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Endocrinology Vol. 141, No. 2 839-845
Copyright © 2000 by The Endocrine Society

ARTICLES

Pendrin, the Protein Encoded by the Pendred Syndrome Gene (PDS), Is an Apical Porter of Iodide in the Thyroid and Is Regulated by Thyroglobulin in FRTL-5 Cells

Ines E. Royaux1, Koichi Suzuki1, Atsumi Mori, Ryohei Katoh, Lorraine A. Everett, Leonard D. Kohn and Eric D. Green

Genome Technology Branch, National Human Genome Research Institute (I.E.R., L.A.E., E.D.G.), and the Metabolic Diseases Branch, National Institute of Diabetes and Digestive and Kidney Diseases (K.S., A.M., L.D.K.), National Institutes of Health, Bethesda, Maryland 20892; and the Department of Pathology, Yamanashi Medical University School of Medicine (R.K.), Tamaho, Japan 409-38

Address all correspondence and requests for reprints to: Dr. Eric Green, Genome Technology Branch, National Human Genome Research Institute, National Institutes of Health, 49 Convent Drive, Building 49, Room 2A08, Bethesda, Maryland 20892. E-mail: egreen{at}nhgri.nih.gov

Pendred syndrome is an autosomal recessive disorder characterized by congenital deafness and thyroid goiter. The thyroid disease typically develops around puberty and is associated with a mild organification defect, characterized by an inappropriate discharge of iodide upon perchlorate stimulation (a positive perchlorate discharge test). The gene (PDS) mutated in Pendred syndrome is expressed in thyroid and encodes a 780-amino acid protein (pendrin) that has recently been shown to function as an iodide/chloride transporter. We sought to establish the location of pendrin in the thyroid and to examine the regulatory network controlling its synthesis. Using peptide-specific antibodies for immunolocalization studies, pendrin was detected in a limited subset of cells within the thyroid follicles, exclusively at the apical membrane of the follicular epithelium. Interestingly, significantly greater amounts of pendrin were encountered in thyroid tissue from patients with Graves’ disease. Using a cultured rat thyroid cell line (FRTL-5), PDS expression was found to be significantly induced by low concentrations of thyroglobulin (TG),but not by TSH, sodium iodide, or insulin. This is different fromthe established effect of TG, more typically a potent suppressor of thyroid-specific gene expression. Together, these results suggest that pendrin is an apical porter of iodide in the thyroid and that the expression and function of both the apical and basal iodide porters are coordinately regulated by follicular TG.




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 Hum Mol GenetHome page
L. A. Everett, I. A. Belyantseva, K. Noben-Trauth, R. Cantos, A. Chen, S. I. Thakkar, S. L. Hoogstraten-Miller, B. Kachar, D. K. Wu, and E. D. Green
Targeted disruption of mouse Pds provides insight about the inner-ear defects encountered in Pendred syndrome
Hum. Mol. Genet., January 1, 2001; 10(2): 153 - 161.
[Abstract] [Full Text] [PDF]

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 Hum Mol GenetHome page
D. A. Scott, R. Wang, T. M. Kreman, M. Andrews, J. M. McDonald, J. R. Bishop, R. J.H. Smith, L. P. Karniski, and V. C. Sheffield
Functional differences of the PDS gene product are associated with phenotypic variation in patients with Pendred syndrome and non-syndromic hearing loss (DFNB4)
Hum. Mol. Genet., July 1, 2000; 9(11): 1709 - 1715.
[Abstract] [Full Text] [PDF]

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 J. Clin. Endocrinol. Metab.Home page
L. Fugazzola, D. Mannavola, N. Cerutti, M. Maghnie, F. Pagella, P. Bianchi, G. Weber, L. Persani, and P. Beck-Peccoz
Molecular Analysis of the Pendred's Syndrome Gene and Magnetic Resonance Imaging Studies of the Inner Ear Are Essential for the Diagnosis of True Pendred's Syndrome