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)

A human immunoglobulin M (IgM) antibody secreting hybridoma, HMG1, has been established and studied for its reactivity against human gastric cancer cells. Lymphocytes isolated from a regional lymph node of patient with gastric adenocarcinoma were fused with mouse myeloma cells NS-1. Supernatants from the generated human-mouse hybrids were first screened for immunoglobulin production by ELISA. The identified human IgM-secreting hybridomas were expanded and subcloned for further analysis or cryopreservation. The screening for binding of antibodies to a panel of human cancer cell lines and normal fibroblast was carried out with PAP or indirect immunofluorescence stain. The selected hybridoma, HMG1 after being cloned three times, was stable in secreting IgM (about 4 micrograms/1 x 10(6) cells) for more than 9 months. Large amount of ascites was obtained by injecting this hybrid to BALB/C nude mice pretreated with anti-lymphocyte serum and pristane. The ascitic fluid contained 5-19 mg human Ig/ml. Subsequently this IgM was extracted from ascitic fluid by saturated ammonium sulphate solution. This crude extract was further purified with immuno-affinity chromatography. Both this purified ascite-IgM as well as IgM from HMG1 supernatant would react with gastric cancer cell line BGC-823 but not with human normal fibroblasts 350Q by PAP or immunofluorescence analysis. The human HMG1-IgM reacted with gastric cancer cells on paraffin embedded tissue section but did not react with normal gastric mucosa cells. HMG1-IgM had some complement dependent cytotoxicity against BGC-823. These results suggest that the establishment of anticancer human monoclonal antibodies with human-mouse hybridoma technique be feasible. There is a possibility for clinical applications of this human monoclonal antibody in the future.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:[Study of anticancer human monoclonal antibody--establishment of human monoclonal antibody to gastric cancer by human-mouse hybridoma]. 324 78

Two IgG1 type monoclonal antibodies ALT-01 and ALT-04 were prepared by two different immunization schedules. ALT-01 was generated by fusing murine myeloma NS-1 cells with splenocytes from a BALB/c mouse immunized by human lung squamous carcinoma cells, which were coated by antisera to mixed human lymphocytes. For preparation of ALT-04, human lung squamous carcinoma xenograft-bearing nude mice were injected I. P. with the spleen cells of normal BALB/c mice in order to acquire immunofunction. The spleen cells from these tumor-bearing nude mice were fused with NS-1 cells. Then, these hybridomas were screened and cloned for 3 times. Two antibodies were shown to recognize the surface antigen on human lung carcinoma cells and several kinds of tumor cell lines but not those on normal cell lines. ALT-01 reacted to neither human lung carcinoma tissue nor its xenograft. ALT-04 reacted to human lung carcinoma tissue, of which, reaction to adenocarcinoma was the strongest but not to various normal tissues. Immunoprecipitation followed by SDS-polyacrylamide gel electrophoresis and autoradiography was used to detect the associated antigen in 35S-labeled human lung carcinoma cells. Antigens, reacting to ALT-01, show one band of Mr 38,000 but those to ALT-04 reveal two bands of Mr 48,000 and 36,000.
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PMID:[Reactivity of monoclonal antibodies ALT-01 and ALT-04 and identification of lung cancer-associated antigens]. 344 54

Multiple primary cancers form 1 to 10% of all malignancies, but only a few cases of quadruple cancers are reported a year in Japan. We report a case of quadruple cancers--gastric adenocarcinoma, transitional cell carcinoma of bladder, multiple myeloma and leiomyosarcoma of bladder.
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PMID:[Quadruple cancers (gastric adenocarcinoma, multiple myeloma, transitional cell carcinoma and leiomyosarcoma of the bladder]. 344 35

The association of a casual reading of blood pressure (BP) in 1963 to subsequent 15-year cancer mortality was examined in a cohort of 10,059 middle-aged and elderly men. Systolic BP (SBP), but not diastolic BP, predicted significantly long-term cancer mortality occurring in 369 subjects. The covariate-adjusted relative risk (RR) estimated by Cox's proportional hazard model was 1.10 [95% confidence interval (CI), 1.00-1.21]. In patients aged less than 60 at the beginning of the study, increased cancer mortality was mainly observed in association with SBP of more than 150 mm Hg. In subjects aged 60 or above, the estimated RR was 1.21 (95% CI, 1.03-1.42). Exclusion of 40 men in whom diagnosis made prior to 1963 or death occurred through 1965 did not alter the results. An excess mortality in men who reported pharmacologic treatment for hypertension while under follow-up was fully accountable by their age, BP, and smoking habits. Analysis by site suggested that the association was mainly due to increased mortality from cancer of the digestive and genitourinary organs (estimated RR's, respectively, 1.20 and 1.26; 95% CI's, respectively, 1.03-1.39 and 0.99-1.59). Analysis by histologic subtype suggests an association with adenocarcinoma (RR = 1.19, 95% CI, 1.04-1.37) but not squamous cell or transitional cell carcinomas, myeloma, lymphomas, and leukemias.
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PMID:Elevated systolic blood pressure as a predictor of long-term cancer mortality: analysis by site and histologic subtype in 10,000 middle-aged and elderly men. 345 26

A monoclonal antibody was prepared by hybridizing mouse myeloma cells with spleen cells from the mouse which was immunized with human colon cancer transplanted in nude mice. The reactivity of the monoclonal antibody, named A7, was tested by immunoperoxidase method. A7 reacted strongly with human adenocarcinoma cell lines and carcinoembryonic antigen (CEA). In surgical specimens, A7 reacted with 10 cancer tissues and 2 normal colon mucosa from 19 colorectal cancer patients. A7 did not react with other cancers. It was thought that A7 reacted with colon- or colon cancer-specific CEA. The reactivity of A7 with colorectal cancers was markedly reduced by preoperative irradiation.
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PMID:A monoclonal antibody against human colon cancers. 352 36

Gallium nitrate is the anhydrate salt of the naturally occurring heavy metal. It has demonstrated antitumor activity in a variety of murine tumor models, including Walker carcinosarcoma 256, fibrosarcoma M-89, leukemia K-1964, adenocarcinoma 755, mammary carcinoma YMC, reticulum cell sarcoma A-RCS, lymphoma P1798, and osteosarcoma 124F. Preclinical studies performed in rats, rabbits, dogs, and monkeys showed the dose-limiting toxicity to be renal. The hepatic, pulmonary, gastrointestinal, hematologic, and integumentary systems were also involved. The major route of elimination is the kidneys, with 35%-71% of the infused dose excreted within 24 hours. Three phase I studies suggested the following phase II doses: 700-750 mg/m2 by short infusion, once every 2-3 weeks; 300 mg/m2/day by short infusion for 3 consecutive days, to be repeated every 2 weeks; and 300 mg/m2/day by continuous infusion for 7 consecutive days, to be repeated every 3-5 weeks. The major organ toxicity reported was renal; however, this can be adequately controlled either by hydration and osmotic diuresis or by use of continuous schedule. (Either maneuver appears to allow delivery of the recommended phase II dose with a less than 30% risk of change in serum creatinine.) In limited phase II evaluation, the drug has shown antitumor activity in patients with either refractory lymphomas or small cell lung carcinoma, with total objective response rates of 28% and 11%, respectively. In addition, it has been effective in the treatment of patients with cancer-related hypercalcemia by having an inhibitory effect on calcium reabsorption from bone. Single-agent phase II studies are planned in all major tumor types. Some are already ongoing in patients with genitourinary malignancies (renal, bladder, prostate, testicular), small cell lung carcinoma, and multiple myeloma. Metabolic studies are in progress at Memorial Sloan-Kettering Cancer Center to further elucidate the mechanism or mechanisms of the hypocalcemic effects.
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PMID:Gallium nitrate: the second metal with clinical activity. 353 51

Mouse monoclonal antibody 17-1A is specific for an antigen expressed on cells of human gastrointestinal malignancies and has been used in radioimmune imaging and therapy trials for patients with colon and pancreatic cancer. The cell line SG3/5 was generated by transfection of a nonproducing mouse myeloma line (SP2/0) with a chimeric gene construct composed of variable regions from the mouse 17-1A immunoglobulin (gamma 2a, kappa) and constant regions of human k and gamma 3 immunoglobulin genes. The secreted immunoglobulin was bound by mouse monoclonal antibodies to human IgG(Fc) and IgG3 but not by staphylococcal protein A. Gel filtration HPLC profiles of purified chimeric antibody were similar to normal human IgG3 but quite different from native 17-1A and normal human IgG1, 2, and 4. Native and chimeric 17-1A had similar patterns of reactivity with colon cancer, other adenocarcinoma, and leukemic cell lines. Competitive inhibition documented that native and chimeric 17-1A had identical capacities to inhibit radiolabeled native 17-1A binding to colon cancer cell lines. Thus, the chimeric 17-1A exhibits molecular characteristics of normal human IgG3 but retains the specificity and binding affinity of the native 17-1A murine monoclonal antibody. The native and chimeric 17-1A mediated similar modest degrees of human lymphocyte and monocyte ADCC in a 4-hr 51Cr release assay, and both failed to mediate complement lysis of colon carcinoma cell lines in the presence of human complement. This human/mouse chimeric monoclonal antibody may be a good candidate for use in clinical trials because it retains the tumor antigen specificity and human effector cell recognition of the native 17-1A, would presumably have a fivefold to 10-fold longer circulating half-life in man, and should be considerably less immunogenic as compared with native murine immunoglobulins.
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PMID:Characterization of a mouse/human chimeric monoclonal antibody (17-1A) to a colon cancer tumor-associated antigen. 358 80

We have evaluated approximately 10,000 monoclonal antibodies (MoAb) resulting from 25 hybridizations of spleen cells from mice immunized with cells from human non-small cell lung carcinoma or fetal lung. The spleen cells were hybridized with NS-1 myeloma cells, and the resulting hybridomas were screened for production of MoAb to non-small cell lung carcinoma by binding assays with either cell extracts or cells growing in culture, followed by immunohistology on frozen sections. Fourteen MoAb had relative specificity for non-small cell lung carcinoma versus normal tissues. Three of these MoAb (L3, L6, L17) also reacted with most carcinomas of the breast and colon, and two MoAb (L20 and L22) reacted with the four samples of small cell lung carcinoma tested. No MoAb defined an antigen of absolute tumor specificity, and no MoAb reacted substantially more with adenocarcinoma than squamous cell carcinoma of the lung (or vice versa). Five MoAb were Ig G1, two were Ig G2a, and the remaining seven were Ig M. Seven MoAb (L5, L6, L15, L17, L20, L22, L23) could bind to the cell surface. Three MoAb (L6, L15, L17) defined carbohydrate antigens, and three (L3, L5, L20) were to protein antigens, while the antigens to which the remaining MoAb are directed have not been identified. Six MoAb could bind to tumor cells in Carnoy-fixed paraffin-embedded sections. An intercellular variability in antigen expression was detected with all 14 MoAb. At least two of the MoAb, L6 and L20, are good candidates for preclinical testing in view of their high level of tumor selectivity, as shown by both immunohistology and binding assays with living cells.
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PMID:Monoclonal mouse antibodies raised against human lung carcinoma. 373 Oct 64

Spleen cells from rats bearing syngeneic metastatic 13762NF mammary adenocarcinoma clone MTLn3 tumors were fused with the rat myeloma Y3 Ag1.2.3 to generate a panel of monoclonal antibodies (MAbs). The MAbs could be divided into three groups: those cross-reactive with all 13762NF cells; those reactive with cloned MTLn3 and MTC cells; and those predominantly reactive with the highly metastatic MTLn3 cells. One of these MAbs, MT10:21 (an immunoglobulin G2a), binds predominantly to highly metastatic MTLn3 cells and has a high tumor-cell affinity as determined by its saturation kinetics. MAb MT10:21 has a 6-h half-life on the MTLn3 cell surface and a 24-h half-life in the blood of syngeneic rats. Immunoblotting experiments using lysates from the cloned 13762NF sublines revealed that MAb MT10:21 binds to several proteins having relative molecular weights of 72,000, 73,000, and 120,000. Using an immunohistochemical procedure with frozen tissue sections, MAb MT10:21 shows little reactivity with normal rat mammary tissue, irrespective of the stage of the estrous cycle, and it failed to react with a number of other normal fetal and adult tissues. Furthermore, MAb MT10:21 is heterogeneous in its reactivity to cloned sublines of the 13762NF mammary adenocarcinoma, on both tissue cultured cells and tissue sections prepared from tumors growing in situ in the mammary fat pads of syngeneic rats. MAb MT10:21 reacted with certain human breast cancer cell lines and with a subpopulation of metastatic human breast cancer cells in frozen tissue sections from biopsies and autopsies. Metastases from breast cancers reacted more intensely than the primary tumors from which they were derived.
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PMID:Monoclonal antibodies against cell-surface antigens of the metastatic rat 13762NF mammary adenocarcinoma and their cross-reactivity with human breast carcinomas. 377 54

PSK is a protein-bound polysaccharide prepared from cultured mycelium of the Basidiomycete Coriolus versicolor. Effects of PSK on the immunologic responsiveness in tumor-bearing animals were investigated using syngeneic or allogeneic tumors in mice (Lewis lung carcinoma, B16 melanoma, Meth A fibrosarcoma, adenocarcinoma 755, X5563 plasmacytoma, colon 26, MOPC 31C myeloma, sarcoma 180 and Ehrlich carcinoma), rats (BC47 bladder carcinoma, Walker 256 sarcoma and AH7974 hepatoma), hamsters (HA-1T tumor and RPMI 1846 melanoma), guinea pigs (line-10 hepatoma) and rabbit (VX2 and VX7 tumor). Oral or intraperitoneal administration of PSK restored the depressed delayed hypersensitivity against sheep erythrocytes to a normal level in these tumor-host systems. Also, oral administration of PSK lowered the activity of immunosuppressive substances in the serum of tumor-bearing animals. These results suggest that PSK exhibits antitumor effects by restoring the depressed immunologic responsiveness in tumor-bearing animals.
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PMID:[Restoration of immunologic responsiveness by PSK in tumor-bearing animals]. 378 58


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