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Accepted Preprint first posted online on 24 September 2009
Endocrine-Related Cancer (2009) In press
DOI: 10.1677/ERC-09-0175
Copyright © 2009 by the Society for Endocrinology.
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RESEARCH

Intracellular expression of ROS-generating NADPH oxidase NOX4 in normal and cancer thyroid tissues

 Urbain Weyemi, Bernard Caillou, Monique Talbot, Rabii Ameziane-El-Hassani, Ludovic Lacroix, Odile Lagent-Chevallier, Abir Al Ghuzlan, Dirk Roos, Jean-Michel Bidart, Alain Virion, Martin Schlumberger and Corinne Dupuy

U Weyemi, FRE 2939, CNRS, Villejuif, France
B Caillou, Institut Gustave Roussy, Villejuif, France
M Talbot, FRE 2939, CNRS, Villejuif, France
R Ameziane-El-Hassani, UBRM, Centre Nationale de l'Energie, des Sciences et des Techniques Nucleaires, Rabat, Morocco
L Lacroix, Institut Gustave Roussy, Villejuif, France
O Lagent-Chevallier, FRE 2939, CNRS, Villejuif, France
A Al Ghuzlan, Institut Gustave Roussy, Villejuif, France
D Roos, Academic Medical Centre, Sanquin Research Institute, Amsterdam, Netherlands
J Bidart, University Paris-Sud 11, Orsay, France
A Virion, FRE 2939, CNRS, Villejuif, France
M Schlumberger, University Paris-Sud 11, Orsay, France
C Dupuy, FRE 2939, CNRS, Villejuif, France

Corinne Dupuy, Email: dupuy{at}igr.fr

Abstract

NOX4 belongs to the NADPH oxidase family that generates reactive oxygen species (ROS). Function and tissue distribution of NOX4 have not yet been entirely clarified. To date, in the thyroid gland, only DUOX1/2 NADPH oxidase systems have been described. NOX4 mRNA expression, as shown by real-time PCR, was present in normal thyroid tissue, regulated by TSH and significantly increased in differentiated cancer tissues. TSH increased the protein level of NOX4 in human thyroid primary culture and NOX4-dependent ROS generation. NOX4 immunostaining was detected in normal and pathologic thyroid tissues. In normal thyroid tissue, staining was heterogeneous and mostly found in activated columnar thyrocytes but absent in quiescent flat cells. Papillary and follicular thyroid carcinomas displayed more homogeneous staining. The p22phox protein that forms a heterodimeric enzyme complex with NOX4 displayed an identical cellular expression pattern and was also positively regulated by TSH. ROS may have various biological effects, depending on the site of production. Intracellular NOX4-p22phox localization suggests a role in cytoplasmic redox signalling, in contrast to the DUOX localization at the apical membrane that corresponds to an extracellular H2O2 production.Increased NOX4-p22phox in cancer might be related to a higher proliferation rate and tumor progression but a role in the development of tumors has to be further studied and established in the future.






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