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)

Till present the advantages of methacrylate embedded bone biopsies for the diagnosis of haemoblastic disorders have been somewhat restricted. This was a result of the impossibility to apply histochemical methods and other sensitive staining procedures to semithin sections. A routine method is described whereby enzyme activity, excellent fixation and good sectioning ability are retained. Fixation is carried out using 4% purified formaldehyde buffered in 0.1M sodium cacodylate. Dehydration is done with a water-miscible glycolmethacrylate. Naphthol-AS-D-chloroacetate esterase activity can be observed in granules of the entire neutropil cell lineage. By use of this method it becomes possible to demonstrate acid phosphatase activity and immunoglobulins in atypical plasma cells of multiple myeloma. A considerable decrease in processing time, as well as a preservation of enzyme activity during the postal mailing of fixed tissue samples from outside are further advantages.
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PMID:Histochemical and immunohistochemical techniques on acrylate embedded bone biopsies. 76 58

Four murine hybridoma clones secreting monoclonal antibodies (mAb) directed against lipopolysaccharide (LPS) antigen of S. newington, serogroup E1, were obtained after a fusion of spleen cells of mice immunized with formaldehyde-killed bacteria and mouse myeloma cells of the X63-Ag8.653 line. Antigen binding properties and specificity of the mAb were studied in bacterial agglutination tests, passive hemolysis and its inhibition, passive hemagglutination tests, passive hemolysis and its inhibition, passive hemagglutination and immunoenzyme tests (ELISA and immunoblotting). Three of the mAb (24E6, 29E1 and 45F6) were agglutinating and were active in all tests used, while mAb 31H12 did not agglutinate bacteria but revealed a high reactivity in the immunoenzyme reactions. It was found that the mAb reacted with LPS and Salmonella strains from serogroup E (E1, E2, E3 and E4) as well as from serogroups C (C1 and C4), F and S thus showing that the O3 antigen possesses more than one epitope, one of which is represented on the LPS antigens of the serovars from the cross-reacting groups mentioned. According to the known chemical the most probable recognized epitope consists of mannose with beta-linkage to the next monosaccharide residue in the LPS chain.
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PMID:Monoclonal antibodies directed to the O antigen of Salmonella serogroup E cross-react with lipopolysaccharides of Salmonella serogroups C, F and S. 128 92

Spleen cells from mice hyperimmunized with a keyhole limpet hemocyanin-tetrodotoxin-formaldehyde conjugate were fused with murine P3X63Ag8.653 myeloma cells. A single hybridoma clone was identified that secretes an IgG1,k monoclonal antibody (MAb), designated T20G10, against tetrodotoxin (TTX), with an estimated affinity of 1.2 x 10(8) L/M. Competitive inhibition enzyme immunoassays (CIEIAs) for detecting TTX were developed using this MAb. A direct CIEIA using alkaline phosphatase-labeled MAb detected TTX with sensitivities at IC50 and IC20 of 6-7 ng/ml and 2-3 ng/ml, respectively. The accuracy of the direct CIEIA was comparable with the high-performance liquid chromatography (HPLC) and the mouse bioassay systems, but the direct CIEIA exhibited greater sensitivity. The direct CIEIA was also more cost effective, as it required less sample preparation, a shorter assay time, and reduced investment in equipment than either of the other assay systems.
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PMID:A monoclonal antibody-based immunoassay for detecting tetrodotoxin in biological samples. 140 32

To investigate the role of employment history and workplace exposures as risk factors for multiple myeloma among women, a population-based case-control study using the Danish Cancer Registry data linkage system was conducted. All cases of myeloma diagnosed in Danish women between 1970 and 1984 (1,010 cases) and 4,040 age-matched women alive at the time of case-diagnosis were identified. Industrial histories from 1964 forward were obtained from the nationwide Pension Fund for 363 cases and 1,517 controls, and the most recent occupation on the tax record was available for 607 cases and 2,596 controls. Using industry/occupational-code combinations for the cases and controls who had industry employment, Danish industrial hygienists assessed the likelihood of exposure to 47 workplace substances. An increased myeloma risk (odds ratio [OR] = 1.2, 95 percent confidence interval [CI] = 1.0-1.5) was seen for women not in the Pension Fund, but who had an occupational title coded as 'Mrs/homemaker.' Nonsignificantly elevated risks of 1.3 or greater were observed for employment in: production of agricultural products; orchards/nurseries; spinning/weaving; other textile and plastics manufacturing; hotel, entertainment, and social services industries. Elevated, but nonsignificant risks were observed for possible and probable exposure to exhaust fumes, formaldehyde, wood dust, animals or animal products, and pesticides. The strongest association with myeloma was employment in the agricultural industry (OR = 1.5, CI = 0.8-2.8), however, the number of women who worked on family farms was unknown and could not be included in this risk estimate.
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PMID:Multiple myeloma among Danish women: employment history and workplace exposures. 152 23

The development of the hybridoma technology allows the identification of tumor associated antigens with monoclonal antibodies (mAbs). Employing this technology mAb Due ABC 3 was obtained by immunization of a BALB/c mouse with bladder tumor cell line SW 1710 and subsequent cell fusion of spleen cells with P3. X63.Ag8.653 mouse myeloma cells. MAb Due ABC 3, an IgM antibody, was found to recognize an antigen present in the membrane of tumor cells in 25 out of 28 (89%) transitional cell carcinoma specimens but rarely (three out of 25 specimens, 12%) on normal urothelial cells. Cross reactions were seen with proximal tubular epithelium of the kidney and seven out of 12 renal cell carcinomas examined. Furthermore, the antigen was expressed by granulocytes, some gastrointestinal epithelia, ovarian and breast carcinoma. The antigen recognized by mAb Due ABC 3 was stable to fixation with formaldehyde and paraffin emmbedding, different proteases, alkaline treatment and heat exposure up to 70C. Antigenicity was abandoned by incubation with periodate but not with neuraminidase treatment. The antigen could be extracted with chloroform/methanol suggesting the involvement of a glycolipid. Immuno-thin layer chromatography revealed a single lipid band reacting with mAb Due ABC 3 but not with anti-CD15, directed against the Lewis X antigen. Although not tumor-specific, mAbs directed against differentiation antigens may be of value for the investigation of cell transformations as well as for diagnostic use.
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PMID:Monoclonal antibody Due ABC 3 directed against transitional cell carcinoma. I. Production, specificity analysis, and preliminary characterization of the antigen. 172 39

Six hybridomas that produce monoclonal antibodies to different antigenic determinants of heterogeneous pig IgG and of pig anti-Dnp antibodies were obtained by fusion between spleen cells from BALB/c mice immunized with non-specific pig IgG and the myeloma line P3-X63-Ag8.653. Antigenic determinants which correspond to individual monoclonal antibodies were located in the individual domains of the IgG molecule by investigating the interaction of monoclonal antibodies with Fab, Fc, and pFc' fragments and with kappa, lambda, and gamma polypeptide chains. To evaluate the interaction, a quantitative equilibrium competitive radioimmunoassay was developed and [14C]formaldehyde-labelled non-specific pig IgG served as labelled antigen. Antibodies PGG-01, PGG-04, and PGG-06 were shown to be directed against determinants in the C lambda domain, antibody PGG-03 very probably against the determinant in the C chi domain, and antibodies PGG-02 and PGG-05 against determinants in the CH3 domain. Antibodies PGG-02 and PGG-05 are highly selective for IgG subpopulations; when combined, they interact with no more than 42% of the heterogeneous IgG population. These two antibodies can be used as a basis for preparing a complete set of reagents for identification of individual subclasses.
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PMID:Limited enzymatic cleavage of pig immunoglobulin and of specific antibodies. V. Monoclonal antibodies to individual fragments and polypeptide chains. 243 58

A 65-kDa estrogen receptor (ER) protein has been demonstrated both by sucrose gradient analysis and by immunoblot, using anti-ER monoclonal antibodies (MAbs). Since the ER is denatured in many experimental situations, such as formaldehyde fixing of samples for histochemistry and electroimmunoblotting studies, in this work we used a denatured 60-70-kDa ER-rich protein preparation as antigen for mice immunization in order to raise anti-ER MAbs. That material was obtained by affinity purification on an allyl-estradiol matrix of the MCF-7 cytosolic ER, followed by further isolation and enrichment by PAGE. NS-1 myeloma cells and spleen lymphocytes from the immunized mice were fused, and resultant hybridoma colonies were screened by [125I]-estradiol-labelled nuclear ER immunoprecipitation. The isolated MAb, E476, shows a moderate ability to precipitate ER and reacts strongly with a 46-kDa antigen in Western blot assay. The 46-kDa antigen was not detectable in native cytosol but became reactive after 50% ammonium sulfate precipitation of cytosolic proteins. The 46-kDa antigen appeared concentrated in the NaSCN plus estradiol eluate of the affinity column used for cytosolic ER purification. Freshly prepared 60-70-kDa material from the preparative gel electrophoresis did not show any E476 reactivity. However, when the 60-70-kDa proteins were frozen, thawed and speed vacuum concentrated, the 46-kDa antigen became detectable. Storage increased the reactivity of the 60-70-kDa material with the E476 MAb. The 46-kDa antigen was present only in the ER positive cell lines, and was absent in all negative cell lines tested. The 46-kDa protein is also present in the ER positive human breast cancer specimens. We conclude that the 46-kDa protein identified with the E476 MAb in human breast cancer is probably a naturally occurring ER fragment.
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PMID:A 46-kDa antigen associated with estrogen receptor in human breast cancer. 338 60

We have recently demonstrated that one of our monoclonal antibodies (MAB's) to glial fibrillary acidic protein (GFAP) recognizes an epitope on this molecule which is to a large degree blocked during fixation with formaldehyde or crosslinking with Dithiobis (Succinimidyl) Propionate (DTSP). This was shown to be due to the crossbinding of a single or a number of proteins to the GFAP and is not due to a change in the epitope on GFAP induced by the fixation itself. In an attempt to produce further MAB's capable of recognizing epitopes on the GFAP molecule available following formaldehyde fixation, we immunized BALB-C mice with cytoskeletal preparations of human glioma cells which contain GFAP where the blocking protein or proteins were crossbound by DTSP or formaldehyde to the GFAP. Following fusion of the spleen lymphocytes to Sp 2/0 myeloma cells we have cloned hybridomas which produce antibodies that recognize GFAP in formaldehyde fixed tissues. This method presents the antigen in its native "fixed" state for the mouse's immune system and avoids the production of MAB's which (although excellent for immunochemical studies) do not recognize any epitopes available on the molecule in question in formaldehyde fixed tissues. Antibodies so produced are of great interest in routine pathology where most tissues are still, unfortunately, undiscriminately fixed in formalin. The results also show that GFAP varies immunologically in different species (i.e. human v. rat/mouse) and confirm that the GFAP of the PNS is immunologically distinct and/or associated with different proteins from that found in the CNS.
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PMID:Monoclonal antibodies to GFAP epitopes available in formaldehyde fixed tissue. 354 74

Monoclonal antibodies (mabs) have been raised against human transthyretin (hTTR). The protein was isolated by an affinity chromatography procedure using Sepharose-hRBP and BALB/c mice were immunized. Following fusion with SP 2/0 myeloma cells, 26 single cell clones producing antibodies against hTTR were isolated. These mabs have been characterized and efforts have been made to establish the epitopes that they recognize. So far at least two different epitopes have been identified both residing in a mid-region fragment corresponding to the amino acid sequence 35-103 of the hTTR subunit. All mabs have been found suitable for immunohistochemical localization of hTTR even in formaldehyde fixed and paraffin embedded tissues.
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PMID:Monoclonal antibodies to transthyretin. 379 88

A retrospective cohort study was performed on a group of 664 male workers employed for at least one month during the period 1942-1979 in a chemical factory. Both established and suspected carcinogens had been handled in the plant, primarily piperazine, but also urethane, ethylene oxide, formaldehyde, and organic solvents. A significantly increased mortality, compared with the regional death rate, was observed in the cohort. The increase was mainly due to violent deaths and cardiovascular diseases. No rise in death rates was observed for asthma, bronchitis or emphysema, in spite of other evidence of a high risk of occupational asthma, due to exposure to piperazine. A statistically significant increase in cancer morbidity was observed for malignant lymphoma/myelomatosis when an induction latency time of at least 10 years was used. Furthermore, an increase in bronchial cancer was noted, but it was statistically significant only when an induction-latency time of at least 15 years was used. A case-referent study within the cohort did not reveal any significant association between any specific chemical exposure and cancer morbidity.
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PMID:Mortality and cancer morbidity among workers in a chemical factory. 382 3


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