Protein metabolism in hypo- and hyperstimulated rat thyroid glands. I. Protein synthesis of different thyroidal proteins.
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.
D000818:Animals; D004072:Digitonin; D006980:Hyperthyroidism / Q000139:chemically induced / Q000378:metabolism*; D007016:Hypophysectomy; D007037:Hypothyroidism / Q000139:chemically induced / Q000378:metabolism*; D007700:Kinetics; D008779:Methylthiouracil; D014176:Protein Biosynthesis / Q000187:drug effects; D051381:Rats; D013954:Thyroglobulin / Q000096:biosynthesis; D013961:Thyroid Gland / Q000187:drug effects / Q000378:metabolism*; D013974:Thyroxine
D013954:Thyroglobulin; D004072:Digitonin; D013974:Thyroxine; D008779:Methylthiouracil