ovalbumin and Cell-Transformation--Neoplastic

Topics: Animals; Antibody Affinity; Antibody Formation; Blood Bactericidal Activity; Cell Transformation, Neoplastic; Chickens; Dose-Response Relationship, Radiation; Hematopoiesis; Hypersensitivity, Delayed; Immune Tolerance; Immunity, Cellular; Leukemia Virus, Murine; Lymphocytes; Lymphoma; Mice; Muramidase; Neutrophils; Ovalbumin; Rabbits; Radiation Chimera; Radiation, Ionizing; Rats; T-Lymphocytes; T-Lymphocytes, Regulatory; X-Rays

Avidin, a high-affinity biotin-binding protein of chicken oviduct, was recently found to be synthesized and secreted by damaged or virus-transformed chicken embryo fibroblasts and by chicken macrophages. We have now localized avidin in fibroblasts that were transformed by Rous sarcoma virus. The cells released to the culture medium up to 12 micrograms avidin per 10(6) cells, as judged by the [14C] biotin-binding method. In immunofluorescence microscopy, avidin was localized to the cytoplasm of transformed and of untransformed damaged cells. Treatment with the ionophore monensin was used to determine whether avidin is processed through the Golgi region, which was localized using rhodamine-labeled wheat germ agglutinin. Under these conditions avidin was largely confined to the Golgi region. At the electron microscopic level avidin could be localized to the endoplasmic reticulum of transformed cells, using anti-avidin antibodies and the avidin-biotin-peroxidase complex (ABC) technique. Biotinyl peroxidase did not stain the endogenous avidin in cell layers processed for light or electron microscopy indicating that its biotin-binding sites were either saturated or denaturated. The possibility that endogenous avidin in tissues or cell cultures may bind biotinylated reagents should be controlled for in techniques involving the avidin-biotin interaction.

Topics: Animals; Antigen-Antibody Complex; Avian Sarcoma Viruses; Avidin; Cell Transformation, Neoplastic; Cells, Cultured; Chick Embryo; Fibroblasts; Fluorescent Antibody Technique; Immunoenzyme Techniques; Microscopy, Electron; Ovalbumin

Brief micrococcal nuclease digestion of chick embryonic red blood cells results in preferential excision and solubilization of monomer nucleosomes associated with beta-globin sequences and also 5'-sequences flanking the beta-globin gene. Both regions are DNAse-I sensitive in nuclei. Such salt-soluble nucleosomes are enriched in all four major HMG proteins but HMG1 and 2 are only weakly associated. These nucleosomes appear to have lost much of the DNAse-I sensitivity of active genes. The HMG14 and 17-containing salt-soluble nucleosomes separated by electrophoresis are not DNAse-I sensitive and contain inactive gene sequences as well as active sequences. Reconstitution of HMG proteins onto bulk nucleosomes or chromatin failed to reveal an HMG-dependent sensitivity of active genes as assayed by dot-blot hybridization and it was found that the DNAse-I sensitivity of ASV proviral sequences as assayed by dot-blot hybridization was not HMG-dependent. These results indicate that higher order chromatin structures might be responsible for nuclease sensitivity of active genes.

Topics: Animals; Avian Sarcoma Viruses; Base Sequence; Cell Transformation, Neoplastic; Chickens; Deoxyribonuclease I; DNA; Endodeoxyribonucleases; Erythrocytes; Genes; Globins; Micrococcal Nuclease; Nucleic Acid Hybridization; Nucleosomes; Ovalbumin; Rats

Topics: Animals; Cell Aggregation; Cell Transformation, Neoplastic; Cell Transformation, Viral; Concanavalin A; Erythroblasts; Erythrocyte Membrane; Erythrocytes; Friend murine leukemia virus; Gelatin; Mice; Microscopy, Electron, Scanning; Microvilli; Muramidase; Ovalbumin; Peptides; Polylysine; Proteins; Sarcosine; Surface Properties

Topics: Animals; Antigens; Cell Transformation, Neoplastic; Cells, Cultured; Chemical Phenomena; Chemistry; Cytotoxicity, Immunologic; Dialysis; Female; Guinea Pigs; Hot Temperature; Immunosuppressive Agents; Interleukin-2; Leukemia, Lymphoid; Lymphocyte Activation; Male; Molecular Weight; Ovalbumin; Phytohemagglutinins; Trypsin

Topics: Animals; Antigens, Neoplasm; Cell Transformation, Neoplastic; Clone Cells; Epitopes; Female; Haptens; Lymphoma; Male; Mice; Mice, Inbred C57BL; Neoplasms, Experimental; Ovalbumin; Retroviridae; T-Lymphocytes

Topics: Animals; Cell Transformation, Neoplastic; Culture Media; Cytotoxicity, Immunologic; Guinea Pigs; Immunity, Cellular; Leukocytes; Lymphokines; Lymphotoxin-alpha; Male; Mitogens; Neoplasms, Experimental; Ovalbumin; Radionuclide Imaging

Topics: Animals; Antigen-Antibody Complex; Cattle; Cell Membrane; Cell Transformation, Neoplastic; Hot Temperature; Immunoglobulin G; Mast-Cell Sarcoma; Mice; Mice, Inbred DBA; Ovalbumin; Receptors, Fc; Rosette Formation; Serum Albumin, Bovine; Solubility

Topics: Alpharetrovirus; Cell Division; Cell Line; Cell Transformation, Neoplastic; Cell Transformation, Viral; Genes; Genes, Viral; Globins; Ovalbumin; RNA, Messenger; Transcription, Genetic