JOE
HOME HELP CONTACT US SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Journal of Endocrinology (1991) 128, 239-NP       DOI: 10.1677/joe.0.1280239
© 1991 Society for Endocrinology
This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Sundick, R. S.
Right arrow Articles by Bagchi, N.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Sundick, R. S.
Right arrow Articles by Bagchi, N.

Thyroidal iodine metabolism in obese-strain chickens before immune-mediated damage

R. S. Sundick, D. Herdegen, T. R. Brown, A. Dhar and N. Bagchi

Several studies have shown that iodine plays a role in spontaneous autoimmune thyroiditis in man and other animals. In addition, abnormalities of iodine metabolism have been found in patients with Hashimoto's thyroiditis and in chickens of the obese strain (OS), an animal model of spontaneous autoimmune thyroiditis. We have examined several parameters of iodine metabolism before immune damage in this model and in the related Cornell strain (CS), a strain which develops a late-onset mild thyroiditis, to discover a possible causal relationship between altered iodine metabolism and the initiation of autoimmunity.

Thyroglobulin was purified from individual chicken thyroid glands and analysed for iodine by the ceric sulphate method. Analogous to the thyroglobulin of Hashimoto's patients, the iodine content of OS thyroglobulin (27 atoms/molecule) was lower than that of normal-strain thyroglobulin (46 atoms/molecule) when the chickens were provided with a normal diet. Also, under conditions of TSH suppression, the iodine content of OS thyroglobulin (18 atoms/molecule) was lower than that of CS thyroglobulin (36 atoms/molecule) and of normal-strain thyroglobulin (32 atoms/molecule). In contrast with Hashimoto's patients, however, the OS and CS chickens had practically no inorganic iodide in their thyroid glands; electrophoretic analysis of thyroid homogenates revealed that essentially all (> 99·62%) 125I was organified by 16 h in all strains of birds tested. Despite the relatively poor iodination of thyroglobulin exhibited by OS chickens, they did not iodinate additional 'unique' proteins, when examined by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) of thyroid proteins labelled with 125I in vivo.

The release of 125I in vivo under conditions of TSH suppression was examined in chicks receiving thyroxine and propylthiouracil. After 14 days both OS and CS chicks showed poorly suppressible release of 85% and 92% respectively, while the normal strain released 33 %. To determine whether the autonomous function of OS and CS thyroid glands was present in a restricted number of follicles or cells or whether it occurred in a majority of cells, autoradiograms of thyroid glands labelled in vivo from TSH-suppressed chickens were examined. Silver grains were present in all cells, indicating that autonomous function was a characteristic of all cells.

These thyroid gland abnormalities are compared with those found in Hashimoto's patients and discussed in the context of their aetiological significance.

Journal of Endocrinology (1991) 128, 239–244







HOME HELP CONTACT US SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1991 by the Society for Endocrinology.