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)

An autopsy case of IgE myeloma, 85-year-old male is reported. He was admitted to our hospital on November 17, 1987 due to pain of left humerus. Osteolytic and osteoporotic foci were found in left humerus, ribs, spinal column and femurs. Complete blood countings were as follows: RBC 3.23 x 10(12)/L, Hb 11.3 g/dl, WBC 6.3 x 10(9)/L, platelet 173 x 10(9)/L. Blood smear showed red cell rouleaux formation without myeloma cells. Examination of bone marrow revealed hypoplasia with 52% myeloma cells which were stained with anti-IgE and antilambda antisera by peroxidase anti-peroxidase method. Total serum protein level was 7.7 g/dl. Monoclonal protein was observed at fast gamma-region by cellulose-acetate electrophoresis. On immunoelectrophoresis, this monoclonal protein made specific M-bow against anti-IgE and anti-lambda antisera. The IgE level in serum and urine were 7.8 x 10(6) IU/ml and 2.4 x 10(3) IU/ml by radio-immunoassay respectively. He was died owing to renal failure on September 7, 1988. Postmortem examination showed infiltration of myeloma cells in bone marrow, spleen, kidneys, lungs and generalized lymph nodes.
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PMID:[An autopsy case of IgE myeloma]. 250

Monoclonal antibodies were generated by immunizing rats with mouse bladder carcinomas, fusing their spleen cells with NS-1 myeloma cells and selecting for antibodies that bound to mouse bladder carcinomas. One of the antibodies, IG5, recognizes an antigenic determinant which is present in mouse bladder carcinoma cytoskeletons and is not detectable in the normal bladder epithelium. Indirect immunofluorescence studies revealed that the antigen is expressed intracellularly and is organized in the form of filamentous arrays. The antigen was detected by peroxidase--antiperoxidase immunocytochemistry in stratified epithelia and glands derived from these, but has not been observed in any tissues of mesenchymal or neuronal origin. Various normal and neoplastic human tissues were subsequently tested for reactivity with antibody IG5. Antigen expression in normal tissues was similar to that in the mouse. Most carcinomas of the bladder and lung were stained, while all of eleven colon carcinomas were negative. Antibody IG5 immunoprecipitated radio-iodinated peptides of 58, 56, 52 and 43 kD molecular weight from mouse bladder carcinomas. Western blotting experiments with antibody IG5 demonstrated bands of 56 and 50 kD in a keratin-enriched fraction of the bladder carcinoma cytoskeleton. Antibody IG5 reacted with molecules which have several properties typical of cytoskeletal keratin peptides. Our findings are discussed in the context of previously described keratin peptides and relevant monoclonal antibodies.
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PMID:A monoclonal antibody recognizing cytoskeletal keratins of stratified epithelia and bladder carcinomas. 257 32

Plastic embedding of bone core biopsy specimens has been promoted as providing superior morphology, primarily because semi-thin sections can thereby be cut at 1-2 mu. The major disadvantages of plastic embedding are that it increases the technical load, is more expensive, and potentially has its own intrinsic problems, including difficulties in performing special stains and immunoperoxidase studies. In order to investigate the possibility that semi-thin paraffin sections may provide similar morphological results without the intrinsic disadvantages of plastic sections, we examined 45 bone core biopsy specimens that were sufficiently large to process one half in plastic and the other half in paraffin following decalcification. Both were cut at 1-2 mu. Although many plastic sections appear esthetically more pleasing, semi-thin paraffin sections of very high quality can also be obtained routinely. Additional advantages of paraffin sections were the ability to perform peroxidase studies, lower cost, less technologist time, and avoidance of problems occasionally arising with plastic, such as difficulties with impregnation or problems with polymerization. Peroxidase studies were particularly useful in patients with possible myeloma that was not overt on hematoxylin-and-eosin section and in confirming the presence or source of metastatic carcinoma. We therefore recommend the use of semi-thin (1-2 mu) paraffin sections for routine examination of bone core biopsy specimens.
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PMID:Bone core biopsies. Plastic or paraffin? 218 39

We report a novel way of obtaining a monoclonal antibody to renal cell carcinoma (RCC). BALB/c mice were immunized with RCC cells (ACHN, ATCC CRL1611) and hyperimmunized spleen cells were fused with Sp/2 murine myeloma cell line by PEG 2000. Many hybridoma supernatants were screened by enzyme linked immunosorbent assay (ELISA). After the cloning by limiting dilution, we established a hybridoma reactive to RCCs and named it A25. It belonged to the IgG1 subclass of immunoglobulins. According to our results using ELISA, 4 of 5 RCC cell lines were reactive to A25, while the remaining 23 non RCC cell lines did not react. The supernatant from A25 was used as a primary antibody preparation for avidin-biotin complex immuno peroxidase staining of multiple cases of RCC, normal tissue, and other tumors. This antibody reacted with 3 of 3 grade 1 RCC, 10 of 11 grade 2 RCC and 0 of 3 grade 3 RCC. Proximal tubules of the kidney shared this antigen. However, cross reactivity of this antibody was observed to pyloric glands of the stomach and adenocarcinoma of the colon. The epitope of A25 seemed to originate from normal kidney tubules. Low grade tumors preserved this epitope well, but this character of the original tissue seemed to disappear as tumor grade increased.
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PMID:[Production of monoclonal antibody to renal cell carcinoma]. 267 65

A human monoclonal antibody termed HMST-1 was produced by fusing lymphocytes from segments of human pelvic lymph nodes from an endometrial cancer patient with murine myeloma cells. The epitope recognized by HMST-1 was determined to be lacto-series type 1 chain-containing glycosphingolipid (Gal beta 1-3GlcNAc beta 1-3Gal beta 1-4Glc beta 1-1Cer) by isolating the antigen from endometrial cancer cell line SNG-II and analyzing with fast atom bombardment mass spectrometry, permethylation analysis, and exoglycosidase treatment. By the immunohistochemical avidin-biotin-peroxidase complex method, no normal endometrium and benign endometrial hyperplasia were stained with HMST-1, but HMST-1 reacted with about 35% of endometrial cancer cases. These facts indicate that the rate of expression of the antigen increases along with the course of malignancy in the endometrium. By sialidase treatment of the section, the positive rate increased to 57% in endometrial cancers and to 13% in normal endometrium, indicating that the antigen was masked with sialic acid and exposed by neuraminidase treatment. Immunohistochemistry also revealed that the antibody reacted with human fetal alimentary tract epithelium and mesothelium, indicating the oncodevelopmental nature of Gal beta 1-3GlcNAc beta 1-3Gal beta 1-4Glc beta 1-1Cer.
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PMID:Human monoclonal antibody (HMST-1) against lacto-series type 1 chain and expression of the chain in uterine endometrial cancers. 268 63

To identify tumor-associated antigens immunogenic to man, human monoclonal antibodies (MAbs) were generated by fusing regional lymph node lymphocytes (LNLs) of each of three colon adenocarcinoma patients with the M5 mouse myeloma cell line. Heterohybridomas in 19 wells secreted human immunoglobulin (Ig) for at least 60 days. To identify immunoreactive MAbs, we devised an immunohistochemical assay with xenografts of six colon tumors. Binding was visualized with a biotin-conjugated goat antihuman Ig antibody followed by an avidin-biotin-peroxidase complex. This assay detected binding with a sensitivity of 0.5 microgram/ml human Ig. Reactivity against tumor-associated antigens (TAAs) in frozen sections of the colon xenografts was detected in 14 of the 19 supernates. However, only nine (three IgGs, five IgMs and one IgA) were reactive against formalin-fixed sections, showing that formalin-fixation destroyed some but not all antigenicity. Four MAbs were cloned and tested against the entire panel of 19 xenografts. One IgM MAb reacted only against colon carcinomas, while the other three (one each of IgA, IgG and IgM) had broader reactivities. Three of the four human MAbs did not cross-react with melanomas. In summary, human regional lymph nodes contain a high proportion of B lymphocytes sensitized to the autochthonous tumor. Immunostaining of human colon tumor xenografts can readily identify human MAbs reactive with colon carcinomas.
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PMID:Human monoclonal antibodies reactive with colon carcinoma: identification by a novel screening procedure with xenografts. 271 74

There are inherent technical difficulties in measuring IgG rheumatoid factor (IgG-RF) in the serum of patients with rheumatoid arthritis (RA). These arise from measuring a reaction between two IgG molecules and the interference of IgM-RF in the reaction. We compared the prevalence of IgG-RF in whole sera and purified IgG fractions from 58 RA patients (43 of whom were latex or sheep cell agglutination positive). Methods of purification were: ammonium sulphate precipitation and DEAE cellulose or protein A-Sepharose chromatography. IgG-RF was measured by two methods: (1) radioimmunoassay and ELISA with a monoclonal myeloma IgG (IgG4,K) as the antigen and radiolabelled rabbit anti-human IgG (previously absorbed on a column with IgG4,K) as the second antibody; (2) ELISA using rabbit IgG as the antigen and a peroxidase conjugated goat anti-human IgG as the second antibody. When whole sera were assayed, 18 (31%) contained IgG-RF. In contrast, only three of the IgG fractions (5%) were positive for IgG-RF by all methods, while the remainder were uniformly negative. These results suggest that IgG-RF determination in whole sera does not accurately reflect IgG-RF activity.
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PMID:IgG rheumatoid factor in purified IgG fractions and whole sera from patients with rheumatoid arthritis. 273 Sep 84

Two monoclonal antibodies, designated 4C4 and 4G1, were produced by immunization of BALB/c mice with a human esophageal carcinoma cell line, CE69T/VGH, followed by fusion of the spleen cells from an immunized mouse with myeloma cells NS-1. 4C4 showed strong binding activity to three human esophageal carcinoma cell lines and one human hepatoma cell line, but not to any other cell lines tested. 4G1 reacted with three human esophageal carcinoma cell lines and four other cell lines. By peroxidase-antiperoxidase staining, 4C4 and 4G1 detected antigens of the epithelial cells on 10 pairs of esophageal carcinoma and normal esophageal specimens. 4G1 recognized a CE69T/VGH antigen with a molecular weight of 180K. Since 4G1 also reacted with purified carcinoembryonic antigen (CEA) and immunoprecipitated 125I-CEA, 4G1 seems to be an antibody recognizing CEA produced by CE69T/VGH cells. Since 4C4 also bound to the epithelial cells of normal uterine, vaginal, breast and liver tissues, it seems to recognize an epithelial antigen, and can be used to characterize the antigen in the specialization or differentiation of epithelial cells.
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PMID:Monoclonal antibodies against human esophageal carcinoma cell lines. 282 67

Peripheral blood mononuclear cells from a patient with chronic myelogenous leukemia (CML), in remission, were depleted of CD8-positive T-cells and cultured with Epstein-Barr virus. Four of 20 cultures (20%) secreted human IgG antibodies selectively reactive with the cell surfaces of certain human leukemia cell lines. Three polyclonal, Epstein-Barr virus-transformed, B-cell lines were expanded and fused with the human-mouse myeloma analogue HMMA2.11TG/O. Antibody from secreting clones HL 1.2 (IgG1), HL 2.1 (IgG3), and HL 3.1 (IgG1) have been characterized. All three react with HL-60 (promyelocytic), RWLeu4 (CML promyelocytic), and U937 (monocytic), but not with KG-1 (myeloblastic) or K562 (CML erythroid). There is no reactivity with T-cell lines, Burkitt's cell lines, pre-B-leukemia cell lines, or an undifferentiated CML cell line, BV173. Leukemic cells from two of seven patients with acute myelogenous leukemia and one of five with acute lymphocytic leukemia react with all three antibodies. Normal lymphocytes, monocytes, polymorphonuclear cells, red blood cells, bone marrow cells, and platelets do not react. Samples from patients with other diverse hematopoietic malignancies showed no reactivity. Immunoprecipitations suggest that the reactive antigen(s) is a lactoperoxidase iodinatable series of cell surface proteins with molecular weights of 42,000-54,000 and a noniodinatable protein with a molecular weight of 82,000. Based on these data these human monoclonal antibodies appear to react with myelomonocytic leukemic cells and may detect a leukemia-specific antigen or a highly restricted differentiation antigen.
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PMID:Human monoclonal antibodies reactive with human myelomonocytic leukemia cells. 292 15

To determine the utility of tissue section immunochemistry in the evaluation of bone marrow involved by lymphoid and plasma cell malignancies, snap-frozen, undecalcified bone marrow core and aspirate samples from 23 patients with these disorders were studied with a battery of monoclonal antibodies. With techniques that preserve architecture, difficult diagnostic cases characterized by core but not aspirate involvement, or the reverse, were resolved. By means of an extensive battery of monoclonal antibodies applied to serial sections, complex tumor cell phenotypes were established in all 23 cases. In addition to the identification of straightforward monoclonal surface immunoglobulin expression in small cleaved cell lymphomas (four cases), the battery approach added immunologic certainty in malignancies with unusual or difficult phenotypes: peripheral T-cell lymphomas with idiosyncratic antigen expression, and chronic lymphocytic leukemias and small cell lymphomas with faint surface immunoglobulin expression (four cases). For the chronic lymphocytic leukemias and the small cell lymphomas, the combined IgD+, B2+, B1+, Ia+, Leu-1+ phenotype taken as a whole had greater utility than any isolated marker. The acute lymphocytic leukemias and the myelomas studied demonstrate the wide range of B-cell antigens that must be detected to account for the variety of B-cell neoplasms encountered. Additionally, the previously undescribed phenotypic subset of CALLA+ myelomas, which is of prognostic relevance, was identified. Marrow frozen section immunotyping is a major asset in the evaluation of patients with lymphoma, leukemia, and myeloma when special care is accorded to tissue handling and to treatment of endogenous peroxidase/pseudoperoxidase and interstitial immunoglobulin.
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PMID:Immunotopographic assessment of lymphoid and plasma cell malignancies in the bone marrow. 293 17


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