help button home button Endocrine Society Endocrinology
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
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
Right arrow Request Copyright Permission
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Morand, S.
Right arrow Articles by Dupuy, C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Morand, S.
Right arrow Articles by Dupuy, C.
Endocrinology Vol. 144, No. 2 567-574
Copyright © 2003 by The Endocrine Society


ARTICLE

Identification of a Truncated Dual Oxidase 2 (DUOX2) Messenger Ribonucleic Acid (mRNA) in Two Rat Thyroid Cell Lines. Insulin and Forskolin Regulation of DUOX2 mRNA Levels in FRTL-5 Cells and Porcine Thyrocytes

Stanislas Morand1, Orquidea Filipe Dos Santos1, Renée Ohayon, Jacques Kaniewski, Marie-Sophie Noel-Hudson, Alain Virion and Corinne Dupuy

Unité 486, Institut National de la Santé et de la Recherche Médicale, Université Paris 11, Faculté de Pharmacie, 92296 Châtenay-Malabry Cedex, France

Address all correspondence and requests for reprints to: C. Dupuy, Unité 486, Institut National de la Santé et de la Recherche Médicale, Faculté de Pharmacie, 92296 Châtenay-Malabry Cedex, France. E-mail: corinne.dupuy{at}cep.u-psud.fr.

The Duox2 flavoprotein is strongly expressed in the thyroid gland, where it plays a critical role in the synthesis of thyroid hormones likely by providing thyroperoxidase with H2O2. A truncated DUOX2 mRNA was isolated from the rat thyroid cell line FRTL-5. The cDNA sequence predicted an open reading frame of 1458 bp, encoding a polypeptide of 486 amino acids corresponding to the carboxyl fragment of the Duox2 flavoprotein. The truncated form of DUOX2 mRNA, expressed in another rat thyroid cell line, the PC Cl3 cell line, was absent from Fischer rat thyroid glands. Although it was expressed in both cell lines to a greater extent than normal mRNA, it failed to support protein synthesis in an in vitro translation system. Insulin increased the levels of both normal and truncated DUOX2 mRNA in FRTL-5 cells grown in TSH-free medium containing a low concentration of serum. The stimulating effect of insulin on DUOX2 mRNA expression was reproduced in pig thyroid follicles in primary culture. The presence of insulin in the culture medium converted forskolin from a stimulator to an inhibitor in FRTL-5 cells maintained in low serum conditions, but not in porcine thyrocytes in primary culture.




This article has been cited by other articles:


Home page
Physiol. Rev.Home page
K. Bedard and K.-H. Krause
The NOX Family of ROS-Generating NADPH Oxidases: Physiology and Pathophysiology
Physiol Rev, January 1, 2007; 87(1): 245 - 313.
[Abstract] [Full Text] [PDF]


Home page
Clin. Chem.Home page
V. Varela, C. M. Rivolta, S. A. Esperante, L. Gruneiro-Papendieck, A. Chiesa, and H. M. Targovnik
Three Mutations (p.Q36H, p.G418fsX482, and g.IVS19-2A>C) in the Dual Oxidase 2 Gene Responsible for Congenital Goiter and Iodide Organification Defect
Clin. Chem., February 1, 2006; 52(2): 182 - 191.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Endocrinology Endocrine Reviews J. Clin. End. & Metab.
Molecular Endocrinology Recent Prog. Horm. Res. All Endocrine Journals
Copyright © 2003 by The Endocrine Society