Cloning of the mouse sodium iodide symporter and its expression in the mammary gland and other tissues

Perron, Barbara; Rodriguez, Anne‐Marie; Leblanc, Gérard; Pourcher, Thierry

doi:10.1677/joe.0.1700185

Cited by 80 publications

(66 citation statements)

References 38 publications

(58 reference statements)

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“…In this study, we used the mouse NIS identified by Perron et al (2001). Its sequence and known functional properties are similar to those of its rat counterpart (data not shown).…”

Section: Discussionmentioning

confidence: 99%

“…Mutagenesis, plasmids, and cDNA construction of His-tagged and chimeric NIS The mouse NIS (mNIS) coding region was subcloned into pcDNA3.1 (Invitrogen) as described previously (Perron et al 2001). The full-length human NIS (hNIS; a generous gift of Prof. S M Jhiang) was inserted between the BamHI and XhoI sites of the pcDNA5 FRT plasmid (Invitrogen).…”

Section: Methodsmentioning

confidence: 99%

“…The key player in this process is the sodium/ iodide symporter (NIS, for natrium iodide symporter). The rat NIS sequence was the first to be identified (Dai et al 1996), followed by the human (Smanik et al 1996) and mouse sequences (Perron et al 2001). The human and rat/ mouse proteins are 643 and 618 amino acids in length respectively.…”

Section: Introductionmentioning

confidence: 99%

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Comparison of expressed human and mouse sodium/iodide symporters reveals differences in transport properties and subcellular localization

Dayem¹,

Basquin²,

Navarro³

et al. 2008

Journal of Endocrinology

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The active transport of iodide from the bloodstream into thyroid follicular cells is mediated by the Na C /I K symporter (NIS). We studied mouse NIS (mNIS) and found that it catalyzes iodide transport into transfected cells more efficiently than human NIS (hNIS). To further characterize this difference, we compared 125 I uptake in the transiently transfected human embryonic kidney (HEK) 293 cells. We found that the V max for mNIS was four times higher than that for hNIS, and that the iodide transport constant (K m ) was 2 . 5-fold lower for hNIS than mNIS. We also performed immunocytolocalization studies and observed that the subcellular distribution of the two orthologs differed. While the mouse protein was predominantly found at the plasma membrane, its human ortholog was intracellular in w40% of the expressing cells. Using cell surface protein-labeling assays, we found that the plasma membrane localization frequency of the mouse protein was only 2 . 5-fold higher than that of the human protein, and therefore cannot alone account for the difference in the obtained V max values. We reasoned that the observed difference could also be caused by a higher turnover number for iodide transport in the mouse protein.We then expressed and analyzed chimeric proteins. The data obtained with these constructs suggest that the iodide recognition site could be located in the region extending from the N-terminus to transmembrane domain 8, and that the region between transmembrane domain 5 and the C-terminus could play a role in the subcellular localization of the protein.

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“…In this study, we used the mouse NIS identified by Perron et al (2001). Its sequence and known functional properties are similar to those of its rat counterpart (data not shown).…”

Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

See 1 more Smart Citation

Comparison of expressed human and mouse sodium/iodide symporters reveals differences in transport properties and subcellular localization

Dayem¹,

Basquin²,

Navarro³

et al. 2008

Journal of Endocrinology

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“…It has been established that NIS expression is also induced in the mammary gland during lactation (3,22,23). Iodide uptake was also detected in nonlactating mammary glands in particular cases (24).…”

Section: Introductionmentioning

confidence: 98%

“…The rat NIS sequence was the first to be identified (1) followed by the human (2) and mouse sequences (3). NIS (also called SLC5A5), a member of the sodium/solute symporter family, is an integral membrane protein that resides in the basolateral membrane of thyroid epithelial cells (for review see (4)).…”

Section: Introductionmentioning

confidence: 99%

Immunoanalysis indicates that the sodium iodide symporter is not overexpressed in intracellular compartments in thyroid and breast cancers

Peyrottes

Navarro

Ondo-Méndez

et al. 2009

European Journal of Endocrinology

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Objective: The active transport of iodide into thyroid cells is mediated by the Na C /I K symporter (NIS) located in the basolateral membrane. Strong intracellular staining with anti-NIS antibodies has been reported in thyroid and breast cancers. Our initial objective was to screen tumour samples for intracellular NIS staining and then to study the mechanisms underlying the altered subcellular localization of the transporters. Methods: Immunostaining using three different anti-NIS antibodies was performed on paraffinembedded tissue sections from 93 thyroid or breast cancers. Western blot experiments were carried out to determine the amount of NIS protein in 20 samples. Results: Using three different anti-NIS antibodies, we observed intracellular staining in a majority of thyroid tumour samples. Control immunohistochemistry and western blot experiments indicated that this intracellular staining was due to non-specific binding of the antibodies. In breast tumours, very weak intracellular staining was observed in some samples. Western blot experiments suggest that this labelling is also non-specific. Conclusions: Our results strongly indicate that the NIS protein level is low in thyroid and breast cancers and that the intracellular staining obtained with anti-NIS antibodies corresponds to a non-specific signal. Accordingly, to increase the efficiency of radiotherapy for thyroid cancers and to enable the use of radioiodine in the diagnosis and therapy of breast tumours, improving NIS targeting to the plasma membrane will not be sufficient. Instead, increasing the expression level of NIS should remain the major goal of this field.

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Small‐Molecule Inhibitors of Sodium Iodide Symporter Function

et al. 2008

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The Na(+)/I(-) symporter (NIS) mediates iodide uptake into thyroid follicular cells. Although NIS has been cloned and thoroughly studied at the molecular level, the biochemical processes involved in post-translational regulation of NIS are still unknown. The purpose of this study was to identify and characterize inhibitors of NIS function. These small organic molecules represent a starting point in the identification of pharmacological tools for the characterization of NIS trafficking and activation mechanisms. The screening of a collection of 17,020 druglike compounds revealed new chemical inhibitors with potencies down to 40 nM. Fluorescence measurement of membrane potential indicates that these inhibitors do not act by disrupting the sodium gradient. They allow immediate and total iodide discharge from preloaded cells in accord with a specific modification of NIS activity, probably through distinct mechanisms.

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Cloning of the mouse sodium iodide symporter and its expression in the mammary gland and other tissues

Cited by 80 publications

References 38 publications

Comparison of expressed human and mouse sodium/iodide symporters reveals differences in transport properties and subcellular localization

Comparison of expressed human and mouse sodium/iodide symporters reveals differences in transport properties and subcellular localization

Immunoanalysis indicates that the sodium iodide symporter is not overexpressed in intracellular compartments in thyroid and breast cancers

Small‐Molecule Inhibitors of Sodium Iodide Symporter Function

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