ABSTRACT
Rats were irradiated by 8Gr in a doze power of 2.33 R per second. A portion of animals were injected subcutaneously with a cow colostrum polypeptide (CP) in a doze of 1 mg per g of body weight before the irradiation and daily after the irradiation during 4 days. In irradiated rat liver nuclei injected with CP the lipid peroxide oxidation was restored. At 90th day after the irradiation the production of dienes and dieneketones in liver nuclei oscillated in normal limits. The structure and cytochrome-c-oxidase activity of the nuclei was restored to 60-90th day after the irradiation.
Subject(s)
Cell Nucleus/drug effects , Colostrum , Lipid Peroxidation/drug effects , Liver/drug effects , Peptides/pharmacology , Animals , Cattle , Cell Nucleus/enzymology , Cell Nucleus/pathology , Cell Nucleus/radiation effects , Electron Transport Complex IV/drug effects , Gamma Rays , Injections, Subcutaneous , Lipid Peroxidation/radiation effects , Liver/enzymology , Liver/pathology , Liver/radiation effects , Male , Rats , Time FactorsSubject(s)
Biological Products/therapeutic use , Liver/drug effects , Milk , Radiation Injuries, Experimental/drug therapy , Animals , Cell Nucleus/drug effects , Cell Nucleus/physiology , Cell Nucleus/ultrastructure , Lipid Peroxidation/drug effects , Liver/cytology , Liver/physiology , Radiation Injuries, Experimental/physiopathology , RatsABSTRACT
Intracellular distribution of labeled cotoran was studied. 3H-cotoran was shown to penetrate through the nuclear membrane to accumulate uneventfully in the intranuclear components. An insignificant amount of 3H-cotoran was associated with the nucleoplasm and the outer nuclear membrane. At the same time, essential radioactivity was observed in the proteins of the nuclear matrix (up to 30%) and in non-histone proteins of chromatin (up to 60%). Acception of 3H-cotoran on metaphase chromosomes of cultured cells as well as specificity of cotoran binding with non-histone proteins of chromatin in vivo and in vitro was studied by radioautography. It was revealed that cotoran was translocated into the interphase nuclei to be accepted by metaphase chromosomes of the HeLa line cells and fibroblasts in human embryo, and specifically, in receptor-like manner, bound to chromatin proteins.
Subject(s)
Cell Nucleus/metabolism , Herbicides/pharmacokinetics , Liver/metabolism , Methylurea Compounds/pharmacokinetics , Animals , Cells, Cultured/metabolism , Chromatin/metabolism , Fibroblasts/metabolism , HeLa Cells/metabolism , Humans , Protein Binding , Rats , Rats, Inbred Strains , TritiumABSTRACT
The work concerns a new approach to evaluating the receptor and hormone-receptor complex specific interaction with DNA and revealing the cause of the absence of the hormone-receptor complex acceptation with HeLa cell chromosomes. It has been shown that hormone-receptor complexing should precede specific interaction with DNA. The purified receptor-thyroxin complex is saturatable and specifically competes with Hae III restrictase, protecting specific sites of DNA recognition from this enzyme. Specificity of the hormone-receptor complex interaction with DNA depends on the sequences surrounding Hae III restriction site. The HeLa cell hormone-receptor complex does not interact with the recognition site for the normal hormone-receptor complex.
Subject(s)
Receptors, Cell Surface/genetics , Thyroxine/genetics , Cells, Cultured , Cytoplasm/analysis , DNA/analysis , Embryo, Mammalian , Female , Fibroblasts , HeLa Cells , Humans , Pregnancy , Translocation, GeneticABSTRACT
The influence of cAMP-dependent pig brain protein kinase and its subunits on transcription in vitro was studied. The increase in the template activity of chromatin isolated from the nuclei after treatment with the catalytic subunit was observed. The regulatory subunit of protein kinase was found to increase the number of binding sites for RNA polymerase on chromatin. The cAMP-dependent pig brain protein kinase was found to phosphorylate the sigma-factor of Escherichia coli RNA polymerase. This phosphorylation led to the increase of the RNA polymerase activity on phage lambda DNA. The nuclear translocation of the protein kinase and its subunits was shown to take place. In the cells with a low cAMP level (SV40 3T3) the transfer of the regulatory subunit to the nucleus was not detected. Only upon addition of cAMP and a subsequent formation of the cAMP-regulatory subunit complex, nuclear translocation was observed in these cells. The dependence of nuclear translocation of the cAMP-dependent protein kinase on cAMP level in the cell is proposed.
Subject(s)
Brain/metabolism , Cell Nucleus/metabolism , Protein Kinases/metabolism , Transcription, Genetic , Animals , Chromatin/metabolism , Cyclic AMP/pharmacology , DNA-Directed RNA Polymerases/metabolism , Enzyme Activation , Karyotyping , Kinetics , Macromolecular Substances , Swine , Templates, GeneticABSTRACT
It is shown that 125J-thyroid hormones are localized on the structures of the interphasic nucleus and metaphasic chromosomes of cultured fibroblasts of 8--10-day human embryos. At the same time, the labelled thyroid hormones, though localizing in the interphasic nuclei of HeLa cells, are not accepted, unlike normal cells, by their metaphasic chromosomes. It is suggested that during transformation the acceptor ares of the HeLa cells genome lost their property to bind their own receptor complexes with thyroid hormones.