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Am J Physiol Gastrointest Liver Physiol 288: G933-G942, 2005. First published December 9, 2004; doi:10.1152/ajpgi.00198.2004
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MUCOSAL BIOLOGY

Dual oxidase2 is expressed all along the digestive tract

Rabii Ameziane El Hassani,1,* Nesrine Benfares,1,* Bernard Caillou,2 Monique Talbot,2 Jean-Christophe Sabourin,2 Virginie Belotte,2 Stanislas Morand,1 Sédami Gnidehou,1 Diane Agnandji,1 Renée Ohayon,1 Jacques Kaniewski,1 Marie-Sophie Noël-Hudson,1 Jean-Michel Bidart,2 Martin Schlumberger,2 Alain Virion,1 and Corinne Dupuy1

1Unité 486 INSERM, Université Paris 11, Faculté de Pharmacie, ChÂtenay-Malabry Cedex and 2UMR 8125 CNRS/CEA LRC 29V, Institut Gustave-Roussy, Villejuif, France

Submitted 29 April 2004 ; accepted in final form 23 November 2004

The dual oxidase (Duox)2 flavoprotein is strongly expressed in the thyroid gland, where it plays a critical role in the synthesis of thyroid hormones by providing thyroperoxidase with H2O2. DUOX2 mRNA was recently detected by RT-PCR and in-situ hybridization experiments in other tissues, such as rat colon and rat and human epithelial cells from the salivary excretory ducts and rectal glands. We examined Duox2 expression at the protein level throughout the porcine digestive tract and in human colon. Western blot analysis identified Duox2 as the same two molecular species (Mr 165 and 175 kDa) as detected in the thyroid. It was expressed in all the tissues tested, but the highest levels were found in the cecum and sigmoidal colon. Immunohistochemical studies showed that Duox2 protein is mainly present in these parts of the gut and located at the apical membrane of the enterocytes in the brush border, indicating that it is expressed only in highly differentiated cells. A Ca2+/NADPH-dependent H2O2-generating system was associated with Duox2 protein expression, which had the same biochemical characteristics as the NADPH oxidase in the thyroid. Indeed, treatment of the thyroid and cecum particulate fractions with phenylarsine oxide resulted in complete calcium desensitization of both enzymes. A marked increase in DUOX2 expression was also found during spontaneous differentiation of postconfluent Caco-2 cells. The discovery of Duox2 as a novel source of H2O2 in the digestive tract, particularly in the cecum and colon, makes it a new candidate mediator of physiopathological processes.

thyroid gland; gastrointestinal system; dual oxidase gene; thyroid oxidase gene; NADPH oxidase; hydrogen peroxide


Address for reprint requests and other correspondence: C. Dupuy, INSERM Unité 486, Faculté de Pharmacie, 92296 ChÂtenay-Malabry Cedex, France (E-mail: corinne.dupuy{at}cep.u-psud.fr)




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