Influence of mitochondrial inhibitors on the respiration and energy-dependent uptake of iodide by thyroid slices

Tyler, D.D.; Gonze, Jeanine; Lamy, Françoise; Dumont, Jacques Emile

doi:10.1042/bj1060123

Cited by 33 publications

(13 citation statements)

References 32 publications

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“…Although the biochemical steps involved in iodide trapping have not been elucidated, the process is energydependent (15). A role for a ouabain-sensitive Na+-K+-activated ATPase in this process has also been suggested (16), though a recent study did not find a stoichiometric relationship between these two processes (17).…”

Section: ±71 204+72mentioning

confidence: 97%

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Demonstration of Iodide Transport Defect but Normal Iodide Organification in Nonfunctioning Nodules of Human Thyroid Glands

Field¹,

Larsen²,

Yamashita³

et al. 1973

J. Clin. Invest.

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Section: ±71 204+72mentioning

confidence: 97%

“…Iodide transport is energy-dependent (15), and the defect in the nodules could reflect an abnormality in production or coupling of energy for this process. An abnormality in energy production seems most unlikely since ATP concentrations in the nodules were not reduced (Table V).…”

Section: ±71 204+72mentioning

confidence: 99%

Demonstration of Iodide Transport Defect but Normal Iodide Organification in Nonfunctioning Nodules of Human Thyroid Glands

Field¹,

Larsen²,

Yamashita³

et al. 1973

J. Clin. Invest.

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“…In studies of sheep thyroid slices, when respiration was inhibited and iodide transport blocked, addition of glucose partially restored iodide transport (27). In other studies, inhibition of glycolysis greatly inhibited colloid endocytosis, and glucose addition counteracted this effect (9).…”

mentioning

confidence: 98%

“…8). It has been suggested that glycolytic ATP may be the preferred source of energy for plasma membrane functions such as iodide transport and colloid endocytosis (4,9,27).…”

mentioning

confidence: 99%

MCT1 and its accessory protein CD147 are differentially regulated by TSH in rat thyroid cells

Fanelli¹,

Grollman²,

Wang³

et al. 2003

American Journal of Physiology-Endocrinology and Metabolism

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. MCT1 and its accessory protein CD147 are differentially regulated by TSH in rat thyroid cells. Am J Physiol Endocrinol Metab 285: E1223-E1229, 2003 10.1152/ ajpendo.00172.2003In thyroid cells, basal and TSH-stimulated glycolysis is associated with lactic acid efflux. In this report, we address whether monocarboxylate transporters (MCTs) are present in thyroid tissue for exporting excess lactic acid generated by aerobic glycolysis. Using immunostaining techniques, we show that MCT4 localizes with its accessory protein CD147 in the basolateral membrane of rat thyroid follicular cells. In cultured rat thyroid (FRTL-5) cells, MCT1 rather than MCT4 is expressed. CD147 colocalizes and coimmunoprecipitates with MCT1. TSH upregulates MCT1/ CD147 expression as a function of time through a cAMPdependent mechanism as forskolin reproduces the effect of TSH. TSH enhances protein expression of both MCT1 and CD147 in FRTL-5 cells. Whereas MCT1 protein expression is controlled at the level of transcription, CD147 protein expression is regulated by a posttranscriptional mechanism. Results of these studies suggest that hormone stimulation of lactate transport is mediated by regulating MCT1 transcription. monocarboxylate transporter 1; monocarboxylate transporter 4; thyroid gland; thyroid-stimulating hormone; FRTL-5 cells; glycolysis; lactate IN THE THYROID GLAND, the primary metabolic fuels are glucose and free fatty acids (1,7,8). Oxidative phosphorylation uses mainly free fatty acids as substrate and accounts for Ͼ80% of ATP production. Mitochondrial respiration is primarily regulated by the ADP supply, and the stimulatory effect of TSH and cAMP is secondary to enhanced cellular processes that consume ATP. Aerobic glycolysis accounts for 70% of the glucose metabolized by the thyroid cell and supplies almost 20% of the cellular ATP (reviewed in Ref.

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“…iodide transport (Tyler et al 1968). However, ouabain does not directly interact with NIS and should not show a rapid effect on the iodide current in oocytes measured by voltage clamp.…”

Section: Resultsmentioning

confidence: 99%

Characterization of small-molecule inhibitors of the sodium iodide symporter

Lindenthal

Lecat-Guillet²,

Ondo-Méndez

et al. 2008

Journal of Endocrinology

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The sodium/iodide symporter (NIS) mediates the active transport of iodide from the bloodstream into thyrocytes. NIS function is strategic for the diagnosis and treatment of various thyroid diseases. In addition, a promising anti-cancer strategy based on targeted NIS gene transfer in non-thyroidal cells is currently developed. However, only little information is available concerning the molecular mechanism of NISmediated iodide translocation. Ten small molecules have recently been identified using a high-throughput screening method for their inhibitory effect on iodide uptake of NISexpressing mammalian cells. In the present study, we analyzed these compounds for their rapid and reversible effects on the iodide-induced current in NIS-expressing Xenopus oocytes. Four molecules almost completely inhibited the iodideinduced current; for three of them the effect was irreversible, for one compound the initial current could be fully re-established after washout. Three molecules showed a rapid inhibitory effect of about 75%, half of which was reversible. Another three compounds inhibited the iodideinduced current from 10 to 50%. Some molecules altered the membrane conductance by themselves, i.e. in the absence of iodide. For one of these molecules the observed effect was also found in water-injected oocytes whereas for some others the iodide-independent effect was associated with NIS expression. The tested molecules show a surprisingly high variability in their possible mode of action, and thus are promising tools for further functional characterization of NIS on a molecular level, and they could be useful for medical applications.

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Influence of mitochondrial inhibitors on the respiration and energy-dependent uptake of iodide by thyroid slices

Cited by 33 publications

References 32 publications

Demonstration of Iodide Transport Defect but Normal Iodide Organification in Nonfunctioning Nodules of Human Thyroid Glands

Demonstration of Iodide Transport Defect but Normal Iodide Organification in Nonfunctioning Nodules of Human Thyroid Glands

MCT1 and its accessory protein CD147 are differentially regulated by TSH in rat thyroid cells

Characterization of small-molecule inhibitors of the sodium iodide symporter

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