Pendred syndrome in two Galician families: insights into clinical phenotypes through cellular, genetic, and molecular studies

J Clin Endocrinol Metab. 2008 Jan;93(1):267-77. doi: 10.1210/jc.2007-0539. Epub 2007 Oct 16.

Abstract

Context: We studied two families from Galicia (northwest Spain) with Pendred syndrome (PS) and unusual thyroid phenotypes. In family A, the proposita had a large goiter and hypothyroxinemia but normal TSH and free T3 (FT3). In family B, some affected members showed deafness but not goiter.

Objective: Our objective was to identify the mutations causing PS and molecular mechanisms underlying the thyroid phenotypes.

Interventions: Interventions included extraction of DNA and of thyroid tissue.

Patients: Propositi and 10 members of the two families participated in the study.

Main outcome measures: Main outcome measures included SLC26A4 gene analysis, deiodinase activities in thyroid tissue, and c.416-1G-->A effects on SLC26A4 splicing. In addition, a primary PS thyrocyte culture, T-PS2, was obtained from propositus B and compared with another culture of normal human thyrocytes, NT, by Western blotting, confocal microscopy, and iodine uptake kinetics.

Results: Proposita A was heterozygous for c.578C-->T and c.279delT, presented with goiter, and had normal TSH and FT3 but low FT4 attributable to high type 1 and type 2 iodothyronine deiodinase activities in the goiter. Propositus B bore c.279delT and a novel mutation c.416-1G-->A; some deaf relatives were homozygous for c.416-1G-->A but did not present goiter. The c.279delT mutation was associated with identical haplotype in the two families. T-PS2 showed truncated pendrin retained intracellularly and high iodine uptake with low efflux leading to iodine retention.

Conclusions: c.279delT is a founder mutation in Galicia. Proposita A adapted to poor organification by increasing deiodinase activities in the goiter, avoiding hypothyroidism. Lack of goiter in subjects homozygous for c.416-1G-->A was due to incomplete penetrance allowing synthesis of some wild-type pendrin. Intracellular iodine retention, as seen in T-PS2, could play a role in thyroid alterations in PS.

Publication types

  • Case Reports
  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adult
  • Amino Acid Sequence
  • Female
  • Goiter, Nodular / enzymology
  • Goiter, Nodular / genetics*
  • Goiter, Nodular / pathology
  • Haplotypes
  • Hearing Loss, Sensorineural / enzymology
  • Hearing Loss, Sensorineural / genetics*
  • Hearing Loss, Sensorineural / pathology
  • Humans
  • Immunohistochemistry
  • Iodide Peroxidase / biosynthesis
  • Iodide Peroxidase / genetics
  • Iodine / pharmacokinetics
  • Iodothyronine Deiodinase Type II
  • Male
  • Membrane Transport Proteins / biosynthesis
  • Membrane Transport Proteins / genetics
  • Middle Aged
  • Molecular Sequence Data
  • Monocarboxylic Acid Transporters / biosynthesis
  • Monocarboxylic Acid Transporters / genetics
  • Pedigree
  • RNA, Messenger / biosynthesis
  • RNA, Messenger / genetics
  • Reverse Transcriptase Polymerase Chain Reaction
  • Spain
  • Sulfate Transporters
  • Symporters
  • Syndrome
  • Thyroid Function Tests

Substances

  • Membrane Transport Proteins
  • Monocarboxylic Acid Transporters
  • RNA, Messenger
  • SLC16A2 protein, human
  • SLC26A4 protein, human
  • Sulfate Transporters
  • Symporters
  • Iodine
  • iodothyronine deiodinase type I
  • Iodide Peroxidase