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)

After a comparison of anti-AFM1-BSA antibody responses between rat and mouse, the spleen cells of rat with stronger responses were chosen as parent cells for fusing with mouse myeloma cells P3X63-Ag8.653. Through HAT medium selection, RIA screening and cloning, five well growing rat-mouse hybridoma clones were obtained that could secret anti-AFM1 antibodies stably. The results from ELISA and competitive binding RIA further proved that the 5 McAbs are direct against AFM1, with significant cross reaction to its derivative, AFB1. The average affinity constant of the 5 McAbs is 10(9)-10(11) l/M. It signifies that these monoclonals have potential application value for the construction of AF detection kit.
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PMID:The establishment of rat-mouse hybridomas secreting anti-aflatoxin M1 antibodies and the properties of their monoclonal antibodies. 129 40

A monoclonal antibody (mAb) has been produced to aflatoxin B1 (AF B1) after successful immunization of mice and fusion of sensitized spleen cells with myeloma cancer cells. The mice were immunized with AF B1-oxime-protein conjugate. Positive mAbs were screened using an indirect ELISA specific for AF B1. The selected mAb was then developed in direct competitive ELISA and immunoaffinity column chromatography methods for aflatoxin detection in foods and feeds. Both assays are rapid, sensitive, specific and require only the minimum of sample preparation. Both immunological assays have now been commercialized and are produced in convenient ready-made kit formats.
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PMID:Aflatoxin monoclonals: academic development to commercial production. 136 50

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

A study of cancer risk among male employees at 241 livestock feed processing companies in Denmark was conducted on the basis of a data linkage system for detailed investigation of occupational cancer providing employment histories back until 1964, established at the Danish Cancer Registry. Crops imported for feed production have often been contaminated with highly variable concentrations of aflatoxins; an estimated average concentration of at least 140 micrograms aflatoxin B1 kg-1 prepared mixed cattle feed prevailed in the past, yielding a daily intake for workers via the respiratory route of approximately 170 ng. Risk was established on the basis of cancer cases among male workers, whose employment in one of the companies was the job they had held for the longest time since 1964. Elevated risks for liver cancer and for cancers of the biliary tract were observed, which increased by two- to three-fold significance after a 10-year latency. Exposure to aflatoxins in the imported crops was judged to be the most probable explanation for these findings, although the influence of lifestyle factors, e.g. alcohol consumption on the results cannot be fully disregarded. Increased risks for salivary gland tumours and multiple myeloma were also detected. However, due to multiple comparisons carried out in this study these new associations must await further confirmation. A decreased risk for lung cancer was observed; despite possible negative confounding due to the smoking habits of the employees, the lung does not seem to be a target organ for the carcinogenic effect of inhaled aflatoxins in humans.
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PMID:Cancer risk and occupational exposure to aflatoxins in Denmark. 317 93

Monoclonal antibodies specific for aflatoxin B1, aflatoxin B2, aflatoxin M1, and the major aflatoxin-DNA adducts were obtained following fusion of mouse SP-2 myeloma cells with spleen cells of mice immunized with aflatoxin B1 covalently bound to bovine gamma globulin. The aflatoxin-modified protein used to immunize mice was produced chemically by activating aflatoxin B1 to a 2,3-epoxide derivative, which then covalently bound to the protein. One of the monoclonal antibodies isolated (2B11) was found to be a high-affinity IgM antibody with an affinity constant for aflatoxin B1, aflatoxin B2, and aflatoxin M1 of about 1 X 10(9) liters per mol. In a competitive radioimmunoassay using [3H]aflatoxin B1, 3 pmol (1 ng) of aflatoxin B1, aflatoxin B2, or aflatoxin M1 caused 50% inhibition with this antibody. The antibody also had significant cross-reactivity for the major aflatoxin-DNA adducts: 2,3-dihydro-2-(N7-guanyl)-3-hydroxyaflatoxin B1 and 2,3-dihydro-2-(N5-formyl-2',5', 6'-triamino-4'oxo-N5-pyrimidyl)-3-hydroxyaflatoxin B1. The antibody was also covalently bound to Sepharose-4B and used in a column-based solid-phase immunosorbent assay system. Aflatoxins added in vitro to phosphate buffer, human urine, human serum, or human milk at levels expected to be obtained in human samples acquired from environmentally exposed individuals were quantitatively recovered by applying the mixture to this antibody affinity column purification system. Preliminary studies using urine samples from rats injected with radiolabeled aflatoxin B1 have also indicated that aflatoxin metabolites can be isolated by these methods. Furthermore, we have found that the monoclonal antibody affinity columns can be regenerated for multiple use. Therefore, the monoclonal antibodies and their application to affinity chromatography represents a useful and rapid technique to purify environmentally occurring levels of this carcinogen and some of its metabolites for quantitative measurements.
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PMID:High-affinity monoclonal antibodies for aflatoxins and their application to solid-phase immunoassays. 644 Jan 43

Monoclonal antibodies were obtained after fusion of mouse P3 X 63 myeloma cells with spleen cells isolated from BALB/c mice that had been immunized with aflatoxin B1-adducted DNA complexed with methylated bovine serum albumin. Selected hybridomas were found to produce monoclonal antibodies specific for aflatoxin B1-modified DNA containing both the 2,3-dihydro-2-(N7-guanyl)-3-hydroxyaflatoxin B1 and the putative 2,3-dihydro-2-(N5-formyl-2',5',6'-triamino-4'oxo-N5-pyrimidyl) -3-hydroxyaflatoxin B1, suggesting that these DNA adducts share a common antigenic determinant. The monoclonal antibody was not reactive towards the free aflatoxin B1-guanine adducts in solution, seven other aflatoxin derivatives, or benzo[a]pyrene-adducted DNA. A noncompetitive ultrasensitive enzyme radioimmunoassay could measure 15 fmol of aflatoxin B1-DNA adducts in 10 ng of DNA and was at least 100-fold more sensitive than the standard enzyme-linked immunosorbent assay. Competitive enzyme-linked immunosorbent assay with these monoclonal antibodies reliably quantitated aflatoxin B1 adducted in vivo to rat liver DNA at adduct levels of one aflatoxin B1 residue per 250,000 nucleotides. The competitive ultrasensitive enzyme radioimmunoassay was determined to be at least 6-fold more sensitive than the competitive enzyme-linked immunosorbent assay in analysis of aflatoxin B1-adducted DNA. Therefore, enzyme immunoassay using monoclonal antibodies will be useful analytical tools for studying both the molecular interactions of aflatoxin B1 with DNA and the occurrence of aflatoxin B1-DNA adducts in biological specimens from people exposed to this environmental carcinogen.
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PMID:Monoclonal antibody to aflatoxin B1-modified DNA detected by enzyme immunoassay. 679 29

Five monoclonal antibodies were obtained after fusion of mouse P3 x 63 myeloma cells with spleen cells isolated from BALB/c mice that had been immunized with aflatoxin B1-adducted DNA complexes with methylated bovine serum albumin. Selected hybridomas were found to produce monoclonal antibodies specific for modified DNA containing both the 2,3-dihydro-2-(N7-guanyl)-3-hydroxyaflatoxin B1 and the putative 2,3-dihydro-2-(N5-formyl-2',5',6'-triamino-4'-oxo-N5-pyrimidyl)-3-hydroxyaflatoxin B1, suggesting that these DNA adducts share a common antigenic determinant. Enzyme immunoassay conditions using these monoclonal antibodies were optimized, and DNA isolated from the livers of rats given dosages of aflatoxin B1 ranging from 0.01 to 1.0 mg aflatoxin B1 per kg body weight was tested. A level of modification in DNA of 1 aflatoxin B1 residue per 1,355,000 nucleotides can be quantitatively measured. Monoclonal antibodies will be useful probes for studying the molecular interactions of aflatoxin B1 with DNA and the occurrence of aflatoxin B1:DNA adducts in tissues and cells of humans exposed to this environmental carcinogen.
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PMID:Quantitation of aflatoxin B1-modified DNA using monoclonal antibodies. 680 38

Two hybridoma cell lines 1B5 and 2F1 capable of secreting specific monoclonal antibodies (McAbs) against aflatoxin B1 (AFT B1) were obtained. BALB/c mice were immunized by intrasplenic injection of AFT B1-human serum albumin conjugate (AFT B1-HSA) containing 9 AFT B1 residue per molecule. Spleen cells of BALB/c mouse with high serum antibody titer were fused with SP 2/0 myeloma cells in the presence of polyethylene glycol. Hybridoma cell lines were selected by using an indirect ELISA with AFT B1-keyhole limpet haemocyanin as coating antigen and grown as ascite tumour cells in BALB/c mice which previously had received an intraperitoneal injection with Freund's incomplete adjuvant. The McAbs were found to have strong reaction with AFT B1-bovine serum albumin conjugate (AFT B1-BSA) and no reaction with HSA or BSA. The reactivity of the McAbs with AFT analogs was determined by an indirect inhibition ELISA and the concentrations (ng/ml) required to inhibit 50 binding of McAb to AFT B1-BSA conjugate solid phase were AFT B1 4.0ng/ml, B2 36.9ng/ml, G1 23.3ng/ml and G2 403.3ng/ml for 1B5 McAb, and AFT B1 2.4ng/ml, B2 2.6ng/ml, G1 2.8ng/ml and G2 4.7ng/ml for 2F1 McAb.
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PMID:[Production and characterization of monoclonal antibody against aflatoxin B1]. 858 91

Five hybridoma cell lines producing monoclonal antibodies (MAb) against Aflatoxin B1 (AFB1) were established after fusion of mouse myeloma cells (SP-2/O-Ag-14) with spleen cells isolated from male BALB/c mice immunized with AFB1-BSA conjugate. Among these, one MAb, designated AFB1-2H8, was of the subtype IgG3 and the acidic fluid of which gave high dilution titers (1:5 x 10(5). The sensitivity of a competitive inhibition enzyme immunoassay (CIEIA) using AFB1-2H8 for AFB1 demonstrated that the linear range was 0.5-50 ng/ml and the minimum detectable concentration of AFB1 was 0.01 ng/ml. The specificity of the MAb was determined and showed no significant crossreaction with any of the metabolites tested. So th-- MAb and the CIEIA described may be useful in the detection of AFB1 in food and feed.
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PMID:Preparation and characterization of monoclonal antibodies against aflatoxin B1. 873 3

An improved enzyme-linked immunosorbent assay (ELISA) combined with monoclonal antibody (MAb) and one-step extraction method was established for the estimation of aflatoxin B1 (AFB1) in a peanut product. AFB1 was converted to AFB1-oxime, and then conjugated with bovine serum albumin (BSA). Spleen cells from mice immunized with AFB1-BSA conjugates were fused with myeloma cells. After double selection with AFB1-ovalbumin (OVA) and carbodiimide-modified OVA, five stable hybridoma cells secreting anti-AFB1 MAbs (AF1, AF 2, AF 3, AF 4, and AF5) were cloned. Using these anti-AFB1 MAbs, we developed the indirect competitive ELISA (cELISA) with alkaline phosphatase (ALP) - labeled sheep anti - mouse IgG as marker and the direct cELISA with AFBi-oxime horseradish peroxidase (POD) as marker.The minimum detectable limits of the indirect cELISA with AF 1, 2, 3, 4, and 5 were 5, 5, 5, 5, and 50 pg of standard AFB1 per assay, respectively, and those of the direct cELISA with AF 1, 3, 4, and 5 were 2.5, 5, 25, and 100 pg of standard AFB1 per assay, respectively. The cross reactivity of each toxins with these MAbs in the indirect cELISA was as follows: (a) AF 1 and AF 2 were reactive with AFB2 as well as AFB1, weakly with AFG2 > AFG1 > aflatoxicol II (COL II) > aflatoxicol I (COL I) and less weakly with other aflatoxins; (b) AF 3 and AF 4 were reactive with COL II as well as AFB1, weakly with COLI > AFQ1 and less weakly with others; (c) AF 5 was AFQ1 as well as AFB1 weakly with COL II > AFG2 > COL I and less weakly with others.The 60% aqueous methanol extracts of oil-roasted blanched peanuts ("butter peanut"), naturally contaminated with AFB1, were assayed by the direct cELISA without further purification. The direct cELISA with the most sensitive MAb AF 1 was allowed to determine 1 ng of AFB1 per g samples.
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PMID:A monoclonal antibody-based enzyme-linked immunosorbent assay of aflatoxin B1 in peanut products. 2360 61


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