TSH regulates pendrin membrane abundance and enhances iodide efflux in thyroid cells

Liuska Pesce, Aigerim Bizhanova, Juan Carlos Caraballo, Whitney Westphal, Maria L. Butti, Alejandro Comellas, Peter Kopp*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

34 Scopus citations

Abstract

Thyroid hormones are essential for normal development and metabolism. Their synthesis requires transport of iodide into thyroid follicles. The mechanisms involving the apical efflux of iodide into the follicular lumen are poorly elucidated. The discovery of mutations in the SLC26A4 gene in patients with Pendred syndrome (congenital deafness, goiter, and defective iodide organification) suggested a possible role for the encoded protein, pendrin, as an apical iodide transporter. We determined whether TSH regulates pendrin abundance at the plasma membrane and whether this influences iodide efflux. Results of immunoblot and immunofluorescence experiments reveal that TSH and forskolin rapidly increase pendrin abundance at the plasma membrane through the protein kinaseApathway in PCCL-3 rat thyroid cells. The increase in pendrinmembraneabundance correlates with a decrease in intracellular iodide as determined by measuring intracellular 125iodide and can be inhibited by specific blocking of pendrin. Elimination of the putative protein kinase A phosphorylation site T717A results in a diminished translocation to the membrane in response to forskolin. These results demonstrate that pendrin translocates to the membrane in response to TSH and suggest that it may have a physiological role in apical iodide transport and thyroid hormone synthesis.

Original languageEnglish (US)
Pages (from-to)512-521
Number of pages10
JournalEndocrinology
Volume153
Issue number1
DOIs
StatePublished - Jan 2012

ASJC Scopus subject areas

  • Endocrinology

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