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 survival of individual patients with multiple myeloma ranging from a few weeks to several years, careful pretreatment evaluation of prognostic factors is extremely important. Several methods of stratification are available, but in spite of their validity they present a number of problems, particularly with regard to their inter-reproducibility. In addition, they are of no help to evaluate response to chemotherapy, quality of remission, plateau phase or kinetics of relapse. Recent studies have clearly demonstrated that serum beta-2 microglobulin, as a single variable, is the best individual determinant as a prognostic marker in multiple myeloma. Using this assay and serum albumin as prognostic determinants, a simple stratification, superior to the three previously available methods, was developed. Serum beta-2 microglobulin is a very useful marker in the follow-up of most multiple myeloma patients. It appears to be a key measurement for assessing the prognosis and response to treatment of these patients.
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PMID:[Role of the assay of serum beta 2 microglobulin in the clinical evaluation of myeloma]. 294 32

The beta-adrenergic antagonist propranolol was activated through its side chain, coupled to bovine serum albumin, and injected into BALB/c mice. After fusion of the splenocytes from these immunized mice with the NS-1 myeloma cell line, two hybridomas, producing monoclonal anti-propranolol antibodies, were isolated. Clone P-49 was monospecific for propranolol, with a significant preference for the 1-stereoisomer, as compared to the d form. On the other hand, clone P-28 cross-reacted with alprenolol as well as some other beta-antagonists. Both classes of antibodies competed with A431 epidermoid carcinoma beta 2-adrenoceptors for the binding of [3H]propranolol. When ascites cells from clone P-28 were fixed with glutaraldehyde, the anti-propranolol monoclonal antibody became cell bound. These cell-bound P-28 antibodies bind propranolol and other beta-adrenergic ligands with a similar ranking order to the soluble monoclonal antibody. The cell-bound antibody displayed a 5-fold higher affinity towards 1-propranolol than the soluble monoclonal antibody. The practical implications of these findings are discussed.
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PMID:Stereospecific antibodies to propranolol. 300 17

The secretion of immunoglobulin (Ig) from cultured mononuclear cells by lipopolysaccharide (LPS) stimulation is inhibited by monoclonal nonspecific suppressor factor (MNSF), a lymphokine produced by murine T cell hybridoma. In an attempt to develop a murine monoclonal antibody (MAb) with specific reactivity against MNSF, a cell fusion technique that incorporated immune murine splenocytes and HAT-sensitive murine myeloma cells was used. Cross-reactivity experiments confirmed that the MAb (MO6) does not bind to unrelated proteins such as bovine serum albumin, mouse IgG, and murine interferon-gamma (IFN-gamma). There are no effects when anti-IFN-gamma antibodies are used with MNSF. As far as biological activity is concerned, MO6 inhibits in vitro the activity of MNSF in terms of the Ig secretion from cultured lymphocytes. By using MO6, affinity chromatography and immunoblotting were performed. The MNSF on the SDS-PAGE showed a band with m.w. of approximately 70,000, indicating the formation of an aggregate in saline; but after treatment with 0.4 M pyridine-acetic acid buffer, separate bands of 24,000 and 16,000 daltons were evident. Therefore MO6 recognizes 70,000 and both 24,000 and 16,000 daltons. Thus we confirmed by using this MAb and affinity chromatography, the existence of human counterpart, human nonspecific suppressor factor (hNSF), in supernatant from concanavalin A-stimulated T cells. When hNSF was fractionated by high pressure liquid chromatography (HPLC), the activity was found in a region corresponding to 70,000 daltons. However, when fractionated in pyridine-acetic acid buffer, hNSF activity was distributed in a slightly wider range of 15,000 to 30,000 daltons. Physicochemical analysis showed that the purified hNSF is resistant to either heating at 56 degrees C or to 2-mercaptoethanol treatment; however, it is labile to acidification at pH 2.0 and is also sensitive to protease treatment, the characteristics of which were similar to those of murine MNSF. Thus MO6 was confirmed to be a pertinent tool for isolation of hNSF, as well as for murine MNSF.
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PMID:Characterization of monoclonal nonspecific suppressor factor (MNSF) with the use of a monoclonal antibody. 310

A number of polyclonal antibodies specific for DNA modified with (+/-)trans-7,8-dihydroxy-anti-9,10-epoxy-7,8,9,10-tetrahydrobenzo[a]pyre ne (BPDE) were obtained from the sera of New Zealand white rabbits immunized with BPDE-DNA, complexed with methylated bovine serum albumin (mBSA). Monoclonal antibodies were developed by fusion of mouse myeloma cells with spleen cells isolated from BALB/c mice immunized with the same complex of BPDE-DNA and mBSA. These antibodies have been characterized for specificity in a highly sensitive, enzyme-linked immunosorbent assay (ELISA). All antibodies showed a very high affinity for single-stranded BPDE-DNA, but had lower affinity towards native BPDE-DNA. The affinity for the free mononucleoside BPDE-dG was at least 100-fold lower than that for BPDE-DNA, and no affinity was detected for BP tetrols or DNA modified with N-acetoxy-N-acetyl-2-aminofluorene. A high cross reactivity was observed with DNA modified with (+/-)-trans-1,2-dihydroxy-anti-3,4-epoxy-1,2,3,4-tetrahydrochrysene++ +. Using five different antibodies, monoclonal or polyclonal, we observed that the antibody affinity for BPDE-DNA was dependent on the level of modification; in the competitive ELISA as little as 4 fmol BPDE-DNA (50 pmol/micrograms) was sufficient for 50% inhibition with our best antisera, but 17 fmol of the adduct was required when [3H]BPDE-DNA of low modification (1-10 fmol/micrograms) was used as inhibitor. When samples of [3H]BP-DNA isolated from the livers of mice, treated i.p. with different doses of [3H]BP were examined by competitive ELISA and calibrated with [3H]BPDE-DNA of low modification (1-10 fmol/micrograms), binding values calculated from the immunoassay were in good agreement with those obtained from radioactivity measurements. In contrast, when this DNA was quantitated in competitive ELISA using highly modified BPDE-DNA as standards, values by ELISA were 20-40% of those obtained by radioactivity. These results indicate that the use of serially diluted BPDE-DNA of high modification as standard competitor in the ELISA will lead to erroneous results in the measurement of adducts in DNAs modified to a low extent (biological samples). The property of antisera specific for BP-DNA, recognizing highly modified DNA more efficiently than DNA modified to a low extent, may be common to all antisera elicited against highly modified DNA immunogens. Therefore we conclude that antibody affinity must be tested also with DNA samples of low modification, obtained either in vitro or in vivo.
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PMID:The binding efficiency of polyclonal and monoclonal antibodies to DNA modified with benzo[a]pyrene diol epoxide is dependent on the level of modification. Implications for quantitation of benzo[a]pyrene-DNA adducts in vivo. 311 53

To investigate the direct toxicity of human Bence Jones protein (BJP), individual nephrons of male Sprague-Dawley rats were perfused in vivo at 20 nl/min with an artificial tubule fluid (ATF) that contained no protein, a human kappa BJP (5 g/dl), or bovine serum albumin (5 g/dl), and proximal convoluted tubule function and morphology were examined. Perfusion with BJP perfusate for less than or equal to 5 minutes produced no changes (P = NS) in absorption of water, Jv, (1.09 +/- 0.20 vs. 1.50 +/- 0.25 nl/min/mm), chloride, JCl, (95 +/- 47 vs. 123 +/- 41 pEq/min/mm), and glucose, JG, (39 +/- 3 vs. 40 +/- 5 pmol/min/mm) compared to perfusions with only ATF. However, perfusion for at least 20 minutes with the same BJP perfusate produced decreased (P less than 0.025) in Jv (0.58 +/- 0.12 vs. 1.15 +/- 0.14 nl/min/mm) and JG (27 +/- 3 vs. 38 +/- 3 pmol/min/mm) compared to perfusions with ATF alone; the decrease in JCl (64 +/- 47 vs. 119 +/- 27 pEq/min/mm) did not reach statistical significance. Perfusion for 20 minutes with ATF containing albumin resulted in no changes in Jv (1.22 +/- 0.21 vs. 1.15 +/- 0.14 nl/min/mm), JCl (207 +/- 29 vs. 119 +/- 27 pEq/min/mm), and JG (31 +/- 1 vs. 38 +/- 3 pmol/min/mm), when compared to the ATF perfusions. Immunocytochemistry, immunofluorescence and immunoelectron microscopy of the BJP-perfused tubules demonstrated the kappa light-chain protein in endosomes and activated lysosomes. In addition, cellular desquamation and fragmentation, prominent cytoplasmic vacuolation, and focal loss of the microvillus border were found in the BJP-perfused tubules, but not in the albumin-perfused tubules. In conclusion, these functional and morphologic data show that a human kappa light-chain is toxic to the proximal convoluted tubule of the rat. This toxicity occurred in a time-dependent fashion when the lysosomal system was markedly activated. Direct damage of the tubule epithelium by BJP's may be involved in the development of the tubulointerstitial nephropathy associated with multiple myeloma.
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PMID:Human Bence Jones protein toxicity in rat proximal tubule epithelium in vivo. 312 60

Two monoclonal antibodies (6A10 and 12F5) were obtained after fusion of mouse P3X63-AG.8.653 myeloma cells with spleen cells isolated from BALB/c mice immunized with imidazole ring-opened aflatoxin B1 (AFB1)-DNA and characterized by competitive enzyme-linked immunosorbent assays. Both antibodies are highly specific for imidazole ring opened AFB1-DNA and show some cross-reactivity with AFB1-DNA and no cross-reactivity with 8,9-dihydro-8-(7-guanyl)-9-hydroxy-AFB1, AFB1 conjugated with bovine serum albumin, aflatoxin M1 conjugated with bovine serum albumin, AFB1, or aflatoxin G1. Antibody 6A10 was further characterized and showed no cross-reactivity with DNA modified by several other carcinogens. It could detect adducts with 4-fold higher sensitivity in highly modified DNA (2.5 adducts/100 nucleotides) than in low modified DNA (4 adducts/10(5) nucleotides). With low modified DNA the limit of sensitivity is 5 adducts/10(7) nucleotides. Antibody 6A10 reliably detected adducts formed in vivo in rats and mice treated with AFB1. In a pilot study, AFB1 adducts were detected in liver tissues from individuals living in areas with suspected exposure to AFB1. Monitoring adduct levels in human tissue may provide information not only on carcinogen exposure but also on the relationship among infection with hepatitis B virus, dietary exposure to aflatoxin B1, and liver cancer.
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PMID:Immunological detection of aflatoxin B1-DNA adducts formed in vivo. 314 Oct 43

We have prepared 16 anti-bilirubin monoclonal antibodies and described their unique reactivity to bilirubin and related compounds. Using the modified mixed anhydride method, bilirubin was covalently coupled to bovine serum albumin. We performed somatic cell fusion between murine spleen cells immunized with this bilirubin-albumin complex and murine myeloma P3-X63-Ag8-U1 cells. After screening assays, 16 clones were identified which were producing antibodies not to albumin but to haptenic bilirubin. In inhibition analysis, the antibodies in the culture supernatants cross-reacted with bilirubin glucuronides to varying degrees, but rarely reacted with structurally related biliverdin, hemin, and azodipyrroles of bilirubin. Albumin, when present in the solution, much reduced the reactivity of several monoclonal antibodies to unconjugated bilirubin, and this effect was partly reversed by addition of salicylate which dissociates the binding between bilirubin and albumin.
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PMID:Anti-bilirubin monoclonal antibody. I. Preparation and properties of monoclonal antibodies to covalently coupled bilirubin-albumin. 319 Nov 53

A monoclonal antibody was obtained by the fusion of mouse myeloma cells with splenocytes isolated from Balb/c mice, which had been immunized with diacetoxyscirpenol-hemiglutarate (DAS-hemiglutarate) and verrucarol-hemiglutarates covalently bound to ethylenediamine-modified bovine serum albumin. The anti-DAS-antibody that could be induced was of the IgM type with kappa-chains. The titer of the monoclonal anti-DAS-antibody in ascites fluid obtained from mice injected the selected cell line was much higher than those of conventional antisera. An enzyme-linked immunosorbent assay based on the competitive binding principle in which the antibody was applied had a sensitivity of 1 ng DAS per assay. The relative cross-reactivity of the monoclonal antibody in the CI-ELISA with the related trichothecenes such as triacetoxyscirpenol, 15-monoacetoxyscirpenol, diacetylverrucarol, 4-monoacetoxyscirpenol and scirpentriol were found to be 1.8, 0.8, 0.15, 0.02 and less than 0.001, respectively. The trichothecenes verrucarol, T-2 toxin, T-2 tetraol, deoxynivalenol, 3-acetyldeoxynivalenol and trichothecin showed no cross-reactivity.
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PMID:Production and characterization of a monoclonal antibody to the trichothecene mycotoxin diacetoxyscirpenol. 320 55

Monoclonal antibodies have been raised against components of glomerular immune deposits in experimental glomerulonephritis and idiopathic human glomerulonephritis. An accelerated model of chronic serum sickness in the rat using cationized human serum albumin was employed to obtain renal tissue with capillary loop and mesangial immune deposits. Mice were immunized with isolated rat glomeruli or a preparation of glomerular basement membrane and mouse spleen cells fused with myeloma cells. Anti-human serum albumin monoclonal antibodies were produced from all technically successful fusions irrespective of the size of the deposits in the immunizing tissue or whether whole glomeruli or glomerular basement membrane were used for immunization. Monoclonal antibodies were then produced following immunization with tissue from postmortem human kidneys with idiopathic membranous and mesangiocapillary glomerulonephritis. Sixteen monoclonal antibodies, apparently reactive with glomerular immune deposits, were cloned; most of these were reactive with components of the complement system including a previously undescribed complement-related protein. These studies demonstrate that monoclonal antibody technology may be useful in determining the identity of antigen and non-antigen components of glomerular immune deposits.
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PMID:Identification of the components of glomerular immune deposits using monoclonal antibodies. 321 90

Monoclonal antibodies (MAbs) against HLA antigens can give better information about the serology and biochemistry of the human major histocompatibility complex (MHC) than HLA antisera obtained from pregnant women. To increase the very limited panel of MAbs against HLA we immunized mice with human cultured cell lines and fused their spleen cells with the Ag8-653 myeloma. We produced MAbs against HLA-A1, A2/w69, A2/28, A2/11/25/26/28/29/30/31/33/34, A25/32, B7/22, and B13. The best dilution medium to store the MAbs in Terasaki plates was RPMI 1640 supplemented with 7% bovine serum albumin. The MAbs are also excellent reagents to investigate public HLA antigens and to stain HLA antigens in cryosections of transplanted organs.
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PMID:Production and applications of new monoclonal antibodies against human lymphocyte antigen-A and -B antigens. 321 87


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