ABSTRACT
The effect of experimental bovine herpes virus (BHV) type I rhinotracheitis on the surfactant system phospholipids in calves was examined. A stimulated exocytosis of pulmonary surfactant phospholipids in the acute phase of the disease was documented biochemically and ultrastructurally. The data presented were assumed as an evidence of the involvement of pulmonary surfactant in lung defense.
Subject(s)
Infectious Bovine Rhinotracheitis/metabolism , Lipid Metabolism , Pulmonary Surfactants/metabolism , Animals , Bronchoalveolar Lavage Fluid/chemistry , Bronchoalveolar Lavage Fluid/metabolism , Cattle , Chromatography, Gas , Chromatography, Thin Layer , Lipids/analysis , Male , Pulmonary Surfactants/analysis , Time FactorsSubject(s)
Infectious Bovine Rhinotracheitis/drug therapy , Pulmonary Surfactants/drug effects , Suramin/therapeutic use , Animals , Bronchoalveolar Lavage Fluid/chemistry , Bronchoalveolar Lavage Fluid/cytology , Cattle , Drug Evaluation, Preclinical , Infectious Bovine Rhinotracheitis/metabolism , Lung/chemistry , Macrophages, Alveolar/chemistry , Male , Pulmonary Surfactants/analysis , Time FactorsABSTRACT
The binding of I125-triiodothyronine by male thyroidectomized rat liver nuclei and mitochondria in vivo and in vitro was studied. Labeled triiodothyronine was bound by the liver nuclei and mitochondria proteins. 90% radioactivity was bound by the nuclear nonhistone proteins. The binding of I125-triiodothyronine to the nuclei and mitochondria protein receptors was inhibited by unlabeled triiodothyronine and ICl. It is suggested that aromatic amino acids serve as the binding sites of the protein receptors, and that iodine atoms in the thyroid hormone molecules participated directly in the binding process.
Subject(s)
Cell Nucleus/metabolism , Liver/ultrastructure , Mitochondria, Liver/metabolism , Receptors, Cell Surface/metabolism , Triiodothyronine/metabolism , Animals , Binding, Competitive , In Vitro Techniques , Iodine Radioisotopes , Isotope Labeling , Male , RatsABSTRACT
Iodine ions exhibited the thyroxin-like effect on incorporation of 1-14C-leucine into proteins of isolated mitochondria and microsomes of thyroidectomized rats in vitro. Thyroxin, triiodothyronine (T3) and ICl increased the incorporation of 1-14C-leucine into proteins of isolated mitochondria of thyroidectomized rats, but did not affect the protein synthesis in microsomes in vitro. Rifampycin and olivomycin abolished completely the stimulating effect of T3 and ICl on incorporation of the label into mitochondrial proteins. The thyroid hormones and iodine ions stimulated protein synthesis in vitro in liver microsomes of thyroidectomized animals only after preincubation with mitochondria or nuclei. In these conditions preincubation with mitochondria elevated the rate of 1-14C-leucine incorporation into microsomal proteins 2--2.5-fold. In similar experiments with nuclei--4--4.8-fold stimulation was detected. Thyroid hormones and iodine ions stimulated synthesis of specific factors in mitochondria (MBS) and in nuclei (NBS) of thyroidectomized rat liver tissue, which increased the protein synthesis in isolated microsomes in vitro. Synthesis of MBS- and NBS-factor required the presence of all the four ribosetriphosphates (ATP, GTP, UTP, CTP) and was inhibited completely by olivomycin; rifampycin blocked only the MBS factor synthesis. NBS- and MBS-factors appear to be RNA (mRNA), synthesized in nuclei and mitochondria, which are transported into the incubation media and translated by ribosomes.
