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)

Hybridoma cells have been obtained by fusing RCY 3 Ag 1-2-3 rat myeloma cells with spleen cells from a rat hyperimmunized with human adenocarcinoma cells (HT 29 cell line) grown in serum-free medium. Immunoglobulins secreted by hybridomas were screened for: (i) specific binding to HT 29 cells; (ii) their ability to inhibit the binding of [125I]-vasoactive intestinal peptide (VIP) to HT 29 cells; (iii) their capacity to modulate the cAMP production induced by VIP. The monoclonal antibodies we have obtained from clones 109-10-16 and 109-10-19 compete for the binding of radiolabelled VIP to HT 29 cells and partially inhibit the production of cAMP induced by VIP while they are ineffective in reducing the intracellular level of cAMP attained after stimulation of HT 29 cells by isoproterenol. We never found antibodies which increase the cAMP level in HT 29 cells. The binding of the purified monoclonal antibody 109-10-16 Ig gamma 2c to HT 29 cells was visualized by indirect immunofluorescence and was not present at the surface of all cells. These observations strongly support the hypothesis that the monoclonal antibodies we have characterized interact with an antigenic determinant which belongs to the VIP receptor or at least to a cell surface component closely associated with the receptor.
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PMID:Anti-cell surface monoclonal antibodies which antagonize the action of VIP in a human adenocarcinoma cell line (HT 29 cells). 631 48

Splenic lymphocytes of BALB/c mice immunized with a glycoprotein-enriched fraction of human ovarian adenocarcinoma were fused with the mouse myeloma cell line P3/NS1/1-Ag4 in the presence of polyethylene glycol (Mr 4,000). The hybrid cultures were screened in an indirect solid-phase radioimmunoassay for the production of relevant antibodies. Hybrids that produced antibodies which bound to the glycoprotein-enriched fractions of ovarian tumors but not to the similar fractions prepared from pooled normal ovary or sera were cloned twice by the limiting dilution method. Two such clones designated 4F4 and 7A10 were expanded in culture and also were grown in mice as ascitic tumors. The immunoglobulin isotype of the clones was of immunoglobulin G1 subclass with kappa light chains. Immunoprecipitation followed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis was used to detect the target antigen in 125I-labeled glycoprotein-enriched fractions of ovarian tumors. A single-chain Mr 48,000 peptide was identified by both clones 4F4 and 7A10. This antigen, which showed binding to concanavalin A-Sepharose, was designated gp48. Monoclonal antibodies against gp48 reacted significantly in radioimmunoassay to approximately 90% of human ovarian tumors and 60% of other tumors, both benign and malignant, but not to normal adult tissues or sera. Quantitative absorption analyses indicated that although the antigen was present in small amounts in some normal adult tissues such as cervix and intestine, it was present in much higher concentrations in most ovarian tumors, in some other tumors, and in fetal intestine and liver. Immunoperoxidase staining of formalin-fixed paraffin-embedded sections of solid ovarian adenocarcinomas revealed strong epithelial reactivity. Monoclonal antibodies to gp48 may be of value for the follow-up and immunotherapy of a variety of human tumors.
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PMID:Identification of a human cancer-associated antigen defined with monoclonal antibody. 638 Jul 8

A patient who presented simultaneously with typical hairy cell leukaemia (HCL) and multiple myeloma (MM) is described. He was treated with melphalan and irradiation and 18 months later presented with an adenocarcinoma. The occurrence of multiple neoplasms in this patient may reflect an underlying predisposition to neoplasia secondary to the immunological defects common in B cell lymphoproliferative diseases.
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PMID:Multiple neoplasms in hairy cell leukaemia. 643 35

A case of adult Fanconi syndrome is described in which there was urinary excretion of kappa light chains. After 13 years the patient developed overt myeloma. She also developed an adenocarcinoma of the colon and an adenocarcinoma of the parathyroid gland. These findings are discussed in relation to the known association between adult Fanconi syndrome, renal damage, and myeloma.
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PMID:Adult Fanconi syndrome progressing to multiple myeloma. 643 83

Monoclonal antibody HBCA-12 obtained by hybridoma procedure after immunization with human mammary adenocarcinoma cell line MDA-MB-231 immunoprecipitated a cell surface sialoglycoprotein gp80 (apparent molecular weight 80 000) from MDA-MB-231 cells and a glycoprotein gp78 from human myeloma cell line ARH 77. A protein of a similar electrophoretic mobility was immunoprecipitated also from 35S-methionine metabolically radiolabeled human melanoma cell line VUP 1. The expression of the antigen recognized by HBCA-12 monoclonal antibody could be detected neither on PHA-induced nor on EBV-transformed peripheral blood mononuclear cells from healthy donors.
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PMID:Biochemical and histochemical characteristics of target antigen detected by monoclonal antibody HBCA-12 against a membrane component of human mammary carcinoma cell line. 652 96

Six patients with occult sternal metastasis presenting with chest pain, and four with sternal deformity associated with "arthritis" had undergone routine roentgenographic examinations, reported as "normal." Subsequent laminography of the sternum demonstrated lytic lesions confirmed by needle biopsy. Adenocarcinoma of the lung and breast were identified in two each of four patients; myeloma and kidney neoplasms were the primary source of malignancy in the remaining two patients. In widespread malignancy, metastasis to the skeletal chest wall is a well-recognized occurrence. Infrequently, it can be an isolated manifestation of an occult or recurrent malignancy, initially overlooked when routine roentgenograms are read as normal. Although sternal x-rays remain the most important means of diagnosis, in suspected cases of sternal metastasis laminography alone may initially reveal lytic lesions.
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PMID:Occult sternal metastasis identified by laminography in patients with chest pain. 671 41

Monoclonal antibodies were produced after immunization of mice with a colorectal adenocarcinoma cell line or liver metastasis membranes from a patient with colon adenocarcinoma. Many monoclonal antibodies were found to react with colorectal adenocarcinoma cells but not with normal colon mucosa, blood lymphocytes, myeloma cells or lung epithelial carcinoma cells. Three of these 'colorectal tumour-specific' antibodies appear to define different antigens that were found in the complex monosialoganglioside fraction from 60 to 90% of the colorectal and pancreatic adenocarcinoma tumours or metastases examined but essentially lacking in normal colon mucosa and other normal or tumour tissues tested.
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PMID:Monoclonal antibodies against gastrointestinal tumour-associated antigens isolated as monosialogangliosides. 684 Aug 74

A xenoantiserum to murine B16 melanoma cells was developed by immunizing rabbits with cultured B16 melanoma cells. This antiserum could, after extensive absorption with normal C57BL/6 mouse tissues, react with syngeneic (B16) and allogeneic (HP) melanomas as well as with other murine neoplasms, including syngeneic 75S adenocarcinoma, allogeneic myeloma and leukemic T cell lines. The antiserum also cross-reacted with syngeneic fetal fibroblasts and with an allogeneic fetal fibroblast cell line (SC-1) either uninfected or infected with murine leukemia virus (MuLV). Immunoprecipitated material from B16 melanoma cell-surface glycoproteins that had been labeled with [125I] by lactoperoxidase and purified by a Lentil lectin column was analyzed by one-dimensional SDS- and two-dimensional polyacrylamide gel electrophoresis, which disclosed an acidic glycoprotein with a molecular weight (mol. wt) of 90 K daltons. Absorption studies suggested that the 90 K mol. wt gylcoprotein represented the oncofetal moiety expressed in murine medanoma, carcinoma and fetal tissues. When the amount of this antigen in developing C57BL/6 mouse fetuses was measured by absorption assays, we found that it was expressed strongly in those fetuses just before birth. Binding and absorption studies demonstrated that the 90 K mol. wt glycoprotein, while being expressed on a variety of fetal and neoplastic cells in mice, did not exist at detectable levels in normal tissues of adult C57BL/6 mice, including tissues of the thymus, lymph node, spleen, liver, brain, lung and kidney.
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PMID:Identification of an oncofetal antigen (gp90) on murine B16 melanoma cells. 688 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

Various studies have demonstrated the usefulness of monoclonal antibodies in recognizing discrete tumor antigenic determinants. The present study describes the tissue reactivity of monoclonal antibodies prepared against a squamous cell carcinoma of the lung. Antigens were purified from the tumor extract by anti-beta 2 microglobulin affinity chromatography. These beta 2-associated antigens demonstrated tumor specificity by the leukocyte adherence inhibition assay. Antibody-secreting hybridomas were generated by fusion of mouse myeloma cells with mouse spleen cells immunized with purified tumor antigens. Hybridomas were selected by a solid-phase tumor membrane-binding immunoassay. The target specificity of the secreted monoclonal antibodies was ascertained by radioimmunoprecipitation analysis and indirect immunofluorescence on various human tumor and normal tissue sections. Monoclonal antibody-secreting hybridomas 48.4.8 and 48.4.2 secreted immunoglobulin that selectively immunoprecipitated polypeptide fragments from human lung tumor membrane antigens. Hybridoma 9.2.2 secreted antibody that was strongly positive by indirect immunofluorescence on all tested lung squamous cell carcinomas. Adjacent or intervening normal lung tissue did not display significant immunofluorescence. Adenocarcinomas of the lung were negative or focally positive when focal squamous cell differentiation was present. Oat cell carcinomas were negative. The secreted antibody did not significantly stain three extrapulmonary tumors or a variety of normal tissues.
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PMID:Monoclonal antibodies to human lung tumor antigens demonstrated by immunofluorescence and immunoprecipitation. 704 19


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