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)

Splenic lymphocytes of mice, immunized with membrane-enriched fractions of metastatic human mammary carcinoma tissues, were fused with the NS-1 non-immunoglobulin-secreting murine myeloma cell line. This resulted in the generation of hybridoma cultures secreting immunoglobulins reactive in solid-phase radioimmunoassays with extracts of metastatic mammary carcinoma cells from involved livers, but not with extracts of apparently normal human liver. As a result of further screening of immunoglobulin reactivities and double cloning of cultures, 11 monoclonal antibodies were chosen that demonstrated reactivities with human mammary tumor cells and not with apparently normal human tissues. These monoclonal antibodies could be placed into at least five major groups on the basis of their differential binding to the surface of various live human mammary tumor cells in culture, to extracts of mammary tumor tissues, or to tissue sections of mammary tumor cells studied by the immunoperoxidase technique. Whereas a spectrum of reactivities to mammary tumors was observed with the 11 monoclonal antibodies, no reactivity was observed to apparently normal cells of the following human tissues: breast, lymph node, lung, skin, testis, kidney, thymus, bone marrow, spleen, uterus, thyroid, intestine, liver, bladder, tonsils, stomach, prostate, and salivary gland. Several of the antibodies also demonstrated a "pancarcinoma" reactivity, showing binding to selected non-breast carcinomas. None of the monoclonal antibodies showed binding to purified ferritin or carcinoembryonic antigen. Monoclonal antibodies of all five major groups, however, demonstrated binding to human metastatic mammary carcinoma cells both in axillary lymph nodes and at distal sites.
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PMID:A spectrum of monoclonal antibodies reactive with human mammary tumor cells. 678 31

Monoclonal antibodies to human prostate adenocarcinoma membrane antigens were produced by fusion of P3X63/Ag8 mouse myeloma cells with spleen cells from BALB/c mice immunized against the prostate cancer cell line DU145. The hybrids were screened for antibody production using glutaraldehyde-fixed cells in a solid-phase radioimmunoassay. Antibody-binding specificity was also checked by quantitative adsorption, membrane immunofluorescence, and complement-dependent cytotoxicity assays. A hybridoma clone (83.21) was isolated that secreted antibodies which preferentially bound to several prostate and bladder cancer cell lines but did not bind to a variety of other normal and malignant human cell lines. This antibody also reacted with a cytomegalovirus-transformed human embryonic lung cell line but not to normal human embryonic lung cells. Quantitative adsorption studies demonstrated that the 83.21 monoclonal antibody was strongly reactive to membrane preparations from human prostate adenocarcinoma tissue and a liver metastasis of prostate carcinoma. Little or no binding activity was observed against two other prostate carcinomas, bening prostatic hyperplasia, normal prostate, or normal liver. Binding studies indicate that the 83.21 monoclonal antibody does not bind to alpha-fetoprotein, carcinoembryonic antigen, prostatic acid phosphatase, human leukocyte antigen, beta 2-microglobulin, HLA-Dr antigens, fibronectin, or prostate antigen. The data indicate that we have isolated a monoclonal antibody that binds to an antigen(s) expressed by several urogenital carcinoma cell lines as well as human prostate tumor tissue and that the antibody is not directed against well-known human tumor cell markers.
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PMID:Monoclonal antibodies to human prostate and bladder tumor-associated antigens. 704 15

Hybridoma cell lines secreting monoclonal antibodies to carcinoembryonic antigen (CEA) were generated by fusing mouse immune lymphocytes with the mouse myeloma variant cell line, NS-1. Antibody secreted by one cloned hybrid cell line could bind only a select portion of the CEA bound by the commercially available goat anti-CEA antiserum used in clinical assays. Radiolabeled CEA could be purified on a monoclonal antibody affinity column. Incorporation of this purified radiolabeled CEA in a double-antibody solid-phase assay with goat anti-CEA antiserum led to an approximately 2.5-fold increase in sensitivity of the assay. Genetically stable hybrid clones may be sources of virtually unlimited quantities of such antibodies which may have potential utility in improving the cancer specificity of clinical assays.
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PMID:Monoclonal antibodies to carcinoembryonic antigen produced by somatic cell fusion. 726 Aug 97

A novel vector pMH-gpt, which is proved useful for cloning mouse immunoglobulin heavy and light chain V genes and for expressing mouse-human chimeric antibody, was constructed. The vector contains human genomic C gamma 1 and C kappa genes, cloning sites for immunoglobulin V region genes, murine Ig promoters, a human Ig heavy chain enhancer, and the selection marker gene Eco-gpt. Because VH and V kappa genes can be cloned into a single vector, a chimeric antibody gene is easily constructed by this simple insertion procedure. The usefulness of the vector was confirmed by construction of two mouse-human chimeric antibodies. Mouse monoclonal antibody (MAb) 196-14 recognizes the ovarian cancer-associated antigen (CA125), and MoAb 2-18 reacts with carcinoembryonic antigen (CEA). Mouse-human chimeric 196-14 and 2-18 antibodies were readily constructed and efficiently produced in a mouse myeloma cell line by utilizing the vector. Both chimeric antibodies retained binding activity to their respective antigens. In biodistribution and immunoscintigraphy studies, specificity of radiolabeled chimeric 196-14 antibody was identical to that of its murine counterpart and significant accumulation at the tumor site was observed. The pMH-gpt vector is useful for constructing and producing mouse-human chimeric antibodies.
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PMID:Construction and expression of chimeric antibodies by a simple replacement of heavy and light chain V genes into a single cassette vector. 786 92

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

A component exhibiting toxicity to B cell hybridoma cells was isolated and purified from fetal calf serum (FCS) by immunoaffinity chromatography using a monoclonal antibody (mAb) which reacted with the high-molecular-weight glycoprotein (6B3.Ag) recognized by a mAb, 6B3, to human large cell lung carcinoma cells (HLC-2). The component (FCS-6B3.Ag) was a high-molecular-weight antigen (approximately 1,000,000), consisting mainly of 76,000 subunits. FCS-6B3.Ag showed the same mobility in the pre-beta globulin region as that of 6B3.Ag on electrophoresis in 1.2% agarose gel. When FCS-6B3.Ag was analyzed by double immunodiffusion, it reacted with anti-6B3.Ag antiserum and the precipitin line fused partially with that formed between 6B3.Ag and anti-6B3.Ag antiserum. FCS-6B3.Ag was found to be toxic to hybridoma cells (anti-6B3.Ag, anti-alpha-fetoprotein, anti-carcinoembryonic antigen or anti-C-reactive protein mAb producing cells) specifically in vitro at 5 micrograms/ml. The antigen also strongly suppressed their growth. The toxic effect of FCS-6B3.Ag appeared immediately after addition, and death of the target cells was complete only after 36-48 h. However, the antigen exhibited only weak suppression of Ig-non-secretory mouse myeloma (P3U1), thymic lymphoma (EL4) of mastocytoma (P815) cell growth. Five lots of FCS contained 2.1 to 4.1 micrograms/ml of FCS-6B3.Ag.
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PMID:Identification and purification of a toxic component to B cell hybridoma cells in fetal calf serum. 820 Aug 50

We have previously reported that a group of monoclonal antibodies (MAbs) to carcinoembryonic antigen (CEA), designated Group F MAbs, are able to discriminate CEA in tumor tissues from the CEA-related normal antigens and that CEA assay systems utilizing at least one Group F MAb show the improved cancer diagnosis. In this study, we cloned the genes coding for two Group F MAbs (F11-35 and F11-39) and deduced the amino acid sequences of the variable regions for their heavy and light chains. The variable region for the heavy chain of F11-35 contained a possible N-glycosylation site (Asn/Asp/Thr) at amino acid positions 89-91. Then, we constructed two mouse-human chimeric antibodies by using the F11-35 and F11-39 variable region genes of heavy and light chains (VH and V kappa) and human heavy and light chain constant region genes (gamma 1 and kappa) derived from a human plasma cell leukemia line (ARH77). The chimeric gene constructs were sequentially co-transfected into murine non-Ig-producing myeloma (P3-U1) or hybridoma (Sp2/0) cells by electroporation. The resulting chimeric heavy chain of F11-35 showed a slightly but significantly higher molecular weight than that of F11-39, but the molecular weights of their unglycosylated peptides synthesized in the presence of tunicamycin were similar, indicating the glycosylation at the possible N-glycosylation site in the variable region of the Ch F11-35 heavy chain. Both chimeric antibodies exhibited the same specificity and affinity for CEA as those of the parental murine hybridoma antibodies, respectively. Ascites production of Sp2/0 transfectomas is sufficiently high (600-900 micrograms/ml) for initial clinical studies with the chimeric antibodies.
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PMID:Construction and expression of two mouse-human chimeric antibodies with high specificity and affinity for carcinoembryonic antigen. 824 16

The first tumor marker (TM) described in Oncology was the Bence-Jones protein in 1847 in patients with multiple myeloma. However, it was not until the early 60s that the first useful TM in gastrointestinal (GI) cancer was recognized, alpha fetoprotein. The development of TM has achieved enormous progress over the last years and its definition includes not only tumor products but elements inherent to the tumor such as oncogenes. A review is presented of the most important TM in GI tumors according to anatomic location. Emphasis is made in colon cancer and the clinical usefulness of carcinoembryonic antigen throughout the different stages in the management of such patients.
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PMID:[Tumor markers in cancer of the digestive system]. 948 May 20

Interleukin-6 (IL-6) is a pleiotropic cytokine that has been shown to regulate immune defense mechanisms and hematopoiesis. In addition, IL-6 may also be involved in malignant transformation and tumor progression. A poor prognosis in patients with multiple myeloma, renal cell carcinoma, ovarian cancer, or prostate cancer has been associated consistently with elevated IL-6 serum levels. The aim of this study was, therefore, to assess IL-6 serum levels in 68 advanced gastrointestinal cancer patients and to correlate them with prognosis. IL-6 serum levels were found to be significantly elevated in cancer patients with respect to controls. Moreover, patients with disseminated cancer displayed significantly higher IL-6 serum levels than patients without apparent metastases. On univariate analysis, both overall survival (OS) and time to disease progression (TTP) were shown to be affected by IL-6 serum levels. However, multivariate analysis failed to demonstrate an independent prognostic significance for IL-6 serum levels while confirming the role of previously established variables, such as performance status, carcinoembryonic antigen (CEA) serum levels, and distant metastases. In conclusion, this study showed that IL-6 serum levels were elevated in advanced gastrointestinal cancer patients and correlated with both OS and TTP. However, they were shown not to be an independent prognostic factor.
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PMID:Interleukin-6 serum level correlates with survival in advanced gastrointestinal cancer patients but is not an independent prognostic indicator. 1117 80

CD66a is a member of the carcinoembryonic antigen family and has been suggested to function as an intercellular adhesion molecule and cell growth regulator. Expression of CD66a in myeloma cells was examined with mAb TS135 against CD66a transfectants of murine-transformed fibroblasts. The reactivity of mAb TS135 with CD66a, CD66c, and CD66e was revealed. CD66a in myeloma cells was considered to be detectable with this mAb, since CD66c and CD66e are not expressed in them. CD66a was detected in three myeloma cell lines and an IgM-producing B-cell line. In clinical bone marrow specimens, including 18 multiple myeloma, two primary macroglobulinemia, and a case of CLL-like chronic lymphoproliferation with monoclonal IgG production, CD66a and three conventional myeloma cell markers (PCA-1, CD38, and CD56) were examined by indirect immunofluorescence assay. The results showed that 18 out of 21 cases (86%) were CD66a+, and PCA-1 showed the highest correlation with CD66a among conventional markers. Primary macroglobulinemia and chronic lymphoproliferation were also CD66a+. Two-dimensional flow cytometry with mAbs TS135 and CD38 confirmed the reactivity of TS135 with myeloma cells in those bone marrow specimens. The findings suggest that CD66a is expressed in multiple myeloma with high frequency.
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PMID:Expression of CD66a in multiple myeloma. 1194 96


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