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)

Monoclonal antibodies against a human osteogenic sarcoma cell line were prepared by production of a somatic cell hybrids between the spleen cells from U-393OS--immunized mice and the mouse myeloma cells SP2/0. From 7 producing and well-growing clones only one--B-0S12--produced antibodies, reactive preferentially with osteosarcoma cells as identified by binding second antibodies and 125I-labeled Protein A. This antibody was tested against a panel of normal and tumor cell targets to determine the pattern of the antigen detected. The monoclonal antibody reacted strongly against U-3930S cells and another human sarcoma in vitro and more weakly against human fibroblasts, peripheral lymphocytes, red blood cells and was negative against mouse fibroblasts. When tested against a panel of unrelated human tumor cell lines, B-0S12 antibody was positive with melanoma cells and negative with cells from bladder, cervix and mammary carcinoma. These cross reactions suggested, that the antibody is reactive with a protein, expressed on different tumor types. This protein is not expressed on the cell surface and is probably associated with cytoskeleton, as revealed by immunofluorescence experiments. Western-blot analysis of a cytoskeletal preparation of U-3930S cells suggests, that B-0S12 antibody recognizes a protein with Mr 55 kD. Further studies are needed to characterize the molecules, carrying the epitope, identified by this monoclonal antibody.
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PMID:Monoclonal antibody to a human osteogenic sarcoma cell line. 304 55

Monoclonal antibodies (MoAbs) against human osteosarcoma cells were obtained by the production and cloning of hybrids resulting from the fusion of mouse myeloma cells P3 X 63Ag8.653 with spleen cells from partially purified, osteosarcoma-associated antigen (OSAA)-immunized BALB/c mice. OSAAs were isolated from the spent culture medium of a human osteosarcoma cell line (TE-85). Five hybrid clones were established and designated as OSA1, OSA2, OSA3, OSA4, and OSA5. OSA1 and OSA2 had similar activity. All 5 MoAbs reacted strongly with most osteosarcoma cell lines and with all osteosarcoma tissues tested but not with 10 tumor cell lines and 2 tumor tissues from other cancers. OSA3, OSA4, and OSA5 cross-reacted with a fibrosarcoma cell line, a colon cell line, and fibrosarcoma, respectively, as well as with a melanoma cell line. None of the MoAbs were reactive with activated normal human peripheral blood mononuclear cells (PBMC). Immunoprecipitation of membrane protein isolated from LM cells and TE-85 cells with the MoAbs OSA1 and OSA2 conjugated with Staphylococcus aureus yielded a molecule with molecular weight of approximately 92,000. No detectable membrane protein was precipitated when 125I-labeled membrane protein from pooled activated human PBMC and tumor cells of other histologic types were used in the immunoprecipitation.
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PMID:Monoclonal antibodies to human osteosarcoma-associated antigen(s). 346 10

Case histories of 5 tumor patients treated with natural leukocyte interferon-alpha (IFN-alpha) are presented. One patient with juvenile laryngeal papillomatosis responded well to interferon treatment, but the disease recurred when therapy was withdrawn. Upon reinstitution of treatment, the patient once again responded well. Another patient with myelomatosis also responded well to interferon therapy and in this case, too, the tumor recurred when interferon treatment was withdrawn. Reinstitution of interferon therapy was, however, unsuccessful. One patient with generalized giant cell tumor of bone responded with regression after more than 5 years of interferon treatment. Another patient with pulmonary osteosarcoma metastases, having received irradiation and interferon combination therapy followed by sole interferon treatment, responded well with a lasting stationary radiogram after 6 years of interferon treatment. One patient with malignant glioma, showing signs of tumor growth during the first few months of interferon therapy, eventually responded, and became disease-free after 6 years. The latter 3 patients are continuously receiving interferon therapy although more than 5 years have elapsed since their interferon therapy was initiated. It is suggested that interferon therapy for malignant tumors be given for life (or to progression of disease) in responding patients. Such a concept entails biological implications for interferon therapy in general and for antitumor action of interferons in particular. Other possible clinical schedules should only be constructed within the framework of controlled clinical trials.
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PMID:Does successful interferon treatment of tumor patients require life-long treatment? 347 1

Monoclonal antibodies (MAbs) against sarcoma-associated cell membrane antigens were prepared by immunizing BALB/c mice with tumor cells from a human osteosarcoma, TPX, grown as a xenograft in athymic BALB/c nude mice. Spleen cells from immunized mice were hybridized with X-63 Ag. 8.653 mouse myeloma cells which yielded 260 growing hybridomas. Seven of these produced antibodies that bound to TPX cells and to cells from another osteosarcoma, but not to autologous skin fibroblasts. MAbs from 2 (TP-1 and TP-3) of these 7 clones did not cross-react with non-sarcomatous tumor cells or peripheral blood lymphocytes. Immunohistochemical studies on frozen tissue sections showed that the TP-1 (IgG-2a) and TP-3 (IgG-2b) antibodies had characteristic and identical specificity profiles. Binding of TP-1 (TP-3) was demonstrated to 15/15 (15/15) osteosarcomas, 3/3 (2/2) synovial sarcomas, 7/9 (6/8) malignant fibrous histiocytomas, 2/2 (1/1) malignant hemangiopericytomas, 1/2 (1/2) chondrosarcomas and 3/6 (1/3) unclassified sarcomas. The antibodies did not bind to any of 16 sarcomas belonging to other histological subtypes, including liposarcomas and leio- and rhabdomyosarcomas. Moreover, they failed to bind to sections of 66 different non-sarcomatous malignancies, or to any of a range of normal adult and fetal tissues, although some weak staining of proximal kidney tubules was seen. The restricted specificity of these antibodies to some major subtypes of human sarcomas makes them promising tools for identification and subclassification of sarcomas.
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PMID:New monoclonal antibodies specific for human sarcomas. 352 38

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

Monoclonal antibodies (MAbs) against a human sarcoma xenograft carried in BALB/c nu/nu mice were produced by immunizing BALB/c mice with tumor cells and fusing their spleens with the SP2/O-Ag 14 mouse myeloma cell line. Hybridoma supernatants were screened using cryostat tissue sections and an immunoperoxidase reaction for ability to stain osteosarcoma xenograft tumor cells but not tonsil lymphocytes. Of 73 supernatants tested, 19 reacted with both osteosarcoma tumor cells and lymphocytes, while three reacted only with osteosarcoma. One of the latter hybridomas was cloned by limiting dilution to establish a line producing an IgG1 MAb (OS-1). By immunoperoxidase, this MAb stained tumor cells in surgical biopsies of primary (6 of 7) and metastatic (1) osteosarcomas and showed limited cross-reactivity with other tumors. It also cross-reacted with some basement membranes, endothelium and muscular media of blood vessels, and smooth muscle, but not with parenchymal cells of various normal tissues. This MAb may prove useful for the immunohistochemical confirmation of a diagnosis of osteosarcoma in surgical pathology.
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PMID:Production of a monoclonal antibody against a human osteosarcoma xenograft. 354 7

The effects of physical restraint and poly I:C treatment on the growth of MOPC 104E myeloma and murine osteosarcoma and survival of animals bearing such tumors were investigated. Our studies show that in the Balb/c mice with MOPC 104E myeloma the effects of restraint stress were detrimental and lead to early death of the mice. When the restraint was combined with poly I:C, during the early course of the disease, restraint stress neutralized the beneficial effects of the poly I:C treatment. These studies show that under certain circumstances, restraint stress can negate the effects of therapy. On the other hand, restraint stress produced an opposite effect in C3H/He mice with murine osteosarcoma tumor treated in the same fashion. In mice with osteosarcoma, restraint stress delayed tumor growth and increased the median survival time. When restraint stress was combined with poly I:C treatment, the mean tumor size was smaller and median survival was substantially increased over the control group. Because poly I:C therapy delayed tumor growth and increased survival in both models, efforts to strengthen this response were tested by conditioning. Our studies show the response to poly I:C as measured by elevation of the NK activity could be conditioned with camphor smell. Conditioning of the host to raise immune activity to alter the outcome of disease is a new area yet to be explored and has important clinical significance. These studies, we believe, are important because they explore the connection between mind and body and resistance to disease.
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PMID:Neural and environmental influences on neoplasia and conditioning of NK activity. 385 49

Hybrid cell lines have been derived from a fusion between mouse myeloma cells, NS1, and spleen cells from mice immunized with freshly resected osteosarcoma cells from an untreated patient. Of the 276 hybrids obtained, five secreted antibodies which bound to osteosarcoma tissues but not to autologous skin fibroblasts. The antibodies from three of these five hybrids, OST6, OST7, and OST15, reacted with all of five osteosarcoma tissues and with one chondrosarcoma tissue but not with other malignant or benign tumors. Tests of various normal tissues were negative, except for weak binding to a subpopulation of chondrocytes in articular cartilage. The reciprocal binding inhibition test showed that OST6, OST7, and OST15 antibodies were directed against different antigenic determinants.
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PMID:Detection of human osteosarcoma-associated antigen(s) by monoclonal antibodies. 617 16

An organ-specific alkaline phosphatase inhibitor, L-homoarginine, at 44.5 mM concentration inhibited [3H]thymidine uptake by C3H/He mouse osteosarcoma (OS) cells, while L-arginine, L-phenylalanine, and glycine had little effect on the uptake. This inhibitory effect of L-homoarginine persisted even after the cells were washed free of the amino acid with fresh media. L-Homoarginine did not affect [3H]thymidine uptake by mouse myeloma MOPC 104E cells. In long-term culture, 22.3 mM L-homoarginine inhibited proliferation of OS cells. L-Arginine at the same concentration inhibited the proliferation to a lesser extent. On the other hand, L-phenylalanine and glycine did not affect in vitro proliferation of OS cells. When the same number of viable OS cells was inoculated s.c. after culturing the 24 hr with 44.5 mM L-homoarginine or L-arginine, the tumor growth in mice given injections of L-homoarginine (but not L-arginine)-treated cells was delayed markedly. Electron microscopic studies indicated that the inhibiting effect on OS cell proliferation was associated with a marked increase in lysosomal granules and a decrease in virus-like structures. Similarly, biochemical assay for acid phosphatase of cell homogenates demonstrated a 2-fold increase of activity in L-homoarginine-treated cells when compared to controls and L-arginine-treated cells. Thus, L-homoarginine inhibits proliferation and alkaline phosphatase activity of mouse OS cells and appears to increase acid phosphatase activity in synthesis of lysosomal granules.
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PMID:Inhibitory effect of L-homoarginine on murine osteosarcoma cell proliferation. 617 11

An organ-specific alkaline phosphatase (AIP) inhibitor, L-homoarginine at 44.5 mM concentration inhibited 3H-thymidine uptake by mouse C3H/He osteosarcoma (OS) cells, while L-arginine, L-phenylalanine and L-glycine had little effect on the uptake. This inhibitory effect by L-homoarginine persisted even after the cells were washed free of the amino acid with fresh media. L-homoarginine did not affect 3H-thymidine uptake by mouse myeloma MOPC 104E cells. In the long-term culture, 22.3 mM L-homoarginine inhibited proliferation of OS cells. L-Arginine at the same concentration inhibited the proliferation to a lesser extent. On the other hand, L-phenylalanine and L-glycine did not affect in vitro proliferation of OS cells. When similar numbers of viable OS cells were inoculated s. c. after culturing with 44.5 mM L-homoarginine or L-arginine for 24 hr, the tumor growth in mice injected with L-homoarginine (but not L-arginine) treated cells was delayed markedly. Electron microscopic studies indicated that the inhibitory effect on OS cell proliferation was associated with a marked increase in lysosomal granules and a decrease in virus-like structures. Similarly, a biochemical assay of acid phosphatase (AcP) of the cell homogenates demonstrated two-fold increase of the activity in L-homoarginine treated cells when compared to the controls and L-arginine treated cells. Thus, L-homoarginine inhibits proliferation and AIP activity of mouse OS cells and appears to promote cell differentiation as evidenced by the increased synthesis of cytoplasmic granules and acid phosphatase activity.
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PMID:[Inhibitory effect of L-homoarginine on murine osteosarcoma cell proliferation]. 619 5


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