377
Review
Cell Physiol Biochem 2011;28:377-384
Accepted: October 10, 2011
Cellular Physiology Cellular Physiology Cellular Physiology Cellular Physiology Cellular Physiology
and Biochemistr and Biochemistr and Biochemistr and Biochemistr and Biochemistry
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Abstract
Human pendrin (SCL26A4, PDS) is a 780 amino
acid integral membrane protein with transport
function. It acts as an electroneutral, sodium-
independent anion exchanger for a wide range of
anions, such as iodide, chloride, formate,
bicarbonate, hydroxide and thiocyanate. Pendrin
expression was originally described in the thyroid
gland, kidney and inner ear. Accordingly, pendrin
mutations with reduction or loss of transport function
result in thyroid and inner ear abnormalities,
manifested as syndromic (Pendred syndrome) and
non- s yndromic hearing loss with an e nlarged
vestibular aqueduct (ns-EVA). Pendred syndrome,
the most common form of syndromic deafness, is an
autosomal recessive disease characterized by
sensorineural deafness due to inner ear
malformations and a partial iodide organification
defect that may lead to thyroid goiter. Later, it
became evident that not only pendrin loss of function,
but also up-regulation could participate in the
pathogenesis of human diseases. Indeed, despite the
absence of kidney dysfunction in Pendred syndrome
patients, evidence exists that pendrin also plays a
crucial role in this organ, with a potential involvement
in the pathogenesis of hypertension. In addition,
recent data underscore the role of pendrin in
exacerbations of respiratory distresses including
bronchial asthma and chronic obstructive pulmonary
disease (COPD). Pendrin expression in other organs
such as mammary gland, testis, placenta,
endometrium and liver point to new, underscored
pendrin functions that deserve to be further
investigated.
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Key Words
Pendrin Inherited hearing loss Functional test
Ion transport Pendred syndrome EVA SLC26A4
Markus Paulmichl MD,
Institute of Pharmacology and Toxicology, Paracelsus Medical University,
Strubergasse 21, Salzburg, A-5020 (Austria)
Tel. +43-662-442002-1230, Fax +43-662-442002-1239;
E-Mail markus.paulmichl@pmu.ac.at
The ESF Meeting on „The Proteomics,
Epigenetics and Pharmacogenetics of Pendrin“
Silvia Dossena
1
*, Charity Nofziger
1
*, Florian Lang
2
, Giovanna Valenti
3
and Markus Paulmichl
1
1
Institute of Pharmacology and Toxicology, Paracelsus Medical University, Salzburg,
2
Department of
Physiology, University of Tübingen, Tübingen,
3
Department of General and Environmental Physiology,
University of Bari, Bari, *SD and CN contributed equally to the present work