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This Article Full Text Full Text (PDF) All Versions of this Article: JME-08-0175v1 43/3/93    most recent Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Google Scholar Articles by Dossena, S. Articles by Paulmichl, M. PubMed PubMed Citation Articles by Dossena, S. Articles by Paulmichl, M.

¹ Institut of Pharmacology and Toxicology, Paracelsus Medical University, A-5020 Salzburg, Austria
² CIMAINA,
³ Department of Biomolecular Sciences and Biotechnology
⁴ Department of Medical Sciences, Università degli Studi di Milano, I-20133 Milan, Italy
⁵ Endocrine and Diabetes Unit, Fondazione Policlinico, IRCCS, I-20122 Milan, Italy

(Correspondence should be addressed to M Paulmichl; Email: markus.paulmichl{at}pmu.ac.at)

Pendred syndrome (PS) is the most frequent form of genetically related syndromic hearing loss, and is associated with mutations of pendrin, encoded by the SLC26A4 gene. This protein localizes to the cellular membrane and permits the exchange of anions between the cytosol and extracellular space. In the inner ear, pendrin conditions the endolymph, allowing for the proper function of sensory cells. Understanding the relationship between the genotype and phenotype of pendrin mutations would aid clinicians to better serve PS patients–however, little is known. Here, we summarize the available data concerning SLC26A4 mutations and how they relate to transporter function. The main findings suggest that all the truncation mutations tested annihilate pendrin function, and that the addition or omission of proline, or the addition or omission of charged amino acids in the sequence of SLC26A4 result in a substantial to dramatic reduction in pendrin function.