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)

We describe an atypical case of IgG lambda multiple myeloma in a 28-year-old patient. He developed multiple cutaneous plasmacytomas, and the terminal event, leukemic conversion by phagocytic plasma cells and disseminated intravascular coagulation. Secretion of monoclonal immunoglobulin (IgG lambda) from myeloma cells was demonstrated by plaque-forming cell assay. Electron microscopy showed myeloma cells with well-developed rough endoplasmic reticulum and erythroid cells or platelets in intracytoplasmic vacuoles.
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PMID:Phagocytic multiple myeloma with disseminated intravascular coagulation. 250 1

Human myeloma cells are malignant counterparts of plasma cells which represent the most differentiated B cells. Myeloma cells are, however, heterogeneous in their surface antigen expression (Katagiri et al, 1984, 1985), which may reflect that normal plasma cells have a spectrum of differentiation. To test this hypothesis, immunoglobulin-secreting cells (ISC) of non-neoplastic nature were studied with regard to their surface antigen expression by using a combination of reverse haemolytic plaque assay and complement-dependent cytolysis. Non-neoplastic ISC were found to have a broad spectrum of differentiation stages from the immature type of CD20+, HLA-DR+, CD38+ in the peripheral blood to the mature type of CD20-, HLA-DR-, CD38+ in the bone marrow. In patients with polyclonal B cell activation (PBA), ISC showed a more immature antigen expression in comparison with ISC in normal controls or patients without PBA. The surface antigen development of ISC was clearly demonstrated throughout the stages in the analysis of mitogen-induced ISC in vitro. No significant difference in the surface phenotype of ISC was found among heavy chain classes. Thus, non-neoplastic ISC show a spectrum of differentiation similar to that of myeloma cells, depending on the site where ISC are located, and on the degree of PBA in vivo.
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PMID:Analysis of surface antigen expression of human immunoglobulin-secreting cells: phenotypic heterogeneity in normal counterparts of myeloma cells. 260 19

Monoclonal antibodies to early (2H2.4, molecular weight 72,000 daltons) and late (2F3.0, molecular weight 68,000 daltons) antigens of the AD-169 strain of cytomegalovirus (CMV) were prepared by fusing mouse spleen cells with NS-1 mouse myeloma cells. The 2H2.4 monoclonal antibody produced a dense immunofluorescence with prominent lobular staining within the nucleus of CMV-infected substrate cells, whereas the reaction of 2F3.0 was more diffuse and generally involved the entire nucleus of the cells. Both monoclonal antibodies had little or no neutralizing activity against CMV in plaque-reduction assays. No cross-reactions were observed between these monoclonal antibodies and other members of the herpesvirus group. The 2H2.4 monoclonal antibody to early CMV antigen was used in a shell vial assay with a low-speed centrifugation step for the rapid (within 16 hours after inoculation) diagnosis of CMV infections. Optimal conditions for the test included centrifugation of shell vials at 700 X g for 45 minutes at 36 degrees C. An inoculum volume of 0.2 ml provided a reasonable balance between the optimal sensitivity for detecting specific viral fluorescence and the easy discrimination of the specific immunofluorescence from the background debris. Because of the commercial availability of the monoclonal antibody and the simplicity of the procedures used in the shell vial assay and subsequent fluorescence techniques, this rapid assay can be done in any laboratory that is familiar with cell culture manipulations.
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PMID:Monoclonal antibody for rapid laboratory detection of cytomegalovirus infections: characterization and diagnostic application. 299 72

Stimulated T lymphocytes and certain T-cell hybridomas secrete molecules capable of inducing B-lymphocyte proliferation and differentiation. It has been shown recently that one such B-cell stimulatory factor is associated with chondroitin sulphate proteoglycan (CSPG) and was designated T-cell proteoglycan fraction, or T-PGF. We report here that mouse spleen cells cultured at high densities or stimulated with lipopolysaccharide (LPS) at low cell densities secrete antibodies directed against T-PGF. Such antibodies react primarily with the CSPG component of T-PGF and can inhibit the induction of plaque-forming cells (PFC) by T-PGF. By fusing high-density cultures of unstimulated mouse spleen cells with the myeloma P3 x 63AG8.653, several anti-T-PGF (CSPG) hybridomas were derived that exhibited activities identical to anti-T-PGF (CSPG) obtained from high-density spleen cell culture supernatants. The role that these spontaneously secreted autoantibodies may play in immunoregulation is discussed.
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PMID:Naturally occurring mouse antibodies against T-cell-secreted chondroitin sulphate proteoglycan. 304 20

Hybrid cell lines producing monoclonal antibodies against Bacteroides forsythus or Wolinella recta were generated by fusion of SP2/0 or FO myeloma cells with splenocytes from Balb/c mice immunized with formalinized cells of B. forsythus FDC 331 or W. recta D13a-g, respectively. Enzyme-linked immunosorbent assays and indirect immunofluorescence tests were used to analyze the distribution of the recognized antigens on a panel of 70 strains representing 35 taxa, most of which are members of the oral flora. All monoclonal antibodies--eight against B. forsythus and six against W. recta--proved specific for the immunizing species. Four of the monoclonal antibodies against W. recta recognized antigens expressed by only some of the tested W. recta strains, thus confirming the earlier noted antigenic heterogeneity of this species. Antibody binding patterns consistent with those previously described or distinct for new serogroups could not, however, be observed. Four of the eight anti-B. forsythus monoclonal antibodies bound to only two of the three tested B. forsythus strains. All the remaining monoclonal antibodies detected every strain tested of the respective species against which they were raised. Preliminary results indicated that several of these antibodies should be very useful for the direct identification and quantification of these organisms in subgingival plaque.
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PMID:Production and characterization of monoclonal antibodies against Bacteroides forsythus and Wolinella recta. 317 Aug 94

We have established a monoclonal antibody (MoAb) AM34 (IgG1) which was prepared by a hybridoma constructed from fusion between murine myeloma cells and murine splenocytes. Crude amyloid proteins which were used as immunogen, were extracted from the kidney of a patient with rheumatoid arthritis by the distilled water method. This antibody strongly reacted with all 8 cases of secondary amyloidosis, but did not react or very weakly reacted with 17 tissue sections of primary or myeloma-associated amyloidosis. Other amyloid tissues did not give any positive reaction. Interestingly, 6 brain tissues of Alzheimer's disease clearly showed positive staining with this antibody, whereas two apparently normal brain tissues exhibited negative staining. Senile plaque cores, neurofibrillary tangles (weakly stained) and cerebrovascular amyloid in Alzheimer's disease were stained. Absorption of the MoAb AM34 with the crude amyloid proteins abolished the immunoreactivity of the MoAb AM34 not only with the kidney tissue section of the secondary amyloidosis, but also with the above mentioned portions of the brain in the case of Alzheimer's disease. Therefore, these immunohistological data suggest that the MoAb AM34 recognizes common epitope which exists in amyloid deposits of both secondary amyloidosis and Alzheimer's disease. An inhibition test on the kidney section showed that the reactivity of MoAb AM34 was not at all inhibited by the pretreatment of the section with 10 times higher concentration of anti-human amyloid A (AA) MoAb KM268 which was prepared against synthetic peptides of AA protein, suggesting that MoAb AM34 might react with amyloid-related protein other than AA protein. In addition, MoAb KM268 did not react with any lesions in Alzheimer's disease.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Detection of novel proteins associated with secondary amyloidosis and Alzheimer's disease by monoclonal antibody. 320 35

The plasma membranes of the cells of the superficial layer of the eye lens and the lens fibres are in close intercellular contact, leaving an intermembrane space of approximately 20 nm or less throughout their entire length. This plasma membrane is underlaid by a filamentous, cytoplasmic web containing actin, proteins of the spectrin and band 4.1 families, alpha-actinin and vinculin. Using immunofluorescence microscopy and immunoblotting of gel electrophoretically separated proteins, we show that plakoglobin, the plaque protein common to desmosomal and nondesmosomal adhering junctions, is present in lens cells and is also a component of the subplasmalemmal coat of these cells. Plakoglobin also exists in the extended regions of intercellular contacts between cultured lenticular cells where it often colocalizes with vinculin but does not occur in other vinculin-rich plasma membrane regions such as the focal adhesions at the ventral cell surface. Plakoglobin associated with plasma membrane regions can also be identified in various other adhesive cultured cells, but it is not detected in cells and tissues that do not establish firm intercellular junctions such as erythrocytes, platelets, cultured myeloma cells and smooth muscle tissue. We conclude that plakoglobin occurs, at least in lens cells, throughout the entire subplasmalemmal coat, coexisting in this situation not only with vinculin but also with spectrin and 4.1 protein(s). This colocalization infers the presence of a distinct, complex type of membrane-skeleton assembly involving the actin filament-associated junctional plaque elements plakoglobin and vinculin together with actin-associated proteins of the spectrin and band 4.1 protein families.
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PMID:Plakoglobin is a component of the filamentous subplasmalemmal coat of lens cells. 330 17

Phycocyanin is a phycobiliprotein with peak absorption at 620 nm. The laser activation, cytotoxic effects, and uptake into atherosclerotic plaque of phycocyanin was studied. Optimal activation was produced by argon dye laser at 0.5 W and a total energy dose of 300 J/cm2 at 620 nm and 650 nm, irradiated through blood with a hematocrit of 8%. Activation was evidenced by reduction of optical density by 0.3 units at 340 nm caused by oxidation of the reduced nicotinamide adenine dinucleotide phosphate (NADPH) in a buffered reaction solution containing 0.1 mg/ml of phycocyanin. Cytotoxicity was evaluated by measuring viability of mouse myeloma cells in culture after incubation with phycocyanin (0.25 mg/ml) and irradiated by 300 J/cm2 at 514 nm. After 72 hours post-treatment the cells showed 15% viability compared to 69% and 71% for control cells exposed to laser only or phycocyanin only, respectively. Atherosclerotic artery segments obtained within 5 hours postmortem were perfused with 0.1 mg/ml phycocyanin in oxygenated Krebs Ringer solution at 30 mm Hg for 5 minutes followed by washout with phycocyanin-free Krebs for 10 minutes. Artery sections examined histologically by light and fluorescence microscopy showed specific fluorescence localization within the plaque particularly at the elastic laminae and to a larger extent at the internal elastic lamina but not in the medial muscle layer. In conclusion, phycocyanin is a cytotoxic photosensitizer that exhibits specific binding to plaque and is activated at a wavelength minimally absorbed by blood. These properties suggest potential therapeutic use for plaque localization and regression.
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PMID:Phycocyanin: laser activation, cytotoxic effects, and uptake in human atherosclerotic plaque. 335 51

Because multiple myeloma is a malignancy that appears in aging humans, the murine plasmacytoma model was selected to investigate the association between tumor formation, age, and immunity. Plasmacytomas were induced in young, middle-aged, and old BALB/c mice by intraperitoneal injections of pristane. Old mice were more vulnerable than middle-aged mice who were more vulnerable than young mice to histopathologically documented plasmacytoma formation. The difference between old and young mice was significant (p less than .05). The increased frequency of plasmacytomas was associated with decreased in vitro immune parameters in pristane-treated mice compared with age-matched saline-treated controls. The decrease was especially marked with T cell responses (mitogenic responses to concanavalin A, phytohemagglutinin, or allogeneic spleen cells) and natural killer (NK) cell activity. It was less striking with the predominantly B-cell parameters of mitogenic response to lipopolysaccharide (LPS) and LPS-induced plaque-forming cells. These findings support the hypothesis that old mice have increased vulnerability to plasmacytoma formation because of diminished NK and T cell activities.
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PMID:Increased susceptibility of old mice to plasmacytoma induction. 348 87

A polypeptide of identical molecular mass (Mr 83,000) and charge to desmosomal plakoglobin from bovine snout epidermis was identified in soluble and pelletable fractions from diverse tissues and cells of different mammalian species, including cells and tissues devoid of desmosomes (e.g. endothelial, retinal, lenticular cells, fibroblasts). The protein, however, was not detected in erythrocytes and platelets and in myeloma cells, nor in smooth muscle tissue. In all cells examined, the plakoglobin soluble upon cell lysis in buffers of near-physiological pH and ionic strength (21-31% of the total plakoglobin in the different cell types) was found to exist in a distinct molecular form. On sucrose gradient centrifugation it appeared at about 7 S and gel filtration chromatography revealed a Stokes radius of about 5.0 nm, from which an Mr of about 170,000 was estimated. By using isoelectric focusing under non-denaturing conditions, soluble approximately equal to 7-S plakoglobin had an isoelectric point at about pH 5.3. The plaque-bound and the soluble form of plakoglobin were indistinguishable by electrical charge and molecular mass, regardless of the source, indicating molecular identity. Cross-linking of soluble proteins with cupric 1,10-phenanthroline resulted in the formaton of a cross-linked product of plakoglobin with similar physical properties as the native approximately equal to 7-S particle, which is compatible with the interpretation that the soluble plakoglobin particle is a dimer. While a major proportion of the plakoglobin in the desmosomal plaque was resistant to various extraction procedures, plakoglobin present in the plaques of non-desmosome-containing cells and tissues was readily extractable under low and high salt conditions. This indicates that differences exist in the binding of plakoglobin to desmosomal plaques and the plaques of non-demosomal junctions.
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PMID:Biochemical characterization of the soluble form of the junctional plaque protein, plakoglobin, from different cell types. 360 23


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