1966European Journal of EndocrinologyRequires access

EFFECT OF PROPYLTHIOURACIL ON THE IODINATION AND MATURATION OF RAT THYROGLOBULIN

Claude Simon, M Roques, Janine Torrésani, Serge Lissitzky

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Abstract

ABSTRACT The effect of propylthiouracil on the maturation of rat thyroglobulin in vivo has been investigated. Newly iodinated thyroglobulin dimer is labile to freezing and thawing. This observation has been used to interpret the findings in the present experiments. From experiments using rats in isotopic equilibrium with 125I, and treated with propylthiouracil or propylthiouracil and tri-iodothyronine and also given a single injection of 131I, the following conclusions were formulated 1) the appearance of iodinated S12 thyroglobulin monomer is due to the dissociation of labile iodinated thyroglobulin dimer and appears more readily if the dimer is poorly iodinated, 2) uniodinated thyroglobulin dimer is the most probable substrate for iodination in vivo, 3) maturation of thyroglobulin dimer (as shown by increasing sedimentation constant from 16—17 to 19) is accompanied by increasing amounts of iodine in the molecule, 4) it is not possible to say at present if iodination and iodothyronine formation is the cause or the consequence of thyroglobulin dimer maturation, 5) propylthiouracil might inhibit thyroglobulin maturation by decreasing iodine organification.

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ABSTRACT The effect of propylthiouracil on the maturation of rat thyroglobulin in vivo has been investigated. Newly iodinated thyroglobulin dimer is labile to freezing and thawing. This observation has been used to interpret the findings in the present experiments. From experiments using rats in isotopic equilibrium with 125I, and treated with propylthiouracil or propylthiouracil and tri-iodothyronine and also given a single injection of 131I, the following conclusions were formulated 1) the appearance of iodinated S12 thyroglobulin monomer is due to the dissociation of labile iodinated thyroglobulin dimer and appears more readily if the dimer is poorly iodinated, 2) uniodinated thyroglobulin dimer is the most probable substrate for iodination in vivo, 3) maturation of thyroglobulin dimer (as shown by increasing sedimentation constant from 16—17 to 19) is accompanied by increasing amounts of iodine in the molecule, 4) it is not possible to say at present if iodination and iodothyronine formation is the cause or the consequence of thyroglobulin dimer maturation, 5) propylthiouracil might inhibit thyroglobulin maturation by decreasing iodine organification.

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Available abstract

ABSTRACT The effect of propylthiouracil on the maturation of rat thyroglobulin in vivo has been investigated. Newly iodinated thyroglobulin dimer is labile to freezing and thawing. This observation has been used to interpret the findings in the present experiments. From experiments using rats in isotopic equilibrium with 125I, and treated with propylthiouracil or propylthiouracil and tri-iodothyronine and also given a single injection of 131I, the following conclusions were formulated 1) the appearance of iodinated S12 thyroglobulin monomer is due to the dissociation of labile iodinated thyroglobulin dimer and appears more readily if the dimer is poorly iodinated, 2) uniodinated thyroglobulin dimer is the most probable substrate for iodination in vivo, 3) maturation of thyroglobulin dimer (as shown by increasing sedimentation constant from 16—17 to 19) is accompanied by increasing amounts of iodine in the molecule, 4) it is not possible to say at present if iodination and iodothyronine formation is the cause or the consequence of thyroglobulin dimer maturation, 5) propylthiouracil might inhibit thyroglobulin maturation by decreasing iodine organification.

Key concepts: Thyroglobulin, Propylthiouracil, Chemistry, Dimer, Endocrinology, Iodine, Internal medicine, Organification

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