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)

Extramedullary plasmacytomas are rare tumors, with 272 cases reported in the literature in English. Less than 10 per cent of these are located in the gastrointestinal tract. This report documents the first primary plasmacytoma of the omentum in association with a recurrent colonic adenocarcinoma. Extramedullary plasmacytoma, a B cell neoplasm, characteristically arises in areas containing lymphoid tissue. In our case the tumor most likely arose in a lymph node or nodes in the omental fat, with subsequent replacement of the entire greater omentum and involvement of the colonic serosa by direct extension. Although the extent and nature of the association between myeloma and carcinoma remain obscure, a review of the literature suggests that such association may occur more frequently than has been supposed. Further investigation would appear to be warranted.
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PMID:Primary extramedullary plasmacytoma of the omentum associated with recurrent adenocarcinoma of the colon: first case report. 740 97

The authors report two cases of myelomatosis localised to the pleura, one of which was associated with an adenocarcinoma. Pleural effusions are relatively rare during the course of multiple myeloma and most often occur with non-specific disorders of the disease. The myelomatous origin of a pleural effusion can only be made by analysis of the pleural fluid and should be recognised early enough to enable aggressive treatment to be instituted even if the prognosis associated with such a localisation is very poor.
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PMID:[Pleural involvement of myeloma. Apropos of 2 cases]. 774 45

A hybridoma 1 G 10 clone was derived from fusion between SP 2/0- Ag14 myeloma cells and spleen cells of BALB/C mice immunized with the soluble Noridet P40 extracts from a human colonic adenocarcinoma cell line SW 620. The 1 G 10 clone was identified to be able to produce monoclonal antibody of IgG1 subclass which had sufficient titer for immunoreactivity to both extracts from SW 620 cells and surgical colonic carcinoma tissues, but no immunoreactivity to both extracts from normal adult colorectal tissues, mixed human lymphocytes and normal human serum (NHS) as well as carcinoma embryonic antigen (CEA) by enzyme-linked immunosorbent assay (ELISA). By affinity column on Sepharose 4 B coupled with 1 G 10 IgG, colonic carcinoma-associated antigen (CCA) was purified from SW 620 cell extracts and thoracic ascitic fluid of a patient with lung adenocarcinoma. Western blotting analysis with 1 G 10 IgG demonstrated that one immunoreactive bands corresponding to 55 Kd molecule was observed in the samples of ascitic fluid and SW 620 cell extracts. The 55 Kd band could be stained with Alcian blue. The immunoreactivity of CCA to 1 G 10 antibody could be abolished completely by the treatment of the antigen with NaIO4 and proteinase K. These results indicated that the determinants of CCA reacted with 1 G 10 monoclonal antibody are probably both present in polysaccharide and protein part of the molecule. The specificity of anti-CCA 1 G 10 monoclonal antibody and its possible application for clinical oncology were discussed.
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PMID:[Studies on a new tumor marker with monoclonal antibody against human colorectal carcinoma antigen]. 780 27

The mouse monoclonal antibody, m30.6 (IgG2b), detects an antigenic determinant expressed predominantly on the surface of colorectal adenocarcinoma cells and has been shown previously to be a potentially useful therapeutic and diagnostic reagent for human colon cancer. We report the production and characterization of a mouse/human chimeric antibody, c30.6, with potent in vitro and in vivo antitumor activity. The genes encoding the variable domains for heavy and light chains were amplified by thermal cycling using degenerate oligonucleotide primers complementary to conserved immunoglobulin framework sequences. The gene segments were sequenced, subcloned into eukaryotic expression vectors containing human constant region genes (IgG1 and kappa), and cotransfected into nonsecreting Sp2/0 mouse myeloma cells. There were significant differences in the biological activities of the murine and chimeric antibodies. The i.p. administration of c30.6 but not of m30.6 produced a marked growth inhibition of s.c. 30.6+ COLO 205 tumors in scid/scid mice (approximately 40% reduction in tumor size, measured 21 days after tumor inoculation). Reduced tumor growth was not due to altered binding characteristics of c30.6 because: (a) the chimeric antibody was shown by flow cytometry to bind exclusively to cell lines that expressed the 30.6 determinant; (b) c30.6 was able to completely inhibit the binding of m30.6 on 30.6+ cells; and (c) the affinity of binding of the two antibodies was the same (Ka, approximately 1.50 x 10(8)). Up to 15% of the total injected antibody dose/g tissue was localized in 30.6+ tumors at 24 h, approximately 13% was present in the tumors at 48 h, and approximately 10% was present at 72 h. Furthermore, c30.6 demonstrated a shorter circulating half-life (53 h; m30.6, 72 h) when given i.p. to C57BL6 x BALB/cF1 mice. Unlike m30.6, c30.6 was also strongly active in antibody-dependent cell-mediated cytotoxicity against a range of 30.6+ tumor target cells in vitro. Up to 80% specific 51Cr release was achieved using either freshly isolated human peripheral blood mononuclear cells or 2-day-old interleukin 2-stimulated human peripheral blood mononuclear cells as effectors. The enhanced antitumor activity of c30.6 suggests that it might be a useful immunotherapeutic reagent for colorectal carcinoma.
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PMID:Chimeric (mouse/human) anti-colon cancer antibody c30.6 inhibits the growth of human colorectal cancer xenografts in scid/scid mice. 795 62

A prospective study of 28 consecutive fine needle aspirates of bone was conducted comparing the sensitivities of cytologic diagnosis with carcinoembryonic antigen (CEA) content to determine if the CEA assay could enhance the sensitivity of cytologic diagnosis of carcinoma metastatic to bone. Aspirates obtained radiologically or at surgery underwent cytologic examination and CEA assay. Cytologic examination was performed on Papanicolaou-stained smears and/or cell blocks. CEA was measured with an enzyme immunoassay; 5 ng/mL was used as the cutoff. Twenty-one were malignant and seven benign. The sensitivities of cytology and CEA were 85% and 47.6%, respectively, and the specificities, 100%. Mean CEA and sensitivity were highest for adenocarcinoma of lung (361.5 ng/mL, 77%), lowest for carcinoma of breast and negative for lymphoma, myeloma and benign aspirates. High CEA was useful in (1) suggesting adenocarcinoma of lung in patients with an unknown primary, (2) suggesting a new primary lung adenocarcinoma in a patient with previous transitional cell carcinoma of bladder, and (3) discriminating lung adenocarcinoma from adenocarcinomas of kidney, thyroid, prostate or endometrium.
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PMID:Cytologic examination and carcinoembryonic antigen assay of fine needle aspirates of bone tumors. 804 20

Four cases of gastric cancer presenting with bone pain due to metastasis as the initial symptom are reported. Investigations revealed solitary osteolytic metastasis in the mandible in one, and left scapula in one patient. Third patient had multiple osteosclerotic metastasis with elevation of acid phosphatase and another had multiple discrete osteolytic metastasis simulating multiple myeloma. All the primary gastric cancers were poorly differentiated adenocarcinoma and three were of Borrman type III on gross appearance. One patient had sparing of the liver inspite of extensive metastasis. Chemotherapy was in effective in two patients and the prognosis was uniformly poor.
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PMID:Unusual bone metastasis as the initial symptom of gastric cancer--a report of four cases. 830 Jan 47

Recent molecular biological approach has revealed the primary structure of some mucin core proteins. Most prominent characteristic is tandemly repeated sequences. cDNA cloning of 6 kinds of mucin core proteins, MUC1-6, have thus been performed. Among them, the entire structure was revealed on MUC1 and 2. MUC 1 is a type I transmembrane protein with a large number of tandem repeat consisting of 20 amino acids. We have found that mouse MoAb MUSE11 against adenocarcinoma, which detects circulating MUC1 in patients with gastrointestinal and pancreatic cancers, recognizes part of the tandem repeat of MUC1 using synthetic peptides. To date, some of the MoAbs to adenocarcinoma which were prepared for the last decade have been shown to react with the tandem repeat of MUC1(MUC1 epitope), suggesting that MUC1 epitope could be highly immunogenic in human. Recently, cytotoxic T-cells against MUC1 epitope were established from breast and pancreas cancer patients. We could also induce those T-cells from the patient with multiple myeloma. Interestingly, CTL functions in a HLA-unrestricted manner, and may be of use as an adoptive immunotherapy. In addition, we have found antibody against MUC1 epitope in patients with ulcerative colitis or colon cancer. EB virus-transformed B-cell clone producing antibody against MUC1 epitope has been established from a cancer patient. Thus, MUC1 is now considered as a targeting molecule for immunotherapy. Indeed, Longenecker's group in Canada has recently tried the basic evaluation for immunotherapy using synthetic peptides of MUC1.
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PMID:[Molecular biological analyses of mucin core proteins and their clinical application]. 831 84

Five hybridoma cell lines secreting monoclonal antibodies (MAbs) to a 65-kDa tumor-associated phosphoprotein (p65) were established. Purified to homogeneity, p65 was used as an immunogen to induce immune response in C57BL/6N mice. Splenocytes were fused with mouse myeloma cells and hybridoma lines were selectively subcloned. A rapid and sensitive sandwich type ELISA, using purified MAbs was established to measure markedly elevated amounts of p65 in sera obtained from both tumor-bearing rats and from cancer patients. The p65 from rat and human sources was added quantitatively to normal sera to construct standard curves. The average level of p65 in normal rat sera was 38 ng/ml +/- 13 ng/ml (mean +/- SD), and in sera from rats bearing mammary adenocarcinomas, the average value was 1005 +/- 140 ng/ml. In normal human sera the mean level of p65 was 34 +/- 35 ng/ml (mean +/- SD) and sera of patients with variety of cancers had an average p65 value of 344 +/- 57 ng/ml. More than 80% of tested sera from adenocarcinoma-bearing rats (20/24) as well as from cancer patients (82/98) had p65 levels elevated two standard deviations above the mean. Overall the assay had a sensitivity of 80.9% and specificity of 85%. The purified IgG1 MAbs, with high titers and strong anti p65 specificities were also used to develop an immunohistochemical method to visualize the expression of p65 in rat tumor tissue sections. The HB2, HF11 and RE6 cell lines have proved to be quite stable in the ability to secrete anti-p65 MAbs.
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PMID:Monoclonal antibodies against a 65-kDa tumor-associated phosphoprotein: development and use in cancer detection. 831 97

Previously we showed that motility-related protein (MRP-1) is an antigen recognized by monoclonal antibody (mAb) M31-15 inhibiting cell motility and that the sequence of MRP-1 coincides with that of CD9. In the present study, plasmid was constructed in which human MRP-1/CD9 cDNA is expressed under the control of the Abelson murine leukemia virus promoter sequence. The expression plasmid for MRP-1/CD9 was introduced into Chinese hamster ovary cells, human lung adenocarcinoma cell line MAC10 (MRP-1 positive), and human myeloma cell line ARH77 (MRP-1 negative). All of the MRP-1/CD9 (over)expressing clones obtained from these transfected cells showed suppressed cell motility (penetration and phagokinetic track assays) depending on the degree of expression of MRP-1/CD9. Overexpression of MRP-1/CD9 by MAC10 cells resulted in the suppression of cell motility (maximally 73%) associated with considerable inhibition of the cell growth (maximally 48%). However, the inhibition of the growth of MAC10 cells by mAb M31-15 was < 17% at an antibody concentration of 1-5 micrograms/ml, which inhibits cell motility by > 90%. These results suggest that MRP-1/CD9 directly regulates cell motility and may also affect cell growth. Effects on metastasis by the expression of MRP-1 CD9 were investigated with mouse melanoma BL6 cells-BALB/c nu/nu mouse system. Metastatic potential of all transformants expressing MRP-1/CD9 was lower than that of parent BL6 cells.
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PMID:Suppression of cell motility and metastasis by transfection with human motility-related protein (MRP-1/CD9) DNA. 847 5

A series of 12 cell fusions of BALB/c mice spleen cells with the SP2/O-Ag14 mouse myeloma cell line were performed after immunizations with normal human pancreas to generate monoclonal antibodies (mAbs) with high affinity against antigens of the exocrine pancreas. The immunohistologic tissue screening resulted in the selection of 14 clones that were further characterized on frozen tissues, tumor cell lines, and lectin binding assays. Four mAbs reacting with pancreatic acini detected granular antigens and three mAbs reacted with acinar cell membrane antigens. Six other clones reacted with pancreatic ducts; among these were three clones positive with antigens in both acini and ducts. Among the clones reactive with secretory products, there was one pair of mAbs identified as pancreas specific (P78C9/P79D4); the other secretory antigens (identified by P97F3 and P109H1) were also detectable in other exocrine organs, but were absent from the gastrointestinal mucosa. Two clones reactive with acinar cell membranes (P96H2 and P100H1) were also positive with hepatocytes. All but four antigens were detectable in pancreatic cancer cell lines Capan-1, Capan-2, and DAN-G. On the whole, immunizations were more effective using whole pancreatic tissues (eight clones selected) compared with single-cell suspensions as immunogen (four clones) or cell membrane preparations (two clones). Therefore, the immunization and screening strategies used in this study resulted in the generation of new mAbs against specific substructures of the exocrine pancreas. The shared expression of some of these antigens with other exocrine organs and pancreatic adenocarcinoma cell lines suggests that these mAbs detect antigens that are characteristic for the exocrine system and could therefore be useful for the study of the exocrine pancreas and pancreatic adenocarcinomas.
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PMID:Characterization of new monoclonal antibodies directed against normal human exocrine pancreas and pancreatic adenocarcinomas. 848 69


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