[Effect of insulin on thyroid function].
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Biomedical subjects
Publications and source records attributed to C Blum.
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A TRH fixation in vitro occurs at the level of the human polynuclear neutrophil, which suggests putative membrane receptor (s) for the hypothalamic hormone. After TRH administration, enzyme modifications (myeloperoxydase, alkaline phosphatase) and metabolism changes (PAS, Sudan black) happen in vivo within the neutrophil, showing a functional activation of that blood cell. Two processes may be considered to explain those data: 1) the TRH is directly fixed, as observed in vitro; 2) a mediate hormone (TSH, T4, T3) is released capable of binding the granulocyte membrane.
In the blood of intact dogs, insulin increases the labelled thyroid hormones (PBI) by about 30% and doubles the T3 level. In athyreotic insulin-administered dogs, the circulating T4 and T3 remain at more or less unvarying values, the plasma disappearance slope of radiothyroxine is not altered. Such data suggest that without the thyroid gland, insulin has no action on the level of the blood thyroid hormones.
The effects of thyrotropin-releasing hormone (TRH) on a group of 12 normal euthyroid subjects (8 males, 4 females) were analyzed through the metabolic response of oxidoreduction chains of red cells and leucocytes of venous blood. During the reaction of the pituitary-thyroid glandular system (increase of circulating TSH and T-3) to hypothalamic stimulation, the authors have demonstrated: (1) a significant reduction in erythrocytic GSH rate with no anomaly of in vitro stability; (2) an obvious stimulation of the two dehydrogenases of the leucocyte pentose shunt: G6PD and 6PGD. Regarding red cells, the same enzymes do not undergo any quantitative modification, and no behavioral difference of acid phosphatase is observed. The authors also refer to the biochemical mechanism which is involved for regulation of the oxidoreductive metabolism in the molecular response to hormonal or hrehormonal solicitations.
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Mouse L 929 cultured fibroblasts revealed saturable and high affinity nuclear receptors for triiodothyronine. 125I-T3 bound rapidly to intact cells, with a steady state achieved between 1-2 h at 37 C. By Scatchard estimation, the maximal binding capacity averaged 18 fentomoles of T3 bound per 100 microgram of DNA, which approximated to 2,000 sites per cell nucleus; the apparent equilibrium association constant Ka averaged 4.90 x 109 LM-1. The relative affinity of T3 analogs tested correlated with their respective thyromimetic potency. Limited capacity, high affinity and specificity of T3 nuclear receptors in these fibroblasts were found to have properties similar to those previously observed in other cell lines or tissues. Such cultured fibroblasts may provide a useful experimental model to investigate the intracellular biological effects of thyroid hormones.
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