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Biomedical subjects

A H Coleoni

Publications and source records attributed to A H Coleoni.

31 records · Page 2Linked to original sources
PubMed1981

Effect of epinephrine and 5-hydroxytryptamine on in vitro thyroid iodine organification.

The effect of epinephrine (E) and 5-hydroxy-tryptamine (5-HT) on some elements involved in thyroid iodine organification was studied using a bovine thyroid subcellular fraction sedimented at 30 000 g. 131I-incorporation into particulate proteins and into tyrosine ws increased by 10(-3) M and 10(-5) M E and 5-HT. This effect was inhibited by 6-n-propyl-2-thiouracil and by catalase. In the presence of these amines the activity of NADPH-cytochrome c reductase was not modified. Both E and 5-HT were able to generate H2O2 when added to the particulate fraction as measured by the oxidation of o-dianisidine. H2O2 generation and [131I]iodotyrosine formation were inhibited by pargyline, a monoamine oxidase (MAO) inhibitor. Tyramine, a specific substrate for thyroid MAO, produced H2O2 and increased [131]iodotyrosine formation. This effect was higher when compared to the effect elicited by E or 5-HT. The stimulatory effects of tyramine were blocked by pargyline. The action of tyramine on H2O2 generation and [131I]iodotyrosine formation was diminished when E or 5-HT were incorporated to the system. From these results it suggested that E and 5-HT serving as MAO substrates would generate H2O2 and in this way increase the thyroid iodine organification. On the other hand, these amines would be able to reduce the increased H2O2 generation induced by tyramine and thus decrease the iodination process. These findings could explain the stimulatory or inhibitory effects of biogenic amines on thyroid function which are dependent on the previous thyroid activity.

Animals↗
PubMed1980

Description and partial characterization of thyroid hormone-specific and thyroid hormone-dependent rat liver nuclear proteins.

A fraction of readily elutable rat liver nuclear proteins (nuclear globulins), analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, contains two proteins which reflect the thyroid status of the animal. The larger (n-band) protein is abundant in normal rat nuclei but diminished in hypothyroidism by thyroidectomy or hypophysectomy and restored with T3 treatment. It is also diminished in starvation, during which time T3 treatment of concurrent hypothyroxinemia is ineffective in tis restoration. Refeeding restores the n-band protein in starved normal rats but not in starved thyroidectomized (Tx) rats. GH does not restore this protein in either Tx or hypophysectomized (Hx) rats. The dual requirements of euthyroidism and adequate nutrition imply that the n-band protein is thyroid hormone dependent but not thyroid hormone specific. The smaller of the two nuclear globulins, the t-band protein, is prominent in Tx or Hx rats and is not altered by additional hypometabolic factors (starvation) or by nonthyroid hormone related hypermetabolic stimuli (refeeding or GH treatment of Hx rats). It is reduced in normal or T3-treated Tx or Hx rats regardless of simultaneous hypometabolic states (starvation or nonthyroid hormone-related deficiencies of hypopituitarism) or hypermetabolic states (refeeding, liver regeneration, or hyperthyroidism). The t-band protein thus appears to be inversely thyroid hormone specific in its concentration. Electrophoretic and chromatographic analysis suggest that the n-band protein is a 125,000 mol wt subunit of a 290,000 mol wt holoprotein. The t-band protein is a 70,000 mol wt peptide which exists, in part, as a monomer but largely as a subunit of a protein complex with a mol wt greater than 100,000.

Animals↗
PubMed1980

Congenital goitre due to "thyroid peroxidase-iodinase defect".

A 16-year-old male cretin with congenital goitrous hypothyroidism and 95% discharge in the perchlorate test underwent thyroidectomy. Thyroid studies disclosed negligible peroxidase (TPO) activity in the tyrosine iodinase assay, 6 nmoles I- inc./g (normals: 220-410). Using the same particulate preparations, a high activity was obtained in the guaiacol assay, 485 U/mg vs. 176 U/mg of a control gland. Goitre TPO was solubilized by treating the thyroid pellets with deoxycholate, trypsin and acetone. Soluble goitre TPO was further purified on Sephadex G-200. By this procedure we obtained a single peak of enzyme activity for oxidizing guaiacol, although no activity was found for iodinating tyrosine. I2 formation, as measured by the triiodide assay, was only 28% of that expected for normal TPO when compared for guaiacol oxidation. It is concluded that this abnormal TPO was the cause of the congenital hypothyroidism of the patient. We suggest the term "thyroid peroxidase-iodinase defect" for defining this newly found inborn error.

Adolescent↗
PubMed1978

Thyroid hormone receptors from liver nuclei: characteristics of receptor from normal, thyroidectomized, and triiodothyronine-treated rats; measurement of occupied and unoccupied receptors, and chromatin binding of receptors.

The capacity and characteristics of liver nuclear receptors for T3 have been compared in normal rats, thyroidectomized rats, and thyroidectomized rats treated with different doses of T3. Receptor capacity was unchanged, with the exception of a decrease of total nuclear receptors in rats treated with 15 microgram T3/day, which is believed due to lack of complete dissociation of the endogenously bound hormone during incubation in vitro. During incubation of the isolated nuclei in 0.32 M sucrose plus 1 mM MgCl2 plus 20 mM Tris-Cl buffer, pH 7.85, about 50% of the nuclear receptors were released to the medium and no effect of T3 treatment on the amount released was found. The affinity of the receptors free in solution was 50% higher than that of receptors retained in the nuclei. Receptors from normal and thyroidectomized rats were studied by ultracentrifugation through sucrose gradients. No difference in sedimentation coefficient was found between the groups of rats, whether the receptors were filled with the labeled hormone before or after centrifugation and separation of the gradient fractions. Occupied and unoccupied receptor capacity was estimated by incubation of receptor preparations at 20 and 0 C for 2 h. Observed capacity at 20 C represents unoccupied plus approximately 80% of occupied sites, while observed capacity at 0 C represents unoccupied plus 10% of occupied site. Binding of receptors to the chromatin was studied by incubating nuclear extract from normal rats with chromatin and measuring the amount of receptor that was not bound and remained free in the supernatant. Receptor not bound to chromatin was incubated at 0 and 20 C, with a saturating concentration of [125I]T3, to measure occupied and unoccupied sites. Both occupied and unoccupied receptor decrease in the supernatant after incubation with the chromatin when the concentration of chromatin in the incubation medium is increased. No saturation of the chromatin-binding sites was achieved by increasing the concentration of receptor several-fold, and no difference in the binding of occupied and unoccupied receptors to chromatin was observed. These data rule out the possibility that the concentration of receptors in the nucleus is under control of the hormone. Major molecular changes of the receptor that could be induced by T3, such as dissociation into subunits, are also ruled out. Binding studies to the chromatin are not necessarily conclusive, as nonspecific binding may be masking the physiological binding of the receptors to a limited number of acceptor sites.

Animals↗
PubMed1977

Effects of amiodarone on thyroid iodine metabolism in vitro.

Since alterations of thyroid function have been reported in patients treated with amiodarone, 2-butyl,3-(4-diethylaminoethoxy-3,4-diiodo, benzoyl) benzufuran, the effects of this drug on the active iodide transport, organic iodine formation, thyroid peroxidase and the enzymatic iodotyrosine deiodination, were studied. In pig thyroid slices the iodide transport was affected by amiodarone at concentrations of 10(-4) M and 10(-5) M, showing a decrease of T/M (tissue/medium) ratios of 20% and 23%, respectively. Lower concentrations produced no significant differences from the controls. Iodotyrosine synthesis was only, but poorly, affected by 10(-4) M and 10(-5) M amiodarone. Inhibition of the DIT formation was greater than that produced for MIT. Thyroid peroxidase activity, as measured by the tyrosine-iodinase assay, showed a 20% decrease at 10(-3) M amiodarone. None of the other concentrations have affected the activity of the enzyme, except for 7% at a concentrations of 10(-4) M. The iodotyrosine deiodination was affected by amiodarone only at a concentration of 10(-3) M and 10(-4) M. The inhibitions were of 22.5% and 16.8%, respectively. We have concluded that, under the conditions of our study, amiodarone per se does not affect the intrathyroidal iodine metabolism in concentrations which are usually present in the sera of patients treated with this drug. However, it is not possible to rule out an in vivo direct action, if amiodarone is substantially concentrated in the human thyroid gland.

Amiodarone↗