This Article Full Text Full Text (PDF) Submit a related Letter to the Editor Purchase Article View Shopping Cart Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Copyright Permission Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Porra, V. Articles by Rousset, B. Search for Related Content PubMed PubMed Citation Articles by Porra, V. Articles by Rousset, B.

Characterization and Semiquantitative Analyses of Pendrin Expressed in Normal and Tumoral Human Thyroid Tissues

INSERM, U-369, Faculté de Médecine Lyon RTH-Laennec (V.P., F.B.-V., S.T.-M., S.S.-R., B.R.); Unité Fonctionnelle de Biologie Cellulaire, Hôpital Edouard-Herriot (V.P., B.R.); and Lyon Thyroid Tumor Bank Organization (N.B.-D., J.-L.P., A.P.), 69372 Lyon, France

Address all correspondence and requests for reprints to: Prof. Bernard Rousset, INSERM, U-369, Faculté de Médecine Lyon-RTH Laennec, 7 rue Guillaume Paradin, 69372 Lyon Cedex 08, France. E-mail: .

Abstract

The gene mutated in Pendred syndrome (PDS), the PDS gene, is expressed in the inner ear, kidney, and thyroid. It encodes a membrane protein named pendrin that is endowed with the function of anion transporter or exchanger. It has been postulated that in the thyroid pendrin could participate in the transport of iodide from the cell to the lumen of follicles. We generated antipeptide antibodies directed against the C- terminal sequence of human pendrin 1) to characterize the protein expressed in the human thyroid, and 2) to analyze its expression level in relation to the functional activity of thyroid tissue. In denaturing conditions, a single molecular species of 110–115 kDa was identified in human thyroid membrane fractions. After treatment of thyroid membranes with N-glycosidase F, pendrin had an apparent molecular mass of 85 kDa. Analyzed by ultracentrifugation on sucrose gradient in nondenaturing conditions, pendrin sedimented as a main 120- to 140-kDa component. Pendrin was assayed by semiquantitative Western blot in thyroid membrane fractions from 25 hyper- or hypofunctioning tumors and paired normal tissue samples. Pendrin was increased 2-fold in toxic adenomas, was not significantly altered in follicular adenoma, and was decreased, on the average, by 35% in papillary carcinomas compared with levels in paired normal tissue. The variations in the pendrin tissue content and PDS transcript levels, assayed by RT-PCR on duplicate samples of the same tumors, were similar. In conclusion, we show that pendrin expressed by the human thyroid gland is a mainly monomeric glycoprotein and that the level of expression of pendrin, although somewhat related, only moderately varied with the functional status of the thyroid tissue.

This article has been cited by other articles:

				P. Dallos, J. Zheng, and M. A. Cheatham Prestin and the cochlear amplifier J. Physiol., October 1, 2006; 576(1): 37 - 42. [Abstract] [Full Text] [PDF]

				V. Porra, C. Ferraro-Peyret, C. Durand, S. Selmi-Ruby, H. Giroud, N. Berger-Dutrieux, M. Decaussin, J.-L. Peix, C. Bournaud, J. Orgiazzi, et al. Silencing of the Tumor Suppressor Gene SLC5A8 Is Associated with BRAF Mutations in Classical Papillary Thyroid Carcinomas J. Clin. Endocrinol. Metab., May 1, 2005; 90(5): 3028 - 3035. [Abstract] [Full Text] [PDF]

				G. De Vita, L. Bauer, V. M. C. da Costa, M. De Felice, M. G. Baratta, M. De Menna, and R. Di Lauro Dose-Dependent Inhibition of Thyroid Differentiation by RAS Oncogenes Mol. Endocrinol., January 1, 2005; 19(1): 76 - 89. [Abstract] [Full Text] [PDF]

				S. Trouttet-Masson, S. Selmi-Ruby, F. Bernier-Valentin, V. Porra, N. Berger-Dutrieux, M. Decaussin, J.-L. Peix, A. Perrin, C. Bournaud, J. Orgiazzi, et al. Evidence for Transcriptional and Posttranscriptional Alterations of the Sodium/Iodide Symporter Expression in Hypofunctioning Benign and Malignant Thyroid Tumors Am. J. Pathol., July 1, 2004; 165(1): 25 - 34. [Abstract] [Full Text] [PDF]

				L. Lacroix, T. Pourcher, C. Magnon, N. Bellon, M. Talbot, T. Intaraphairot, B. Caillou, M. Schlumberger, and J.-M. Bidart Expression of the Apical Iodide Transporter in Human Thyroid Tissues: A Comparison Study with Other Iodide Transporters J. Clin. Endocrinol. Metab., March 1, 2004; 89(3): 1423 - 1428. [Abstract] [Full Text] [PDF]

				M. Xing, Y. Tokumaru, G. Wu, W. B. Westra, P. W. Ladenson, and D. Sidransky Hypermethylation of the Pendred Syndrome Gene SLC26A4 Is an Early Event in Thyroid Tumorigenesis Cancer Res., May 1, 2003; 63(9): 2312 - 2315. [Abstract] [Full Text] [PDF]

				P. M. Piermarini, J. W. Verlander, I. E. Royaux, and D. H. Evans Pendrin immunoreactivity in the gill epithelium of a euryhaline elasmobranch Am J Physiol Regulatory Integrative Comp Physiol, October 1, 2002; 283(4): R983 - R992. [Abstract] [Full Text] [PDF]