Topology of the thyroid sodium-iodine symporter
DOI:
https://doi.org/10.24220/2318-0897v19n1/6a829Keywords:
Thyroid gland, Iodine, SymportersAbstract
The synthesis of thyroid hormones depends essentially on the uptake of iodide by thyrocytes, which is mediated by an intrinsic membrane glycoprotein, the
sodium-iodide symporter. The NIS actively cotransports a sodium cation and an iodide anion simultaneously. NIS-mediated transport of iodide is driven by the
electrochemical sodium gradient generated by Na+/K+ ATP´ase. Sodium-Iodide Symporter also mediates active iodide transport in other tissues, including salivary
glands, gastric mucosa, and lactating mammary gland. The ability of the thyroid to accumulate iodide via NIS has long provided the basis for diagnostic scintigraphic imaging of the thyroid with radioiodine and served as an effective means for therapeutic doses of radioiodide to target and destroy hyperfunctioning thyroid tissue, as seen in Graves’ disease. Another relevant clinical aspect of Sodium-Iodide Symporter is the fact that some spontaneous mutations have been identified as the cause of congenital iodide transport defect, resulting in hypothyroidism. Furthermore, the sodium-iodide symporter can become the target of autoantibodies, resulting in autoimmune thyroid diseases. Finally, the molecular analysis of NIS clearly holds the potential of having an even greater impact on a wide spectrum of fields, ranging from the structure and function of transport proteins to the diagnosis and treatment of cancer, in thyroid and nonthyroid
tissues. The aim of this paper is to describe the sodium/iodide symporter present in the thyroid gland, highlighting its sequence of amino acid residues, topology, and all other relevant aspects of structure and function. This study is based on a systematic review of the domestic and international literature found in Medline/PubMed with the keywords: iodide, thyroid, carrier, topology, sequence of amino acid residues and structure.
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