This Article Full Text (PDF) Submit a related Letter to the Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Copyright Permission Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by KIM, P. S. Articles by DUNN, J. T. Search for Related Content PubMed PubMed Citation Articles by KIM, P. S. Articles by DUNN, J. T.

Altered Immunoreactivity of Thyroglobulin in Thyroid Disease^*

Division of Endocrinology, Department of Medicine, University of Virginia School of Medicine Charbttesville, Virginia 22908

Address requests for reprints to: Dr. John T. Dunn, Box 511, University of Virginia Medical Center, Charlottesville, Virginia 22908.

We prepared 3 samples of 19S thyroglobulin (Tg), 1 from a patient with Graves’ disease, another from a patient with nontoxic goiter, and the third from a pool of Tg from normal subjects, and used each Tg preparation to produce a polyvalent antiserum in rabbits. The 3 antisera were similar to each other in their reactivity with thyroid Tg samples from 25 patients with various thyroid disorders and from 10 normal subjects. However, the immunoreactivity of the 35 individual Tg samples varied considerably. Decreased reactivity was associated with proteolysis during Tg preparation, iodination in vitro with 20 or more atoms of iodine/molecule Tg, the 27S species of Tg, Tg from 3 patients with thyroid cancer, and Tg from several patients with Graves’ disease. The antiserum to Graves’ Tg contained some antibodies that did not bind normal Tg on an affinity column, and these antibodies reacted more with Tg from patients with Graves’ disease than with Tg from normal subjects or patients with nontoxic goiters. Thus, Tg from patients with Graves’ disease may contain antigenic sites that are not present or exposed in Tgs from other subjects.

We conclude that thyroid Tgs from patients with Graves’ disease and from those with thyroid cancer may be different in structure from the Tgs of normal subjects. This conclusion is important to an understanding of Tg structure in thyroid disease and to the use of thyroid Tg for preparation of antisera and standards for measuring serum Tg concentrations

^* This work was supported in part by NIH Grant AM-11043.

Received September 8, 1987.

This article has been cited by other articles:

				F. Latrofa, D. Ricci, L. Grasso, P. Vitti, L. Masserini, F. Basolo, C. Ugolini, G. Mascia, A. Lucacchini, and A. Pinchera Characterization of Thyroglobulin Epitopes in Patients with Autoimmune and Non-Autoimmune Thyroid Diseases Using Recombinant Human Monoclonal Thyroglobulin Autoantibodies J. Clin. Endocrinol. Metab., February 1, 2008; 93(2): 591 - 596. [Abstract] [Full Text] [PDF]

				A. M. Saboori, N. R. Rose, S. C. Yuhasz, L. M. Amzel, and C. L. Burek Peptides of Human Thyroglobulin Reactive with Sera of Patients with Autoimmune Thyroid Disease J. Immunol., December 1, 1999; 163(11): 6244 - 6250. [Abstract] [Full Text] [PDF]