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pubmed-article:11716040pubmed:abstractTextThe iodide-concentrating ability of the thyroid gland is essential to the production of thyroid hormone. We report the nucleotide and amino acid sequence of the mouse sodium iodide symporter (mNIS), which mediates this activity within the thyroid gland. An open reading frame of 1,857 nucleotides codes for a protein of 618 amino acids with 95% identity to rat NIS and 84% identity to human NIS. Transient expression of the mNIS cDNA in Chinese hamster ovary (CHO) cells, a nonthyroid cell line, resulted in sodium-dependent, perchlorate-sensitive iodide uptake. Western blot analysis of membrane preparations of CHO cells transiently transfected with mNIS cDNA showed a band of 90 kd when probed with an antibody directed against rat NIS. mNIS will serve as an important reagent in determining the role of NIS in experimental thyroid diseases and for monitoring the immune response to in animal models of NIS-mediated gene therapy.lld:pubmed
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pubmed-article:11716040pubmed:year2001lld:pubmed
pubmed-article:11716040pubmed:articleTitleCloning of the mouse sodium iodide symporter.lld:pubmed
pubmed-article:11716040pubmed:affiliationDepartment of Urology, Mayo Clinic, Rochester, Minnesota 55905, USA.lld:pubmed
pubmed-article:11716040pubmed:publicationTypeJournal Articlelld:pubmed
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