the antigen-binding site of the IgG1 KOL molecule is discussed using the data obtained from X-ray diffraction analysis.
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PMID:[Three-dimensional structure determination of antibodies. Primary structure of crystallized monoclonal immunoglobulin IgG1 KOL, I]. 688 94

Crystalline tissue deposits were found at the time of autopsy in a 52-year-old male subject who had had multiple myeloma for 6 1/2 years and in whom the hyperviscosity syndrome had developed terminally. The tissue deposits were digested by trypsin, but could not be further characterized by immunohistochemical techniques. The crystals varied in size and shape and were located in tissue histiocytes, renal tubular cells, Leydig's cells, and adrenocortical cells. No crystals were identified within plasma cells. Their presence in the present case may have been related to the relatively long course of the disease, the high levels of serum proteins terminally, and unusual physicochemical structure of the secreted proteins, or possibly to the effects of chemotherapy.
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PMID:Crystalline tissue deposits on a case of multiple myeloma. 689 25


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