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Production of Immunoreactive Thyroglobulin C-Terminal Fragments during Thyroid Hormone Synthesis

Unit 38 of the French Institute of Health and Medical Research, Faculté de Médecine Timone, Université de la Méditerranée, Marseille, France

Address all correspondence and requests for reprints to: Dr. Jean Ruf, U38 INSERM, Faculté de Médecine Timone, 27 boulevard Jean Moulin, F-13385 Marseille Cedex 5, France. E-mail: jean.ruf{at}medecine.univ-mrs.fr

Here, we studied the fragmentation of the prothyroid hormone, thyroglobulin (Tg), which occurs during thyroid hormone synthesis, a process which involves iodide, thyroperoxidase, and the H₂O₂-generating system, consisting of glucose and glucose oxidase. Various peptides were found to be immunoreactive to autoantibodies to Tg from patients and monoclonal antibodies directed against the immunodominant region of Tg. The smallest peptide (40 kDa) bore thyroid hormones and was identified at the C-terminal end of the Tg molecule, which shows homologies with acetylcholinesterase. Similar peptides were obtained by performing metal-mediated oxidation of Tg via a Fenton reaction. It was concluded that the oxidative stress induced during hormone synthesis generates free radicals, which, in turn, cleave Tg into immunoreactive peptides.

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