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Originally published In Press as doi:10.1074/jbc.M101086200 on April 9, 2001

J. Biol. Chem., Vol. 276, Issue 24, 21337-21342, June 15, 2001
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Role of Extracellular Molecular Chaperones in the Folding of Oxidized Proteins
REFOLDING OF COLLOIDAL THYROGLOBULIN BY PROTEIN DISULFIDE ISOMERASE AND IMMUNOGLOBULIN HEAVY CHAIN-BINDING PROTEIN *

Frédéric Delom, Bernard MalletDagger , Pierre Carayon, and Pierre-Jean Lejeune

From the Unité 555 INSERM and Laboratoire de Biochimie Endocrinienne et Métabolique, Faculté de Médecine, Université de la Méditerranée, 13385 Marseille Cedex 5, France

The process of thyroid hormone synthesis, which occurs in the lumen of the thyroid follicles, results from an oxidative reaction leading, as side effects, to the multimerization of thyroglobulin (TG), the prothyroid hormone. Although hormone synthesis is a continuous process, the amount of Tg multimers is relatively constant. Here, we investigated the role of two molecular chaperones, protein disulfide isomerase (PDI) and immunoglobulin heavy chain-binding protein (BiP), present in the follicular lumen, on the multimerization process due to oxidation using both native Tg and its N-terminal domain (NTD). In vitro, PDI decreased multimerization of Tg and even suppressed the formation of NTD multimers. Under the same conditions, BiP was able to bind to Tg and NTD multimers but did not affect the process of multimerization. Associating BiP with PDI did not enhance the ability of PDI to limit the formation of multimers produced by oxidation. However, when BiP and PDI were reacted together with the multimeric forms and for a longer time (48 h), BiP greatly increased the efficiency of PDI. Accordingly, these two molecular chaperones probably act sequentially on the reduction of the intermolecular disulfide bridges. In the thyroid, a similar process may also be effective and participate in limiting the amount of Tg multimers present in the colloid. These results suggest that extracellular molecular chaperones play a similar role to that occurring in the endoplasmic reticulum and, furthermore, take part in the control of multimerization and aggregation of proteins formed by oxidation.

* This work was supported in part by the Association pour le Développement des Recherches Biologiques et Médicales.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence and reprint requests should be addressed. Tel.: 33 4.91.32.43.92; Fax: 33 4.91.79.77.74; E-mail: bernard. mallet@medecine.univ-mrs.fr.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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