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Journal articles on the topic 'HeLa cells; Osmotic cell swelling; Taurine'

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1

Hall, J. A., J. Kirk, J. R. Potts, C. Rae, and K. Kirk. "Anion channel blockers inhibit swelling-activated anion, cation, and nonelectrolyte transport in HeLa cells." American Journal of Physiology-Cell Physiology 271, no. 2 (1996): C579—C588. http://dx.doi.org/10.1152/ajpcell.1996.271.2.c579.

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The effect of osmotic cell swelling on the permeability of HeLa cells to a range of structurally unrelated solutes including taurine, sorbitol, thymidine, choline, and K+ (96Rb+) was investigated. For each solute tested, reduction in the osmolality of the medium from 300 to 200 mosmol/kgH2O caused a significant increase in the unidirectional influx rate. In each case, the osmotically activated transport component was nonsaturable up to external substrate concentrations of 50 mM. Inhibitors of the swelling-activated anion channel of HeLa cells [quinine, 4,4'-diisothiocyanostilbene-2,2'-disulfon
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2

Stutzin, A., A. L. Eguiguren, L. P. Cid, and F. V. Sepulveda. "Modulation by extracellular Cl- of volume-activated organic osmolyte and halide permeabilities in HeLa cells." American Journal of Physiology-Cell Physiology 273, no. 3 (1997): C999—C1007. http://dx.doi.org/10.1152/ajpcell.1997.273.3.c999.

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Organic osmolyte and halide permeability pathways activated in epithelial HeLa cells by osmotically induced cell swelling were studied using electrophysiological and radiotracer efflux techniques. On hypotonic challenge, HeLa cells responded by activating an efflux pathway for [3H]taurine and a swelling-induced outwardly rectifying Cl- channel. Removal of extracellular Cl-, or its replacement by a less permeable anion, enhanced taurine efflux and decreased the inward current (Cl- efflux). The effect of Cl- removal on taurine efflux was not a consequence of changes in membrane potential. The de
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3

Numata, Tomohiro, Takahiro Shimizu, and Yasunobu Okada. "TRPM7 is a stretch- and swelling-activated cation channel involved in volume regulation in human epithelial cells." American Journal of Physiology-Cell Physiology 292, no. 1 (2007): C460—C467. http://dx.doi.org/10.1152/ajpcell.00367.2006.

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Stretch- and swelling-activated cation (SSAC) channels play essential roles not only in sensing and transducing external mechanical stresses but also in regulating cell volume in living cells. However, the molecular nature of the SSAC channel has not been clarified. In human epithelial HeLa cells, single-channel recordings in cell-attached and inside-out patches revealed expression of a Mg2+- and Gd3+-sensitive nonselective cation channel that is exquisitely sensitive to membrane stretch. Whole cell recordings revealed that the macroscopic cationic currents exhibit transient receptor potential
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4

Tomassen, Sebastian F. B., Durk Fekkes, Hugo R. de Jonge, and Ben C. Tilly. "Osmotic swelling-provoked release of organic osmolytes in human intestinal epithelial cells." American Journal of Physiology-Cell Physiology 286, no. 6 (2004): C1417—C1422. http://dx.doi.org/10.1152/ajpcell.00468.2003.

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Human Intestine 407 cells respond to osmotic cell swelling by the activation of Cl−- and K+-selective ionic channels, as well as by stimulating an organic osmolyte release pathway readily permeable to taurine and phosphocholine. Unlike the activation of volume-regulated anion channels (VRAC), activation of the organic osmolyte release pathway shows a lag time of ∼30–60 s, and its activity persists for at least 8–12 min. In contrast to VRAC activation, stimulation of organic osmolyte release did not require protein tyrosine phosphorylation, active p21rho, or phosphatidylinositol 3-kinase activi
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5

Stutzin, Andrés, Rubén Torres, Macarena Oporto, et al. "Separate taurine and chloride efflux pathways activated during regulatory volume decrease." American Journal of Physiology-Cell Physiology 277, no. 3 (1999): C392—C402. http://dx.doi.org/10.1152/ajpcell.1999.277.3.c392.

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Organic osmolyte and halide permeability pathways activated in epithelial HeLa cells by cell swelling were studied by radiotracer efflux techniques and single-cell volume measurements. The replacement of extracellular Cl− by anions that are more permeant through the volume-activated Cl− channel, as indicated by electrophysiological measurements, significantly decreased taurine efflux. In the presence of less-permeant anions, an increase in taurine efflux was observed. Simultaneous measurement of the125I, used as a tracer for Cl−, and [3H]taurine efflux showed that the time courses for the two
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6

Basavappa, Srisaila, Stine F. Pedersen, Nanna K. Jørgensen, J. Clive Ellory, and Else K. Hoffmann. "Swelling-Induced Arachidonic Acid Release via the 85-kDa cPLA2 in Human Neuroblastoma Cells." Journal of Neurophysiology 79, no. 3 (1998): 1441–49. http://dx.doi.org/10.1152/jn.1998.79.3.1441.

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Basavappa, Srisaila, Stine F. Pedersen, Nanna K. Jørgensen, J. Clive Ellory, and Else K. Hoffmann. Swelling-induced arachidonic acid release via the 85-kDa cPLA2 in human neuroblastoma cells. J. Neurophysiol. 79: 1441–1449, 1998. Arachidonic acid or its metabolites have been implicated in the regulatory volume decrease (RVD) response after hypotonic cell swelling in some mammalian cells. The present study investigated the role of arachidonic acid (AA) during RVD in the human neuroblastoma cell line CHP-100. During the first nine minutes of hypo-osmotic exposure the rate of 3H-arachidonic acid
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7

Avella, Martine, Olivier Ducoudret, Didier F. Pisani, and Philippe Poujeol. "Swelling-activated transport of taurine in cultured gill cells of sea bass: physiological adaptation and pavement cell plasticity." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 296, no. 4 (2009): R1149—R1160. http://dx.doi.org/10.1152/ajpregu.90615.2008.

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We have investigated volume-activated taurine transport and ultrastructural swelling response of sea bass gill cells in culture, assuming that euryhaline fish may have developed particularly efficient mechanisms of salinity adaptation. In vivo, when sea basses were progressively transferred from seawater to freshwater, we noticed a decrease in blood osmotic pressure. When gill cells in culture were subjected to 30% hypotonic shock, we observed a five-fold stimulation of [3H]taurine efflux. This transport was reduced by various anion channel inhibitors with the following efficiency: 5-nitro-2-(
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8

Lambert, Ian Henry, Jane Vendelbo Jensen, and Per Amstrup Pedersen. "mTOR ensures increased release and reduced uptake of the organic osmolyte taurine under hypoosmotic conditions in mouse fibroblasts." American Journal of Physiology-Cell Physiology 306, no. 11 (2014): C1028—C1040. http://dx.doi.org/10.1152/ajpcell.00005.2014.

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Mammalian target of rapamycin (mTOR) is a serine/threonine kinase that modulates translation in response to growth factors and alterations in nutrient availability following hypoxia and DNA damage. Here we demonstrate that mTOR activity in Ehrlich Lettré ascites (ELA) cells is transiently increased within minutes following osmotic cell swelling and that inhibition of phosphatidylinositol-3-phosphatase (PTEN) counteracts the upstream phosphatidylinositol kinase and potentiates mTOR activity. PTEN inhibition concomitantly potentiates swelling-induced taurine release via the volume-sensitive tran
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9

Thoroed, S., M. Soergaard, E. Cragoe, and K. Fugelli. "The osmolality-sensitive taurine channel in flounder erythrocytes is strongly stimulated by noradrenaline under hypo-osmotic conditions." Journal of Experimental Biology 198, no. 2 (1995): 311–24. http://dx.doi.org/10.1242/jeb.198.2.311.

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Stimulation of flounder erythrocytes by noradrenaline under isosmotic conditions (330 mosmol kg-1) and physiological Na+ concentration (113 mmol l-1) caused swelling of the cells. The EC50 of this cell swelling was 0.65 µmol l-1 noradrenaline. The effect of the noradrenaline-induced cell swelling on the taurine channel under isosmotic conditions was negligible. However, when the cells were stimulated by noradrenaline (1.0 µmol l-1) before, simultaneously with or after reduction of osmolality (255 mosmol kg-1), the volume regulatory efflux of taurine mediated by the taurine
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10

Pedersen, Stine F., Kristian A. Poulsen, and Ian H. Lambert. "Roles of phospholipase A2 isoforms in swelling- and melittin-induced arachidonic acid release and taurine efflux in NIH3T3 fibroblasts." American Journal of Physiology-Cell Physiology 291, no. 6 (2006): C1286—C1296. http://dx.doi.org/10.1152/ajpcell.00325.2005.

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Osmotic swelling of NIH3T3 mouse fibroblasts activates a bromoenol lactone (BEL)-sensitive taurine efflux, pointing to the involvement of a Ca2+-independent phospholipase A2 (iPLA2) (Lambert IH. J Membr Biol 192: 19–32, 2003). We report that taurine efflux from NIH3T3 cells was not only increased by cell swelling but also decreased by cell shrinkage. Arachidonic acid release to the cell exterior was similarly decreased by shrinkage yet not detectably increased by swelling. NIH3T3 cells were found to express cytosolic calcium-dependent cPLA2-IVA, cPLA2-IVB, cPLA2-IVC, iPLA2-VIA, iPLA2-VIB, and
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11

WARSKULAT, Ulrich, Matthias WETTSTEIN, and Dieter HÄUSSINGER. "Osmoregulated taurine transport in H4IIE hepatoma cells and perfused rat liver." Biochemical Journal 321, no. 3 (1997): 683–90. http://dx.doi.org/10.1042/bj3210683.

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The effects of aniso-osmotic exposure on taurine transport were studied in H4IIE rat hepatoma cells. Hyperosmotic (405 mosmol/l) exposure of H4IIE cells stimulated Na+-dependent taurine uptake and led to an increase in taurine transporter (TAUT) mRNA levels, whereas hypo-osmotic (205 mosmol/l) exposure diminished both taurine uptake and TAUT mRNA levels when compared with normo-osmotic (305 mosmol/l) control incubations. Taurine uptake increased 30Ő40-fold upon raising the ambient osmolarity from 205 to 405 mosmol/l. When H4IIE cells and perfused livers were preloaded with taurine, hypo-osmoti
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12

Jackson, P. S., and K. Strange. "Volume-sensitive anion channels mediate swelling-activated inositol and taurine efflux." American Journal of Physiology-Cell Physiology 265, no. 6 (1993): C1489—C1500. http://dx.doi.org/10.1152/ajpcell.1993.265.6.c1489.

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C6 glioma cells accumulate the organic osmolyte inositol in response to chronic hypertonic stress. Upon return to isotonic conditions, cell swelling activates a Na(+)-independent passive low-affinity inositol efflux mechanism that is inhibited 80-100% by a number of anion transport blockers, certain lipoxygenase blockers, and various polyunsaturated fatty acids. Taurine efflux is also enhanced by cell swelling. The taurine efflux pathway has characteristics that are identical to those of the inositol efflux mechanism, including kinetics of activation and inactivation, osmotic sensitivity, phar
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13

Friis, Martin Barfred, Katrine Gribel Vorum, and Ian Henry Lambert. "Volume-sensitive NADPH oxidase activity and taurine efflux in NIH3T3 mouse fibroblasts." American Journal of Physiology-Cell Physiology 294, no. 6 (2008): C1552—C1565. http://dx.doi.org/10.1152/ajpcell.00571.2007.

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Reactive oxygen species (ROS) are produced in NIH3T3 fibroblasts during hypotonic stress, and H2O2 potentiates the concomitant release of the organic osmolyte taurine (Lambert IH. J Membr Biol 192: 19–32, 2003). The increase in ROS production [5-(and-6)-carboxy-2′, 7′-dichlorodihydrofluorescein diacetate fluorescence] is detectable after a reduction in the extracellular osmolarity from 335 mosM (isotonic) to 300 mosM and reaches a maximal value after a reduction to 260 mosM. The swelling-induced ROS production is reduced by the flavoprotein inhibitor diphenylene iodonium chloride (25 μM) but i
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14

Ullrich, Nina, Adrian Caplanusi, Bert Brône, et al. "Stimulation by caveolin-1 of the hypotonicity-induced release of taurine and ATP at basolateral, but not apical, membrane of Caco-2 cells." American Journal of Physiology-Cell Physiology 290, no. 5 (2006): C1287—C1296. http://dx.doi.org/10.1152/ajpcell.00545.2005.

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Regulatory volume decrease (RVD) is a protective mechanism that allows mammalian cells to restore their volume when exposed to a hypotonic environment. A key component of RVD is the release of K+, Cl−, and organic osmolytes, such as taurine, which then drives osmotic water efflux. Previous experiments have indicated that caveolin-1, a coat protein of caveolae microdomains in the plasma membrane, promotes the swelling-induced Cl− current ( ICl,swell) through volume-regulated anion channels. However, it is not known whether the stimulation by caveolin-1 is restricted to the release of Cl− or whe
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15

Shennan, D. B. "Hyposmotically-Activated Efflux of L-Carnitine from a Human Mammary Cancer Cell Line." Bioscience Reports 21, no. 6 (2001): 779–87. http://dx.doi.org/10.1023/a:1015584724234.

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Cell-swelling, induced by a hyposmotic challenge, stimulated the efflux of L-carnitine from a human mammary cancer cell line, MDA-MB-231. The response was dependent upon the extent of the osmotic shock. Hyposmotically-activated L-carnitine efflux was inhibited by the anion transport blocker diiodosalicylate. The efflux of taurine from MDA-MB-231 cells was also stimulated by a hyposmotic shock via a pathway sensitive to diiodosalicylate. L-carnitine efflux from MDA-MB-231 cells was stimulated by isosmotic swelling in a manner which was inhibited by diiodosalicylate. The results suggest that L-c
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16

Sørensen, Belinda Halling, Unnur Arna Thorsteinsdottir, and Ian Henry Lambert. "Acquired cisplatin resistance in human ovarian A2780 cancer cells correlates with shift in taurine homeostasis and ability to volume regulate." American Journal of Physiology-Cell Physiology 307, no. 12 (2014): C1071—C1080. http://dx.doi.org/10.1152/ajpcell.00274.2014.

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Cisplatin resistance is a major challenge in the treatment of cancer and develops through reduced drug accumulation and an increased ability to avoid drug-induced cell damage, cell shrinkage, and hence initiation of apoptosis. Uptake and release of the semiessential amino acid taurine contribute to cell volume homeostasis, and taurine has been reported to have antiapoptotic effects. Here we find that volume-sensitive taurine release in cisplatin-sensitive [wild-type (WT)] human ovarian cancer A2780 cells is reduced in the presence of the phospholipase A2 inhibitor bromenol lactone, the 5-lipox
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17

Bursell, J. D., and K. Kirk. "Swelling-activated K+ transport via two functionally distinct pathways in eel erythrocytes." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 270, no. 1 (1996): R61—R70. http://dx.doi.org/10.1152/ajpregu.1996.270.1.r61.

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Following osmotic swelling, erythrocytes from the European eel, Anguilla anguilla, underwent a regulatory volume decrease. This was prevented by replacement of Na+ with K+ in the suspending medium, consistent with a role for the (normally outward) electrochemical K+ gradient in the volume-regulatory response. The effect of cell swelling on K- transport in these cells was investigated using 86Rb+ as a tracer for K+. Osmotic swelling resulted in an increase in ouabain-insensitive K+ transport that was highest for cells in Cl- and Br- media but which was also significant in I- and NO3- media. Tre
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18

Netti, Vanina, Alejandro Pizzoni, Martha Pérez-Domínguez, et al. "Release of taurine and glutamate contributes to cell volume regulation in human retinal Müller cells: differences in modulation by calcium." Journal of Neurophysiology 120, no. 3 (2018): 973–84. http://dx.doi.org/10.1152/jn.00725.2017.

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Neuronal activity in the retina generates osmotic gradients that lead to Müller cell swelling, followed by a regulatory volume decrease (RVD) response, partially due to the isoosmotic efflux of KCl and water. However, our previous studies in a human Müller cell line (MIO-M1) demonstrated that an important fraction of RVD may also involve the efflux of organic solutes. We also showed that RVD depends on the swelling-induced Ca2+ release from intracellular stores. Here we investigate the contribution of taurine (Tau) and glutamate (Glu), the most relevant amino acids in Müller cells, to RVD thro
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19

Falktoft, B., and I. H. Lambert. "Ca2+-mediated Potentiation of the Swelling-induced Taurine Efflux from HeLa Cells: On the Role of Calmodulin and Novel Protein Kinase C Isoforms." Journal of Membrane Biology 201, no. 2 (2004): 59–75. http://dx.doi.org/10.1007/s00232-004-0705-6.

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