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)

Twelve C57BL/6J anti-B-1355S monoclonal antibodies (five IgM lambda and seven IgM kappa) were characterized immunochemically by binding and inhibition ELISA. All 12 were negative for the expression of the cross-reactive idiotype (IdX) of BALB/c mice, as expected from previous work; no kappa IdX+ antibodies have been reported and IdX- lambda class antibodies were observed in B-1355-Con A induced immune sera [Geckeler W., Blomberg B., dePreval D. and Cohn M. (1977) Cold Spring Harb. Symp. quant. Biol. 41, 743-748]. The antibodies studied bind to B-1355 coated plates and this binding is inhibited by B-1355 but not by dextrans B-512 (F) or B-742S; the latter two have no linear alpha (1----3; 1) linkages. The nomenclature of Jeanes is used [Jeanes A. (1986) Molec. Immun. 23, 999-1028]; alpha (1----3; 1) refers to glucosyl diose residues linked alpha (1----3) linearly. In the case of B-1355 these linear stretches alternate with alpha (1, 6) linkages and are non-contiguous; alpha (1----3; b) refers to the linkage at a branching residue, e.g., a 1,3,6 linked moiety. The IgM kappa class antibodies are not inhibited by nigerose or nigerantetraose, suggesting that they have binding site sizes which are unusually large for B-1355 specific antibodies. The five IgM lambda antibodies are inhibited identically by equimolar amounts of nigerose and nigerantetraose, suggesting that their binding sites accommodate a disaccharide epitope. These antibodies are also inhibited by the alpha (1----6), alpha (1----4) triose, panose. The kappa class antibodies do not bind to alpha (1----3)-diglucosyl-(nigerosyl; N)-BSA. Four of the five lambda class antibodies show weak binding to N-BSA, while the fifth binds N-BSA better but less well than MOPC 104E (the BALB/c myeloma protein). All 12 antibodies are unique when compared to BALB/c antibodies derived from B-1355 immunization. The primary response of 15 C57BL/6J mice to B-1355 was re-assessed for kappa and lambda class antibody contribution. A patchy lambda class response was observed suggesting that previous lambda class responses may have been overlooked.
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PMID:Immunochemical analyses of C57BL/6J monoclonal anti-alpha (1----3) dextran antibodies. 246 48

Cryoglobulinemia is seen in a minority of patients with plasma cell dyscrasias and can be of clinical relevance if intravascular gelling or precipitate formation occurs at low temperatures. We observed a patient suffering from IgG-kappa multiple myeloma which was complicated by instability of the immunoglobulin forming crystalline precipitates at low pH and low temperature. Short exposure to extreme cooling initiated an unusual course terminating in disseminated vascular occlusion and fatal outcome which was connected with an adverse effect of blood exchange. Crystal formation was noticed in anticoagulated blood samples even at 37 degrees C. In vitro studies showed a critical pH dependency of solubility of the immunoglobulin close to the physiological pH of the blood. These observations suggest that the fatal outcome was due to a vicious circle of ischemia, metabolic acidosis and intravascular precipitations, initiated not only by low acral temperatures but by cold-induced ischemic tissue acidosis as well. Serum of patients with monoclonal gammopathy and cryoglobulinemia should be tested for pH dependent immunoglobulin insolubility.
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PMID:Cryocrystalglobulinemia: pH-dependent precipitation of a monoclonal IgG-kappa-immunoglobulin. 249 13

While in carps kept in warm water (28 degrees C) and immunized with a human myeloma protein a challenge leads to an increase, the antibody titres in carps kept in cold water (14 degrees C) are changed only unsignificantly. Antibody titres of carps immunized once respectively three times and kept in cold water are not markedly different. In testing the specificity of the antisera taken from each of the three groups no differences could be recognized. With carp anti-IgGZei sera using the passive hemagglutination inhibition test a paraprotein characterizing determinant (s) is just as well demonstrable as by using a rabbit antiserum.
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PMID:[Specificity of carp antihuman myeloma protein sera depending on the holding temperature]. 293 21

A hybridoma-producing monoclonal antibody blocking the binding of human IgE to lymphocytes Fc receptor (Fc epsilon R) was established by the fusion of murine myeloma cells. P3X63.653.Ag8, with BALB/c spleen cells immunized with Fc epsilon R(+) human B lymphoblastoid cell line cells, RPMI1788. A clone of the hybridoma (H107) produced a monoclonal IgG2b antibody that inhibited the rosette formation of Fc epsilon R(+) human B lymphoblastoid cell line cells (RPMI1788, RPMI8866, CESS, Dakiki, and IM9) with fixed ox red blood cells (ORBC) conjugated with human IgE (IgE-ORBC). In contrast, the rosette formation with IgG-conjugated ORBC (IgG-ORBC) on Fc gamma R(+), Fc epsilon R(-) Daudi cells were not affected by the H107 antibodies. A close association of Fc epsilon R and the antigenic determinant recognized by H107 antibody was suggested by the following results. First, the bindings of 125I-labeled IgE (125I-IgE) or 125I-labeled H107 IgG2b antibody (125I-H107) to RPMI8866 cells were inhibited by cold human IgE and H107 IgG2b but not by other classes of human Ig (IgA and IgG), MPC11 IgG2b, or unrelated monoclonal antibodies. Second, H107 antibody reacted with Fc epsilon R(+) B cell lines but not with Fc epsilon R(-) B cell lines as determined by an indirect immunofluorescence. Third, Fc epsilon R(+) cells were depleted by the incubation in the dish coated with H107 antibody or IgE but not in the dish coated with unrelated antibodies. Finally, there was a correlation between the increase of Fc epsilon R(+) cells and that of H107(+) cells in the peripheral blood lymphocytes of the patients with atopic dermatitis. The surface antigens on Fc epsilon R(+) RPMI8866 cells recognized by H107 antibodies had the molecular size of 45,000 as determined by immunoprecipitation and sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis.
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PMID:Monoclonal antibody (H107) inhibiting IgE binding to Fc epsilon R(+) human lymphocytes. 294 2

The radiographic patterns of the skeleton of 73 patients affected by multiple myeloma (MM) were compared to the correspondent scintigraphic findings. Whole body scans were performed using 99m Tc-diphosphonates (bone scintigraphy), and 99m Tc-microcolloids (bone marrow scintigraphy). The results indicate that: a) radiography is more sensitive and accurate than scintigraphy in detecting typical myeloma-related bone lesions; b) bone scintigraphy is useful in detecting alterations in particular locations--i.e., sternum, ribs, scapulae, etc.--which are difficult to demonstrate by plain X-rays; moreover, the recovery of the fractures can be visualized; c) bone marrow scintigraphy is employed to demonstrate the presence of marrow expansion, of cold/hot spots, and relative marrow uptake, related to phagocytic activity. Since in adult men red marrow is confined to the epiphysis of long bones and to the spine, all the diseases affecting bone marrow cause medullary expansion/reduction, which are both easily detected by specific radiopharmaceuticals. The peripheral expansion is clearly documented especially in distal humeri and femora since marrow uptake is included, in healthy adults, in the axial and proximal appendicular skeleton. In spite of its yielding unique information, bone marrow scintigraphy remains an additional technique of bone scan, because of its low diagnostic accuracy.
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PMID:[Bone marrow scintigraphy in multiple myeloma. A comparison with bone scintigraphy and skeletal radiology]. 314 87

In searching for disease on skeletal images it is important to identify areas of increased activity and cold lesions, which are usually more difficult to identify. Focal photon-deficient lesions are due to metastatic disease in over 80% of cases. They may occur if the tumor is extremely aggressive, if there is disruption of the blood supply to the bone, or if there is significant marrow involvement, particularly in a vertebral body. Some of the common causes of a photopenic lesion are avascular necrosis, malignant bone tumors such as multiple myeloma, metastasis, radiation therapy, attenuation artifacts such as prosthesis or pacemaker, and early osteomyelitis. A case of hemangioma of the dorsal vertebra, a rare cause of photopenic lesion, is reported here.
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PMID:Hemangioma, a rare cause of photopenic lesion on skeletal imaging. 318 Jun 15

Vero cells, SP2/O-Ag 14 myeloma cells and 4B87 hybridoma cells were stored either at refrigeration (5 degrees C) or freezing (-18 degrees C) temperatures. Cells were recovered every five days and percentages of viable cells were determined by the trypan blue exclusion staining method before the cells were incubated at 37 degrees C in a 5% CO2 atmosphere. SP2/0 cells grew after 30 days of storage at 5 degrees C. Hybridoma (4B87) cells survived 20 days of cold storage in HY medium and maintained antibody production. For each cell type, higher percentages of viable cells were observed among cells stored in HY medium than among cells stored in DMEM. Vero cells stored for 40 days at 5 degrees C grew when removed to optimal conditions of 37 degrees C and 5% CO2. There was no growth of cells recovered after storage at -18 degrees C.
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PMID:Survival of Vero, myeloma and hybridoma cells during cold storage. 340 8

Freshly separated human NK cells (NKH-1+) inhibited IgE synthesis from IgE myeloma U266/AF-10 as much as 70% whereas they enhanced IgG and IgA synthesis 200 and 500% from the lymphoblastoid cell lines GM-1500 and GM-1056, respectively. The inhibition of IgE synthesis by NK cells was due to a direct cytolytic effect on AF-10. This could be reversed using K562 cells in a cold target competition assay. NK cells also inhibited spontaneous IgE as well as IgG and IgA synthesis from B cells of highly atopic donors. On the other hand the enhancement of Ig secretion by NKH-1+ cells was shown to be mediated by soluble factors released from NK cells. Furthermore when NK cells were preincubated with immune complexes (IgE-IC) constructed of human IgE and mouse IgG1 monoclonal anti-human IgE, inhibition of IgE synthesis was reversed, and in some cases actual enhancement of IgE synthesis was observed, while enhancement of IgG and IgA synthesis was not affected. In contrast to NK cells, T cells depleted of NK cells (T-NK), when activated by IgE-IC, suppressed IgE synthesis in an isotype specific fashion. Thus, NK and T-cell modulation of ongoing Ig synthesis involve distinct mechanisms.
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PMID:Modulation of ongoing human immunoglobulin synthesis by natural killer cells. 349 49

Mouse myeloma NS1-Ag4 cells were fused with spleen cells from a BALB/c mouse previously immunized with luteinizing hormone releasing hormone (LHRH) conjugated to serum bovine albumin (BSA). Fused cells were grown in HAT restrictive medium which was screened for LHRH binding ability via a primary binding assay employing [125I]LHRH and cold ethanol precipitation. One clone (hy-USASK/DSIL-LHRH-A1) was selected for further study. Cell culture fluid and ascites fluid bound 30% of [125I]LHRH at 1:4000 and 1:400,000 dilution respectively. A competitive inhibition assay using ascites fluid at 1:2,000,000 dilution and LHRH standards at 0.125-32.0 ng/ml was established. Initial studies using rabbit anti-mouse allotype sera in a horseradish peroxidase (HRP)-ELISA system indicate the antibody is IgG1. A dose of 0.5 ml ascites fluid containing LHRH antibody given intravenously (i.v.) on day 9 of gestation was effective in terminating pregnancy in rats. A 1 cm progesterone implant made of elastomer polymer and placed interperitoneally blocked this effect. Ascites fluid (4.5 ml) containing LHRH antibody, when infused i.v. into mature spayed female dogs induced a precipitous decline in mean luteinizing hormone (LH) levels and reduced LH pulsatility over 4 days. It was concluded that the mouse monoclonal antibody is specific for LHRH, and can interrupt reproductive events in vivo.
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PMID:Monoclonal antibodies against LHRH: development and immunoactivity in vivo and in vitro. 388 2

95 of 1,019 (9.3%) sera with monoclonal immunoglobulins (MIg) were found to have cold-reacting lymphocytotoxins (LCT). There was no difference in the prevalence of LCT in multiple myeloma, macroglobulinemia, cancer, lymphoma or benign monoclonal gammopathy. Prevalence of LCT was similar in various classes and types of MIg with the exception of the IgG/lambda group in which LCT were more common than in IgG/K (p = 0.013). IgMs had the most potent whereas IgAs had the weakest LCT activity. MIg were purified from 61 LCT-positive sera. 25 pure MIg (41%) had LCT activity. In the rest, LCT activity resided in other fractions. 64 sera with LCT were tested against B and T cells; 56% were equally cytotoxic to B and T cells, 39% killed more B cells and 5% killed more T cells. 18 purified lymphocytotoxic MIg killed both B and T cells. When serial dilutions of sera, and of purified MIg were tested, in all but one instance the reactivity with the T cells weakened more than that with the B cells. Lymphocytotoxins absorbed to and eluted from the peripheral blood lymphocytes or separately from B or from T cells retained LCT activity against B and T lymphocytes. It may be concluded that about one tenth of sera with M components have lymphocytotoxic activity and that in about 40% of these positive sera, this activity is related to the monoclonal immunoglobulins. LCT react with both B and T cells. Antilymphocyte activity of MIgs may play a role in immunoregulatory abnormalities in plasmalymphocytic diseases.
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PMID:Lymphocytotoxic activity of monoclonal immunoglobulins in plasmalymphocytic diseases. 393 40


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