Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UMLS:C0029463 (osteosarcoma)
 16,637 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Three murine hybridomas (TMMR-1-3) were developed by repeated immunizations of mice with four different human osteosarcoma cell lines in an alternating sequence of inoculations. The monoclonal antibodies were screened for reactivities to cultured cell lines and tissue sections of osteosarcomas using flow cytometry and immunohistochemical techniques. TMMR-2 is a highly specific antibody (IgG1) that reacted with all 14 osteosarcoma tumors and eight human osteosarcoma cell lines tested, including the established human osteosarcoma cell lines HOS and Saos-2. Benign neoplastic cells from two osteoblastomas, osteoblasts from regions of reparative osteoid formation and neonatal new bone, are also reactive with TMMR-2. TMMR-1 has mesenchymal specificity while TMMR-3, although reactive with osseous differentiated cells, also reacted with mitotic cells of all cell types. Characterization of antigen structure by Western immunoblotting revealed that TMMR-2 reacted with a 100 degrees C heat labile mercaptoethanol-sensitive Mr 26,000 protein, and TMMR-3 recognized a mercaptoethanol-resistant Mr 97,000 protein whereas TMMR-1 reacted with a series of bands from 65,000 to 85,000 molecular weight, all of which were mercaptoethanol sensitive. TMMR-1 and TMMR-2 monoclonal antibodies showed complement-independent inhibition of [3H]thymidine incorporation into DNA, but did not exhibit cytotoxic activity. The results suggest that TMMR-2 is a specific antibody that recognizes an osteoblast/osteocyte surface antigen present in normal, reactive, and neoplastic disorders of bone. The inhibitory effects on DNA synthesis in cultured osteosarcoma cells by TMMR-2 indicate an important cell growth/proliferation role of this surface antigen. These monoclonal antibodies, in combination with other known antibodies, can be used to characterize mesenchymal cell surface antigenic structure and differentiation.
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PMID:Monoclonal antibody to human osteosarcoma: a novel Mr 26,000 protein recognized by murine hybridoma TMMR-2. 229 50

Using a somatic cell hybridization technique, four murine monoclonal antibodies (three immunoglobulin M and one immunoglobulin G3) were produced against a human neuroblastoma cell surface glycolipid antigen. They reacted strongly with all human neuroblastoma tumor-containing specimens and six of eight human neuroblastoma cell lines. More than 98% of each neuroblastoma cell population possessed this surface antigen, and in the presence of complement, 100% of them were killed. While melanoma and osteogenic sarcoma carried this antigen, leukemia and most Ewing's and Wilms' tumors did not. There was no cross-reaction with 30 normal or remission bone marrow samples and none with normal human tissues other than neurons in vitro. This antigen was neuraminidase sensitive, separable on thin-layer chromatogram, and did not modulate after combining with the monoclonal antibodies. These antibodies could detect less than 0.1% tumor cells deliberately seeded in the bone marrow samples. Because of their unique properties, these monoclonal antibodies may have diagnostic and therapeutic potentials.
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PMID:Monoclonal antibodies to a glycolipid antigen on human neuroblastoma cells. 258 Jun 25

Monoclonal antibody 791T/36 directed against surface antigen on the human osteosarcoma cell line and cross-reacting with surface antigen p72 presenting on human PHA-stimulated T-lymphoblasts was used in analysis of p72 antigen expression on human mononuclear peripheral blood cells, between 2-4 days of culture. Using FACS-IV system and fluorescence microscope, it was shown that expression of p72-antigen is dependent on PHA-stimulation and the ability of lymphocytes proliferation. The expression of p72 preceding the entry of the cells into the cell cycle. This is not significantly dependent of cell size, stage of the cycle, and RNA-transcription activity. In PHA-stimulated cultures, between 2-4 days, the number of lymphoblasts expressing enough receptors for 791T/36 monoclonal antibody is sufficient to exhibit a distinct effect of Ricin A-chain conjugated with 791T/36 over 50% inhibition of 3H-Thymidine incorporation into the cells. These observations emphasises the importance of cross-reactions in cases using immunotoxins.
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PMID:[Study of expression of surface antigen p72 using monoclonal antibody 79IT/36 and the effect of ricin A chain-bound 79IT/36 on phytohemagglutinin-stimulated human lymphocytes]. 261 66

Monoclonal antibody 791T/36, directed against surface antigen on the human osteosarcoma cell line (791T), and cross-reacting with surface antigen p72 expressed on activated (PHA, MLR) human peripheral blood mononuclear cells (PBM), was used in analysis of p72 antigen in vitro. Using FACS-IV system and fluorescence microscope, it was shown that expression of p72 antigen on PBM cells is dependent on phytohaemagglutinin (PHA) stimulation, and alloantigens in mixed lymphocyte reaction (MLR). The increase of p72 expression is always connected with lymphocytes proliferation activity (FACS-IV analysis and 3H-Thymidine incorporation assay). The expression of p72 is not significantly dependent on cell size, and stage of the cell in the cell cycle. A suggestion, that p72 is a one of so-called "proliferation antigens" is discussed. Present study emphasizes a problem of cross-reactivity in the context of possible errors in diagnosis and therapy, when a monoclonal antibody cross-reacts with cells other than intendent target cells.
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PMID:Cross-reaction of 791T/36 monoclonal antibody with immunological activated human peripheral blood mononuclear cells. 326 80

The relationship between total surface antigen expression per cell (means) - measured by fluorescence-labelled monoclonal antibodies (fluorescence-histograms) and the distribution of cells in the cell cycle (DNA-histograms) and size-scattergrams (cell sorter FACS-IV) were analysed in drug treated unsynchronized and synchronized osteogenic sarcoma cells (2OS) in vitro. Drugs with various sites of action in the cell cycle were used. Adriamycin, Vindesine, in concentrations applied accumulate cells in G2 + M phase. Methotrexate arrests cells in the boundary of G1/S phase. Size-scattergram and DNA-histogram analysis have shown that the entrance of cells to the cell cycle is usually accompanied by an increase in the cells size and amount of their DNA. The size of the cells influenced antigenic expression much more than the distribution of the cells in the various cell cycle phases: in the bigger cells the expression per cell was more pronounced. The increase of antigen expression was the highest for Adriamycin and for Methotrexate treated cells. However, this increase was limited and never exceeded plus 50% in relation to the control. This relatively low difference resulted from the fact, that a given phase of the cell cycle included cells markedly heterogenic in respect of size and antigenic content. It was also shown that lower concentration of serum in culture medium and confluent growth of older cultures decrease surface antigen expression per cell.
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PMID:Analysis of surface antigen expression per cell of human osteogenic sarcoma cells by fluorescence-labelled monoclonal antibodies. 659 41

Ganglioside GD2 is a tumor-associated surface antigen found in a broad spectrum of human cancers and stem cells. They include pediatric embryonal tumors (neuroblastoma, retinoblastoma, brain tumors, osteosarcoma, Ewing sarcoma, rhabdomyosarcoma), as well as adult cancers (small cell lung cancer, melanoma, soft tissue sarcomas). Because of its restricted normal tissue distribution, GD2 has been proven safe for antibody targeting. Anti-GD2 antibody is now incorporated into the standard of care for the treatment of high-risk metastatic neuroblastoma. Building on this experience, novel combinations of antibodies, cytokines, cells, and genetically engineered products all directed at GD2 are rapidly moving into the clinic. In this review, past and present immunotherapy trials directed at GD2 will be summarized, highlighting the lessons learned and the future directions.
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PMID:GD2-targeted immunotherapy and radioimmunotherapy. 2544 Jun 5