Pavlović-Hournac M, Delbauffe D
Horm Metab Res. 1975 Nov;7(6):492-8. doi: 10.1055/s-0028-1093711.
The comparative study of the in vivo synthesis of thyroglobulin and proteins other than thyroglobulin was carried out in thyroid glands from animals submitted to different levels of TSH stimulation. The different levels of hormonal stimulation modify neither the rate of labeling after injection of the isotope, nor the level of the free labeled amino acid in the glands (percent of the total uptake), but they have a very significant effect on the level of incorporation of the isotope into total proteins. In hypostimulated thyroids the total protein synthesis is very much reduced, while in hyperstimulated glands it is significantly increased. In both hyper- and hypostimulated animals, the proportion of radioactivity bound to the particulate protein fraction is higher than in control rats. However, the solubilization by digitonine of these proteins is lower in hypostimulated and higher in hyperstimulated animals than in controls. Thyroglobulin synthesis is significantly modified qualitatively and quantitatively in both hypo- and hyperstimulated glands. Qualitative modifications are characterized by a changed ratio of 19 S/12 S molecules with respect to the controls. This is probably caused by a more important dissociation of 19S molecules, due to the lower level of halogenation in both hypo- and MTU treated glands. The quantitative modifications of thyroglobulin synthesis, expressed either in absolute values (DPM/mg of tissue), or relatively to the total proteins (percent of total newly formed proteins), are characterized by a very important inhibition of this synthesis in hypostimulated glands, and its stimulation in glands chronically submitted to the TSH action. The modifications of synthesis observed for the proteins other than thyroglobulin are less significant in both types of treated glands than are those observed for thyroglobulin. The level of hormonal stimulation has no effect on the distribution of these proteins between soluble and the particulate fraction, but seems to have a slight effect on the solubilization of the latter ones. Comparative evaluation of the TSH effect on the synthesis of different thyroidal proteins shows that it has a much more specific and significant action on thyroglobulin than on other proteins. The differential effect of TSH on the synthesis of thyroglobulin and proteins other than thyroglobulin suggests that different mechanisms may exist by which TSH regulates the synthesis of these two types of proteins.
对处于不同促甲状腺激素（TSH）刺激水平的动物甲状腺中甲状腺球蛋白及甲状腺球蛋白以外的蛋白质的体内合成进行了比较研究。不同水平的激素刺激既不改变注射同位素后的标记率，也不改变腺体中游离标记氨基酸的水平（占总摄取量的百分比），但它们对同位素掺入总蛋白的水平有非常显著的影响。在刺激不足的甲状腺中，总蛋白合成大大减少，而在刺激过度的腺体中则显著增加。在刺激过度和刺激不足的动物中，与颗粒蛋白部分结合的放射性比例均高于对照大鼠。然而，与对照相比，刺激不足的动物中这些蛋白经洋地黄皂苷溶解的程度较低，而刺激过度的动物中则较高。在刺激不足和刺激过度的腺体中，甲状腺球蛋白的合成在质量和数量上均有显著改变。质量改变的特征是与对照相比，19S/12S分子的比例发生变化。这可能是由于在刺激不足和经甲硫氧嘧啶（MTU）处理的腺体中卤化水平较低，导致19S分子解离更为明显。甲状腺球蛋白合成的数量改变，无论是以绝对值（每分钟衰变数/毫克组织）表示，还是相对于总蛋白（新形成总蛋白的百分比）表示，其特征都是在刺激不足的腺体中该合成受到非常重要的抑制，而在长期接受TSH作用的腺体中则受到刺激。在两种处理类型的腺体中，观察到的甲状腺球蛋白以外的蛋白质合成改变不如甲状腺球蛋白明显。激素刺激水平对这些蛋白在可溶性部分和颗粒部分之间的分布没有影响，但似乎对后者的溶解有轻微影响。对TSH对不同甲状腺蛋白合成的作用进行比较评估表明，它对甲状腺球蛋白的作用比对其他蛋白更具特异性和显著性。TSH对甲状腺球蛋白和甲状腺球蛋白以外的蛋白质合成的差异作用表明，可能存在不同的机制，通过这些机制TSH调节这两种类型蛋白质的合成。
