Expression of Reduced Nicotinamide Adenine Dinucleotide Phosphate Oxidase (ThoX, LNOX, Duox) Genes and Proteins in Human Thyroid Tissues1 (original) (raw)
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1Departments of Pathology (B.C., M.N., M.T.), 94805 Villejuif
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4INSERM Unité 486 (C.D., R.O., D.D., A.V.), Faculté de Pharmacie, 92296 Châtenay-Malabry Cedex, France
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2Clinical Biology (L.L., J.M.B.), 94805 Villejuif
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1Departments of Pathology (B.C., M.N., M.T.), 94805 Villejuif
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1Departments of Pathology (B.C., M.N., M.T.), 94805 Villejuif
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4INSERM Unité 486 (C.D., R.O., D.D., A.V.), Faculté de Pharmacie, 92296 Châtenay-Malabry Cedex, France
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4INSERM Unité 486 (C.D., R.O., D.D., A.V.), Faculté de Pharmacie, 92296 Châtenay-Malabry Cedex, France
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2Clinical Biology (L.L., J.M.B.), 94805 Villejuif
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3Nuclear Medicine (M.S.), Institut Gustave-Roussy, 94805 Villejuif
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4INSERM Unité 486 (C.D., R.O., D.D., A.V.), Faculté de Pharmacie, 92296 Châtenay-Malabry Cedex, France
*Address all correspondence and requests for reprints to: A. Virion, M.D., INSERM Unité 486, Faculté de Pharmacie, 92296 Châtenay-Malabry Cedex, France.
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Revision received:
06 December 2000
Revision received:
08 March 2001
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Bernard Caillou, Corinne Dupuy, Ludovic Lacroix, Maria Nocera, Monique Talbot, Renée Ohayon, Danielle Dème, Jean-Michel Bidart, Martin Schlumberger, Alain Virion., Expression of Reduced Nicotinamide Adenine Dinucleotide Phosphate Oxidase (ThoX, LNOX, Duox) Genes and Proteins in Human Thyroid Tissues, The Journal of Clinical Endocrinology & Metabolism, Volume 86, Issue 7, 1 July 2001, Pages 3351–3358, https://doi.org/10.1210/jcem.86.7.7646
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The large homolog of NADPH oxidase flavoprotein LNOX2, and probably LNOX1, are flavoproteins involved in the thyroid H2O2 generator. Western blot analysis of membrane proteins from normal human thyroid, using antipeptide antibodies, indicated that LNOX1,2 are 164-kDa glycoproteins and that N-glycosylated motifs account for at least 10–20 kDa of their total apparent molecular mass. Northern blot analysis of 23 different human tissues demonstrated that LNOX2 messenger RNA (mRNA) is strongly expressed only in the thyroid gland, although blast analysis of expressed sequence tags databases indicated that LNOX genes are also expressed in some nonthyroid cells.
We investigated LNOX1_,_2 gene and protein expressions in normal and pathological human thyroid tissues using real-time kinetic quantitative PCR and antipeptide antibodies, respectively. In normal tissue, LNOX1,2 are localized at the apical pole of thyrocytes. Immunostaining for LNOX1,2 was heterogeneous, inside a given follicle, with 40–60% of positive follicular cells. Among normal and pathological tissues, variations of LNOX1 and LNOX2 mRNA levels were parallel, suggesting a similar regulation of both gene expressions. Whereas LNOX mRNAs seemed slightly affected in benign disease, the expression of protein was highly variable. In multinodular goiters, 40–60% of cells were stained. In hypofunctioning adenomas, LNOX immunostaining was highly variable among follicles, whereas sodium/iodide (Na+/I-) symporter immunostaining was decreased. In hyperfunctioning thyroid tissues, only few cells (0–10%) were weakly stained, whereas sodium/iodide symporter staining was found in the majority of follicular cells.
In conclusion, LNOX proteins are new apical glycoproteins with a regulation of expression that differs from other thyroid markers.
Copyright © 2001 by The Endocrine Society
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