EFFECT OF IODIDE AND THYROTROPHIN ON IN VITRO 14C-AMINO ACID INCORPORATION INTO RAT THYROID PROTEINS

Abstract

ABSTRACT Thyroid lobes from rats on normal (NID) or low iodine (LID) intake were incubated for 4 hours in vitro in the presence of 14C-amino acids. The 14C-amino acid incorporation into thyroid protein was significantly higher in thyroids from LID than from NID fed rats, 7.82 ± 1.01 % (mean ± sd) of total radioactivity of the incubation mixture per 100 mg tissue compared to 3.74 ± 0.60 % respectively. Thyrotrophin (TSH) in vitro did not influence the 14C-amino acid incorporation. Iodide in concentration 10−7 m and higher decreased 14C-radioactivity incorporation into protein by 19.40 ± 3.06 and 26.59 ± 4.06 % of the control value for NID and LID rats respectively. This effect of iodide did not depend on iodine organification and was not influenced by the changes of free amino acids pool. There were no significant differences in the relative concentration of 14C-labelled thyroglobulin and total 14C-thyroid protein. Differential fragility demonstrable by unfolding or dissociation was observed between different classes of thyroglobulin. The fragility was increasing from the old non-labelled molecules to newly iodinated and newly synthesized ones. It is concluded that iodide has a direct intrathyroidal blocking effect on thyroid protein synthesis which may contribute to its antigoitrogenic action. The lack of in vitro stimulation of protein synthesis by TSH remains unexplained.