Biomaterial Database

Effects of sodium on iodide transport in primary cultures of turtle thyroid cells. 1986

S Y Chow, and Y C Yen-Chow, and H S White, and D M Woodbury

Iodide uptake by primary cultures of turtle thyroid cells decreased linearly with reduction of Na+ concentration in the medium, but changes in medium Cl- concentration did not affect iodide uptake. Ouabain, furosemide, monensin, and perchlorate all decreased 125I-uptake by cultured thyroid cells, whereas amiloride and triamterene did not. Ouabain, monensin, perchlorate, and amiloride depolarized the membrane of cultured cells, whereas furosemide and triamterene had no effect. Ouabain and perchlorate increased intracellular Na+ and Cl- and decreased K+ activities; furosemide and monensin reduced all three ions, but triamterene had no effect. Amiloride decreased intracellular Na+ and increased intracellular Cl- activities, however, its effect on K+ activity could not be determined because of interference by this compound of the K+ ion exchanger. All the agents, except furosemide, inhibited Na+-K+-ATPase activity. These experiments demonstrate that 1) Na+-I- cotransport is responsible for most iodide accumulation in thyroid cells; 2) Na+-I- cotransport system is linked to the Na+-K+ pump; 3) active iodide transport does not always correlate with Na+-K+-ATPase activity; 4) a perchlorate-sensitive iodide transport system is present in thyroid cells; 5) transport processes, not involved in active iodide transport (Na+-Cl- cotransport and Na+-H+ counter transport), are also present in cultured thyroid cells.

UI	MeSH Term	Description	Entries
D007454	Iodides	Inorganic binary compounds of iodine or the I- ion.	Iodide
D008564	Membrane Potentials	The voltage differences across a membrane. For cellular membranes they are computed by subtracting the voltage measured outside the membrane from the voltage measured inside the membrane. They result from differences of inside versus outside concentration of potassium, sodium, chloride, and other ions across cells' or ORGANELLES membranes. For excitable cells, the resting membrane potentials range between -30 and -100 millivolts. Physical, chemical, or electrical stimuli can make a membrane potential more negative (hyperpolarization), or less negative (depolarization).	Resting Potentials,Transmembrane Potentials,Delta Psi,Resting Membrane Potential,Transmembrane Electrical Potential Difference,Transmembrane Potential Difference,Difference, Transmembrane Potential,Differences, Transmembrane Potential,Membrane Potential,Membrane Potential, Resting,Membrane Potentials, Resting,Potential Difference, Transmembrane,Potential Differences, Transmembrane,Potential, Membrane,Potential, Resting,Potential, Transmembrane,Potentials, Membrane,Potentials, Resting,Potentials, Transmembrane,Resting Membrane Potentials,Resting Potential,Transmembrane Potential,Transmembrane Potential Differences
D008985	Monensin	An antiprotozoal agent produced by Streptomyces cinnamonensis. It exerts its effect during the development of first-generation trophozoites into first-generation schizonts within the intestinal epithelial cells. It does not interfere with hosts' development of acquired immunity to the majority of coccidial species. Monensin is a sodium and proton selective ionophore and is widely used as such in biochemical studies.	Coban,Monensin Monosodium Salt,Monensin Sodium,Monensin-A-Sodium Complex,Rumensin,Monensin A Sodium Complex
D010042	Ouabain	A cardioactive glycoside consisting of rhamnose and ouabagenin, obtained from the seeds of Strophanthus gratus and other plants of the Apocynaceae; used like DIGITALIS. It is commonly used in cell biological studies as an inhibitor of the NA(+)-K(+)-EXCHANGING ATPASE.	Acocantherin,G-Strophanthin,Acolongifloroside K,G Strophanthin
D011506	Proteins	Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.	Gene Products, Protein,Gene Proteins,Protein,Protein Gene Products,Proteins, Gene
D002478	Cells, Cultured	Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.	Cultured Cells,Cell, Cultured,Cultured Cell
D002712	Chlorides	Inorganic compounds derived from hydrochloric acid that contain the Cl- ion.	Chloride,Chloride Ion Level,Ion Level, Chloride,Level, Chloride Ion
D004247	DNA	A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine).	DNA, Double-Stranded,Deoxyribonucleic Acid,ds-DNA,DNA, Double Stranded,Double-Stranded DNA,ds DNA
D005665	Furosemide	A benzoic-sulfonamide-furan. It is a diuretic with fast onset and short duration that is used for EDEMA and chronic RENAL INSUFFICIENCY.	Frusemide,Fursemide,Errolon,Frusemid,Furanthril,Furantral,Furosemide Monohydrochloride,Furosemide Monosodium Salt,Fusid,Lasix
D000254	Sodium-Potassium-Exchanging ATPase	An enzyme that catalyzes the active transport system of sodium and potassium ions across the cell wall. Sodium and potassium ions are closely coupled with membrane ATPase which undergoes phosphorylation and dephosphorylation, thereby providing energy for transport of these ions against concentration gradients.	ATPase, Sodium, Potassium,Adenosinetriphosphatase, Sodium, Potassium,Na(+)-K(+)-Exchanging ATPase,Na(+)-K(+)-Transporting ATPase,Potassium Pump,Sodium Pump,Sodium, Potassium ATPase,Sodium, Potassium Adenosinetriphosphatase,Sodium-Potassium Pump,Adenosine Triphosphatase, Sodium, Potassium,Na(+) K(+)-Transporting ATPase,Sodium, Potassium Adenosine Triphosphatase,ATPase Sodium, Potassium,ATPase, Sodium-Potassium-Exchanging,Adenosinetriphosphatase Sodium, Potassium,Pump, Potassium,Pump, Sodium,Pump, Sodium-Potassium,Sodium Potassium Exchanging ATPase,Sodium Potassium Pump