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Journal articles on the topic 'Antiporno'

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Published: 25 June 2021

Last updated: 29 July 2025

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1

Tonnessen, T. I., K. Sandvig, and S. Olsnes. "Role of Na(+)-H+ and Cl(-)-HCO3- antiports in the regulation of cytosolic pH near neutrality." American Journal of Physiology-Cell Physiology 258, no. 6 (1990): C1117—C1126. http://dx.doi.org/10.1152/ajpcell.1990.258.6.c1117.

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In Vero cells, Na(+)-H+ antiport as well as Na(+)-coupled and Na(+)-independent Cl(-)-HCO3- antiport are involved in regulation of cytosolic pH (pHi) after large (unphysiological) deviations from neutrality. In this paper we have studied to which extent each of the three antiports is involved in regulation of pHi after small deviations from neutrality expected to occur under physiological conditions. At physiological extracellular pH (pHo), inhibition of Na(+)-H+ exchange by amiloride did not alter pHi. At neutral and alkaline pHo, pHi was found to be lower in the presence of HCO3- than in its

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2

Cavaliere, Matteo, and Daniela Genova. "P Systems with Symport/Antiport of Rules." JUCS - Journal of Universal Computer Science 10, no. (5) (2004): 540–58. https://doi.org/10.3217/jucs-010-05-0540.

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Moving "instructions" instead of "data" using transport mechanisms inspired by biology is the basic idea of the computing device presented in this paper. Specifically, we propose a new class of P systems that use both evolution rules and symport/antiport rules. The idea of this kind of systems is the following: during a computation, symbol-objects (the "data") evolve using evolution rules, but they cannot be moved, on the other hand, the evolution rules (the "instructions") can be moved across the membranes using classical symport/antiport rules. We present a number of results using different

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3

Cheng, J., K. Baldwin, A. A. Guffanti, and T. A. Krulwich. "Na+/H+ antiport activity conferred by Bacillus subtilis tetA(L), a 5' truncation product of tetA(L), and related plasmid genes upon Escherichia coli." Antimicrobial Agents and Chemotherapy 40, no. 4 (1996): 852–57. http://dx.doi.org/10.1128/aac.40.4.852.

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An Escherichia coli transformant expressing the Bacillus subtilis tetA(L) gene from a weak promoter was challenged by growth on medium with low, increasing tetracycline concentrations. Changes in the substrate preference ratios of the TetA(L)-mediated resistances and antiports were examined in view of recent findings suggesting that TetA(L) catalyzes efflux of Na+ in exchange for protons in addition to having the ability to catalyze metal-tetracycline/H+ antiport. After growth of the transformant on 1 microgram or more of tetracycline per ml for 12 to 15 h, the tetA(L) gene in the plasmid was

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4

Houle, Karen. "Antiporn Cons and Pros." International Studies in Philosophy 30, no. 1 (1998): 79–90. http://dx.doi.org/10.5840/intstudphil1998301110.

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5

Eaton, A. W. "A Sensible Antiporn Feminism." Ethics 117, no. 4 (2007): 674–715. http://dx.doi.org/10.1086/519226.

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6

CAVALIERE, MATTEO, and VINCENZO DEUFEMIA. "FURTHER RESULTS ON TIME-FREE P SYSTEMS." International Journal of Foundations of Computer Science 17, no. 01 (2006): 69–89. http://dx.doi.org/10.1142/s012905410600370x.

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Membrane systems (currently called P systems) are parallel computing devices inspired by the structure and the functioning of living cells. A standard feature of P systems is that each rule is executed in exactly one time unit. Actually, in living cells different chemical reactions might take different times to be executed; moreover, it might be hard to know precisely such time of execution. For this reason, in [7] two models of P systems (time-free and clock-free P systems) have been defined and investigated, where the time of execution of the rules is arbitrary and the output produced by the

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7

Ng, L. L., P. Delva, and J. E. Davies. "Intracellular pH regulation of SV-40 virus transformed human MRC-5 fibroblasts and cell membrane cholesterol." American Journal of Physiology-Cell Physiology 264, no. 4 (1993): C789—C793. http://dx.doi.org/10.1152/ajpcell.1993.264.4.c789.

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Alterations in membrane cholesterol could affect the activity of various membrane transporters, including the Na(+)-H+ antiport. The effect of cellular cholesterol depletion (with phosphatidylcholine liposomes) and enrichment (with cholesterol and phosphatidylcholine liposomes) on cellular pH regulation was studied in SV-40 virus transformed human MRC-5 fibroblasts. Cellular cholesterol depletion led to activation of the Na(+)-H+ antiport by an increased maximal velocity (Vmax) of the transporter, with no changes in the apparent dissociation constant (Kd) or Hill coefficient for intracellular

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8

Cutaia, M. V., N. Parks, J. Centracchio, S. Rounds, K. P. Yip, and A. M. Sun. "Effect of hypoxic exposure on Na+/H+antiport activity, isoform expression, and localization in endothelial cells." American Journal of Physiology-Lung Cellular and Molecular Physiology 275, no. 3 (1998): L442—L451. http://dx.doi.org/10.1152/ajplung.1998.275.3.l442.

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Little is known about the effects of prolonged hypoxic exposure on membrane ion transport activity. The Na+/H+antiport is an ion transport site that regulates intracellular pH in mammalian cells. We determined the effect of prolonged hypoxic exposure on human pulmonary arterial endothelial cell antiport activity, gene expression, and localization. Monolayers were incubated under hypoxic or normoxic conditions for 72 h. Antiport activity was determined as the rate of recovery from intracellular acidosis. Antiport isoform identification and gene expression were determined with RT-PCR and Norther

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9

Southworth, Thomas W., Arthur A. Guffanti, Anne Moir, and Terry A. Krulwich. "GerN, an Endospore Germination Protein ofBacillus cereus, Is an Na+/H+-K+ Antiporter." Journal of Bacteriology 183, no. 20 (2001): 5896–903. http://dx.doi.org/10.1128/jb.183.20.5896-5903.2001.

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ABSTRACT GerN, a Bacillus cereus spore germination protein, exhibits homology to a widely distributed group of putative cation transporters or channel proteins. GerN complemented the Na+-sensitive phenotype of an Escherichia coli mutant that is deficient in Na+/H+ antiport activity (strain KNabc). GerN also reduced the concentration of K+ required to support growth of an E. coli mutant deficient in K+ uptake (strain TK2420). In a fluorescence-based assay of evertedE. coli KNabc membrane vesicles, GerN exhibited robust Na+/H+ antiport activity, with a Km for Na+ estimated at 1.5 mM at pH 8.0 an

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10

Jin, Jie, Arthur A. Guffanti, Catherine Beck та Terry A. Krulwich. "Twelve-Transmembrane-Segment (TMS) Version (ΔTMS VII-VIII) of the 14-TMS Tet(L) Antibiotic Resistance Protein Retains Monovalent Cation Transport Modes but Lacks Tetracycline Efflux Capacity". Journal of Bacteriology 183, № 8 (2001): 2667–71. http://dx.doi.org/10.1128/jb.183.8.2667-2671.2001.

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ABSTRACT A “Tet(L)-12” version of Tet(L), a tetracycline efflux protein with 14 transmembrane segments (TMS), was constructed by deletion of two central TMS. Tet(L)-12 catalyzed Na+/H+antiport and antiport with K+ as a coupling ion as well as or better than wild-type Tet(L) but exhibited no tetracycline-Me2+/H+ antiport inEscherichia coli vesicles.

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11

Incerpi, S., S. Spagnuolo, F. Terenzi, and S. Leoni. "EGF modulation of Na+/H+ antiport in rat hepatocytes: different sensitivity in adult and fetal cells." American Journal of Physiology-Cell Physiology 270, no. 3 (1996): C841—C847. http://dx.doi.org/10.1152/ajpcell.1996.270.3.c841.

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The modulation by epidermal growth factor (EGF) of the Na+/H+ antiport in fetal and adult rat hepatocytes was studied in nominally HCO3- free solution. EGF (10 nM) activated the antiport in adult rat hepatocytes by 0.22 +/- 0.03 (mean +/- SD;n=10) pH units over basal value, measured with the fluorescent pH-sensitive intracellular probe, 2',7'-bis(carboxyethyl)-5(6)- carboxyfluorescein (BCECF). The effect of EGF was inhibited by amiloride analogue 5-(N-ethyl-N-isopropyl) amiloride (EIPA), by ouabain, inhibitor of the Na+ pump, and by erbstatin analogue, an inhibitor of the tyrosine kinase activ

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12

Puceat, M., O. Clement-Chomienne, A. Terzic, and G. Vassort. "Alpha 1-adrenoceptor and purinoceptor agonists modulate Na-H antiport in single cardiac cells." American Journal of Physiology-Heart and Circulatory Physiology 264, no. 2 (1993): H310—H319. http://dx.doi.org/10.1152/ajpheart.1993.264.2.h310.

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We investigated the effects of an alpha 1-adrenoceptor (phenylephrine) and a purinoceptor agonist (ATP), both of which accelerate the phosphoinositide turnover, on the Na-H antiport activity of rat single cardiac cells using the pH-sensitive fluorescent indicator seminaphthorhodafluor-1 (SNARF-1). Both phenylephrine, in the presence of a beta-adrenoceptor blocker, and ATP enhanced the ability of the cell to regulate its intracellular pH (pHi) after an imposed acid load. This effect was observed in HCO3-free N-2-hydroxyethylpiperazine-N'-2-ethanesulfonic acid (HEPES) and prevented by Na-H antip

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13

Sastrasinh, M., P. Young, E. J. Cragoe, and S. Sastrasinh. "The Na+/H+ antiport in renal mitochondria." American Journal of Physiology-Cell Physiology 268, no. 5 (1995): C1227—C1234. http://dx.doi.org/10.1152/ajpcell.1995.268.5.c1227.

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In isolated renal mitochondria, Na+ and Li+ stimulated H+ efflux from the mitochondrial matrix. In submitochondrial particles (SMP), Na+ flux was also coupled to H+ transport in the opposite direction. The overshoot of Na+ uptake in SMP with an outwardly directed H+ gradient indicated that downhill efflux of H+ through the mitochondrial membrane induced uphill transport of Na+. Similar to the Na+/H+ antiport in other types of mitochondria, the antiport in renal mitochondria was more sensitive to amiloride derivatives than to amiloride itself. Benzamil and ethylisopropylamiloride (EIPA), but no

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14

Jung, Dennis W., and Gerald P. Brierley. "Matrix free Mg2+ and the regulation of mitochondrial volume." American Journal of Physiology-Cell Physiology 277, no. 6 (1999): C1194—C1201. http://dx.doi.org/10.1152/ajpcell.1999.277.6.c1194.

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Mitochondria must maintain volume homeostasis in order to carry out oxidative phosphorylation. It has been postulated that the concentration of free Mg2+([Mg2+]) serves as the sensor of matrix volume and regulates a K+-extruding K+/H+antiport (K. D. Garlid. J. Biol. Chem. 255: 11273–11279, 1980). To test this hypothesis, the fluorescent probe furaptra was used to monitor [Mg2+] and free Ca2+ concentration ([Ca2+]) in the matrix of isolated beef heart mitochondria, and K+/H+antiport activity was measured by passive swelling in potassium acetate. Concentrations that result in 50% inhibition of m

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15

Mills, G. B., R. K. Cheung, E. J. Cragoe, S. Grinstein, and E. W. Gelfand. "Activation of the Na+/H+ antiport is not required for lectin-induced proliferation of human T lymphocytes." Journal of Immunology 136, no. 4 (1986): 1150–54. http://dx.doi.org/10.4049/jimmunol.136.4.1150.

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Abstract Interaction of some mitogenic lectins and growth factors with the cell surface leads to activation of the Na+/H+ antiport and a resultant cytoplasmic alkalinization. Because amiloride inhibits both Na+/H+ exchange and cell proliferation, it has been hypothesized that activation of the antiport is an obligatory requirement and may, perhaps, be the "trigger" for proliferation. However, concentrations of amiloride which inhibit the antiport also inhibit several other intracellular processes, including protein synthesis and phosphorylation. To determine whether activation of the Na+/H+ an

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16

Davies, J. E., and L. L. Ng. "Simvastatin and Intracellular pH Regulation by the Na+/H+ Antiport of Sv40-Virus-Transformed Human Mrc5 Fibroblasts." Clinical Science 84, no. 6 (1993): 633–43. http://dx.doi.org/10.1042/cs0840633.

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1. Inhibition of 3-hydroxy-3-methylglutaryl-CoA reductase by simvastatin leads to inhibition of both cell growth and Na+/H+ antiport activity. The effect of simvastatin on intracellular pH and Na+/H+ antiport activity was therefore studied on an adherent cell line, the SV40-virus-transformed MRC5 human fibroblast. 2. Simvastatin led to a dose-dependent decrease in intracellular pH, attributed to a reduction in Na+/H+ exchange, together with a rounding of cell shape. Mevalonate (1 mmol/l) prevented these effects of simvastatin, and when added after inhibition of the antiport by simvastatin, rev

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17

Mitchell, Claire H., Johannes C. Fleischhauer, W. Daniel Stamer, K. Peterson-Yantorno, and Mortimer M. Civan. "Human trabecular meshwork cell volume regulation." American Journal of Physiology-Cell Physiology 283, no. 1 (2002): C315—C326. http://dx.doi.org/10.1152/ajpcell.00544.2001.

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The volume of certain subpopulations of trabecular meshwork (TM) cells may modify outflow resistance of aqueous humor, thereby altering intraocular pressure. This study examines the contribution that Na+/H+, Cl−/HCO[Formula: see text]exchange, and K+-Cl− efflux mechanisms have on the volume of TM cells. Volume, Cl− currents, and intracellular Ca2+ activity of cultured human TM cells were studied with calcein fluorescence, whole cell patch clamping, and fura 2 fluorescence, respectively. At physiological bicarbonate concentration, the selective Na+/H+ antiport inhibitor dimethylamiloride reduce

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18

Rotin, D., and S. Grinstein. "Impaired cell volume regulation in Na(+)-H+ exchange-deficient mutants." American Journal of Physiology-Cell Physiology 257, no. 6 (1989): C1158—C1165. http://dx.doi.org/10.1152/ajpcell.1989.257.6.c1158.

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To elucidate the mechanism of regulatory volume increase (RVI) in Chinese hamster ovary cells, Na(+)-H+ exchange-deficient mutants, called AP-1, were derived from WT-5 cells, a wildtype subclone. The absence of functional antiports in AP-1 cells was established through measurements of intracellular pH (pHi) and Na+ uptake. Cells exposed to hypotonic medium initially swelled but regained near-normal volume within minutes. When isotonicity was then restored, WT-5 cells shrank immediately and then carried out RVI, which was inhibited by 0.1 mM amiloride. This amiloride-sensitive RVI was absent in

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19

Civan, M. M., E. J. Cragoe, and K. Peterson-Yantorno. "Intracellular pH in frog skin: effects of Na+, volume, and cAMP." American Journal of Physiology-Renal Physiology 255, no. 1 (1988): F126—F134. http://dx.doi.org/10.1152/ajprenal.1988.255.1.f126.

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Single skins were analyzed by 31P-nuclear magnetic resonance (NMR) spectroscopy during alternate perfusion with control and experimental solutions. Intracellular (pHc) and extracellular (pHo) pH were monitored by measuring the spectral frequencies of intracellular Pi and external methylphosphonate, respectively. Base-line pHc was 7.20 +/- 0.02 (SE) when pHo was 6.99 +/- 0.02. A 4-acetamido-4'-isothiocyanostilbene-2,2'-disulfonic acid (SITS)-inhibitable, HCO3--dependent alkaline shift in pHc can be elicited by replacing external Cl- by gluconate or sulfate. We now report that this effect is obs

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20

HENDRICH, LARS, and CHRIS H. S. WATTS. "An endemic predaceous water beetle from the Murchison River in Western Australia—Antiporus kalbarriensis sp.n. (Coleoptera: Dytiscidae, Hydroporinae, Hydroporini)." Zootaxa 2338, no. 1 (2010): 35. http://dx.doi.org/10.11646/zootaxa.2338.1.3.

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Antiporus kalbarriensis sp.n. is described from the Murchison bioregion in Western Australia. The species appears to be restricted to backwater pools and oxbows along the Murchison River. Morphologically it is near Antiporus bakewellii (Clark, 1862) (Queensland, New South Wales), A. jenniferae Watts, 1997 (Northern Territory, N Queensland, NW Australia) and A. simplex Watts, 1978 (Queensland) but differs by the form of the median lobe, size and male proclaw. The habitat and its water beetle coenosis are described in detail. Additional distributional records for A. bakewellii and A. jenniferae

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21

Robinson, Anne E., Nathan E. Thomas, Emma A. Morrison, Bryan M. Balthazor, and Katherine A. Henzler-Wildman. "New free-exchange model of EmrE transport." Proceedings of the National Academy of Sciences 114, no. 47 (2017): E10083—E10091. http://dx.doi.org/10.1073/pnas.1708671114.

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EmrE is a small multidrug resistance transporter found in Escherichia coli that confers resistance to toxic polyaromatic cations due to its proton-coupled antiport of these substrates. Here we show that EmrE breaks the rules generally deemed essential for coupled antiport. NMR spectra reveal that EmrE can simultaneously bind and cotransport proton and drug. The functional consequence of this finding is an exceptionally promiscuous transporter: not only can EmrE export diverse drug substrates, it can couple antiport of a drug to either one or two protons, performing both electrogenic and electr

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22

Mackovic-Basic, M., L. G. Fine, J. T. Norman, E. J. Cragoe, and I. Kurtz. "Stimulation of Na+/H+ exchange is not required for induction of hypertrophy of renal cells in vitro." Journal of the American Society of Nephrology 3, no. 5 (1992): 1124–30. http://dx.doi.org/10.1681/asn.v351124.

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Hypertrophy of renal proximal tubular cells is associated with an early increase in Na+/H+ antiport activity both in vivo and in vitro. The purpose of the study presented here was to determine whether functioning Na+/H+ antiport activity is required for hypertrophy to occur. LLC-PK1 cells deficient in Na+/H+ antiport activity were prepared by the "proton-suicide" method. Mutant cells had 28 to 40% of the normal Na+/H+ antiport activity. The addition of 50 nM methylisobutylamiloride to these cells decreased the antiport activity to less than 5% of the control value. In the mutant cells, steady-

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23

Grinstein, S., S. Cohen, J. D. Goetz, and A. Rothstein. "Osmotic and phorbol ester-induced activation of Na+/H+ exchange: possible role of protein phosphorylation in lymphocyte volume regulation." Journal of Cell Biology 101, no. 1 (1985): 269–76. http://dx.doi.org/10.1083/jcb.101.1.269.

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The Na+/H+ antiport is stimulated by 12-O-tetradecanoylphorbol-13, acetate (TPA) and other phorbol esters in rat thymic lymphocytes. Mediation by protein kinase C is suggested by three findings: (a) 1-oleoyl-2-acetylglycerol also activated the antiport; (b) trifluoperazine, an inhibitor of protein kinase C, blocked the stimulation of Na+/H+ exchange; and (c) activation of countertransport was accompanied by increased phosphorylation of specific membrane proteins. The Na+/H+ antiport is also activated by osmotic cell shrinking. The time course, extent, and reversibility of the osmotically induc

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24

Ricci, R., P. Baldini, L. Bogetto, et al. "Dual modulation of Na/H antiport by atrial natriuretic factor in rat aortic smooth muscle cells." American Journal of Physiology-Cell Physiology 273, no. 2 (1997): C643—C652. http://dx.doi.org/10.1152/ajpcell.1997.273.2.c643.

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The aim of the present work was to study the effect of the atrial natriuretic factor (ANF) on the Na/H antiport in rat aorta smooth muscle cells, evaluated as intracellular pH (pHi) recovery after an acid load with ammonium chloride. The Na/H antiport was studied using a fluorescent probe, sensitive to pHi, 2',7'-bis(carboxyethyl)-5(6)-carboxyfluorescein. Our data indicate that ANF modulates the activity of the Na/H antiport in both a dose- and time-dependent manner. Hormone concentrations of 10(-10) M activate the antiport, increasing both the rate of recovery and the set point by approximate

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25

Ng, L. L., and J. E. Davies. "HMG CoA reductase inhibitors affect Na(+)-H+ antiport activity in human lymphoblasts." American Journal of Physiology-Cell Physiology 261, no. 5 (1991): C780—C786. http://dx.doi.org/10.1152/ajpcell.1991.261.5.c780.

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The Na(+)-H+ antiport is a membrane-bound glycoprotein that extrudes intracellular acid loads and regulates cellular volume. Cellular synthesis of the oligosaccharide side chains of glycoproteins is dependent on a supply of mevalonate, itself a product of the rate-limiting enzyme of cholesterol synthesis 3-hydroxy-3-methylglutaryl coenzyme A (HMG CoA) reductase. The effect of two HMG CoA reductase inhibitors (simvastatin and 25-hydroxycholesterol) on intracellular pH and Na(+)-H+ exchange was therefore studied. Inhibition of the Na(+)-H+ antiport by these agents led to a fall in intracellular

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26

Dudley, C. R. K., D. J. Taylor, L. L. Ng, et al. "Evidence for Abnormal Na+/H+ Antiport Activity Detected by Phosphorus Nuclear Magnetic Resonance Spectroscopy in Exercising Skeletal Muscle of Patients with Essential Hypertension." Clinical Science 79, no. 5 (1990): 491–97. http://dx.doi.org/10.1042/cs0790491.

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1. Exercise-induced pH changes in skeletal muscle were studied in a group of eight subjects with essential hypertension by using 31P n.m.r. spectroscopy. 2. Leucocyte Na+/H+ antiport activity was measured in vitro in the same subjects using a pH-sensitive fluorescent dye. 3. Resting skeletal muscle pH and unstimulated leucocyte pH values were similar to those in control subjects, but increased Na+/H+ antiport activity was demonstrated in the leucocytes from hypertensive subjects by acid loading in vitro. Decreased skeletal muscle acidification and an increased rate of pH recovery was also demo

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27

Jiang, Suxia, Tao Liang, Bowen Xu, Zhichao Shen, Xiaoliang Zhu, and Yanfeng Wang. "Cell-like P Systems with Channel States and Synchronization Rule." Mathematics 11, no. 1 (2022): 117. http://dx.doi.org/10.3390/math11010117.

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Cell-like P systems with channel states and symport/antiport rules (CCS P systems) are a type of nondeterministic parallel biological computing model, where there exists a channel between adjacent regions and there is a state on each channel to control the execution of symport/antiport rules. In this work, a synchronization rule is introduced into CCS P systems, a variant of CCS P systems called CCS P systems with synchronization rule (CCSs P systems) is proposed. The universality of CCSs P systems with only uniport (symport or antiport) rules is investigated. By simulating the register machin

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Swartz, Talia H., Masahiro Ito, Takayuki Ohira, Shinsuke Natsui, David B. Hicks, and Terry A. Krulwich. "Catalytic Properties of Staphylococcus aureus and Bacillus Members of the Secondary Cation/Proton Antiporter-3 (Mrp) Family Are Revealed by an Optimized Assay in an Escherichia coli Host." Journal of Bacteriology 189, no. 8 (2007): 3081–90. http://dx.doi.org/10.1128/jb.00021-07.

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ABSTRACT Monovalent cation proton antiporter-3 (Mrp) family antiporters are widely distributed and physiologically important in prokaryotes. Unlike other antiporters, they require six or seven hydrophobic gene products for full activity. Standard fluorescence-based assays of Mrp antiport in membrane vesicles from Escherichia coli transformants have not yielded strong enough signals for characterization of antiport kinetics. Here, an optimized assay protocol for vesicles of antiporter-deficient E. coli EP432 transformants produced higher levels of secondary Na+(Li+)/H+ antiport than previously

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Grinstein, S., A. Rothstein, and S. Cohen. "Mechanism of osmotic activation of Na+/H+ exchange in rat thymic lymphocytes." Journal of General Physiology 85, no. 5 (1985): 765–87. http://dx.doi.org/10.1085/jgp.85.5.765.

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The activity of the Na+/H+ exchange system of rat thymic lymphocytes was determined by means of intracellular (pHi) and extracellular pH (pH0) measurements. In isotonic media, the antiport is virtually quiescent at physiological pHi (7.0-7.1), but is greatly activated by cytoplasmic acidification. At normal pHi, the antiport can also be activated by osmotic shrinking. Osmotic activation occurs after a delay of 20-30 s and is reversed several minutes after iso-osmolarity is restored. The mechanism of activation was analyzed by comparing the kinetic parameters of transport in resting (isotonic)

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30

Church, J. G., G. B. Mills, and R. N. Buick. "Activation of the Na+/H+ antiport is not required for epidermal growth factor-dependent gene expression, growth inhibition or proliferation in human breast cancer cells." Biochemical Journal 257, no. 1 (1989): 151–57. http://dx.doi.org/10.1042/bj2570151.

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Mitogen interaction with specific receptors in many cell types leads to activation of the Na+/H+ antiport and a resultant cytoplasmic alkalinization. Since amiloride inhibits both Na+/H+ exchange and cell proliferation, it has been hypothesized that activation of the antiport is an obligatory requirement for mitogenesis. However, concentrations of amiloride which inhibit the antiport also inhibit other cellular processes, including protein synthesis and phosphorylation. We have used an epidermal growth factor (EGF) receptor gene-amplified human breast cancer cell line, the growth of which is i

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Vallance, S. J., C. P. Downes, E. J. Cragoe, and A. D. Whetton. "Granulocyte-macrophage colony-stimulating factor can stimulate macrophage proliferation via persistent activation of Na+/H+ antiport. Evidence for two distinct roles for Na+/H+ antiport activation." Biochemical Journal 265, no. 2 (1990): 359–64. http://dx.doi.org/10.1042/bj2650359.

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Macrophages respond to a variety of extracellular stimuli which can modulate the proliferation, development, activation and functional activity of these cells. The effects of two such agents, granulocytemacrophage colony-stimulating factor (GM-CSF, which stimulates proliferation) and platelet-activating factor (PAF, which stimulates chemotaxis and bactericidal activity), on cellular signal transduction mechanisms were compared. PAF can stimulate inositol lipid hydrolysis leading to Ca2+ mobilization. GM-CSF on the other hand has no effect on these events. Both agonists do, however, share an ab

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Cutaia, M., K. Tollefson, J. Kroczynski, N. Parks, and S. Rounds. "Role of the Na/H antiport in pH-dependent cell death in pulmonary artery endothelial cells." American Journal of Physiology-Lung Cellular and Molecular Physiology 278, no. 3 (2000): L536—L544. http://dx.doi.org/10.1152/ajplung.2000.278.3.l536.

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We investigated the role of intracellular pH (pHi) and Na/H exchange in cell death in human pulmonary artery endothelial cells (HPAEC) following a metabolic insult (inhibition-oxidative phosphorylation, glycolysis). Metabolic inhibition in medium at pH 7.4 decreased viability (0–15% live cells) over 6 h. Cell death was attenuated by maneuvers that decreased pHi and inhibited Na/H exchange (acidosis, Na/H antiport inhibitors). In contrast, cell death was potentiated by maneuvers that elevated pHi or increased Na/H exchange (monensin, phorbol ester treatment) before the insult. HPAEC demonstrate

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33

Hensley, C. B., M. E. Bradley, and A. K. Mircheff. "Parathyroid hormone-induced translocation of Na-H antiporters in rat proximal tubules." American Journal of Physiology-Cell Physiology 257, no. 4 (1989): C637—C645. http://dx.doi.org/10.1152/ajpcell.1989.257.4.c637.

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Parathyroid hormone (PTH) is believed to inhibit bicarbonate reabsorption by inhibiting Na-H antiport activity in proximal tubular brush-border membranes. The sequence of events triggered by PTH was investigated in a crude preparation of proximal tubules obtained by mechanical disruption and filtration through nylon mesh filters. Tubule samples were subjected to analytical subcellular fractionation after 2-, 5-, and 30-min treatments with 1 IU/ml PTH. These PTH-treatment intervals caused 54, 63, and 68% decreases in the Na-H antiport activity of a population of brush-border membrane vesicles t

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34

Yamaguchi, D. T., R. Sakai, L. Bahn, E. J. Cragoe, and S. C. Jordan. "Amiloride inhibition of DNA synthesis and immunoglobulin production by activated human peripheral blood mononuclear cells is independent of sodium/hydrogen antiport." Journal of Immunology 137, no. 4 (1986): 1300–1304. http://dx.doi.org/10.4049/jimmunol.137.4.1300.

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Abstract Activation of sodium/proton (Na+/H+) antiport activity has been shown to occur as an early event in mitogenesis. Because amiloride inhibits Na+/H+ antiport activity, it is hypothesized that mitogenesis may be inhibited by amiloride. In this work, we examined the effect of amiloride on DNA synthesis as measured by [3H]thymidine uptake and immunoglobulin (Ig) production as measured by an ELISA system in human peripheral blood mononuclear cells (PBM). Amiloride at 100 microM concentration inhibited irradiated Raji cell (*R)-activated and phytohemagglutinin-P (PHA-P)-stimulated DNA synthe

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35

Alarie, Yves, and Chris H. S. Watts. "Larvae of the genus Antiporus (Coleoptera : Dytiscidae) and phylogenetic implications." Invertebrate Systematics 18, no. 5 (2004): 523. http://dx.doi.org/10.1071/is03025.

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The larvae of Antiporus blakeii (Clark), A. femoralis (Boheman), A. gilbertii (Clark), A. hollingsworthi Watts, A. jenniferae Watts, A. uncifer Sharp and A. willyamsi Watts are described with an emphasis on chaetotaxy of the head capsule, head appendages, legs, last abdominal segment and urogomphi. A parsimony analysis based on 17 informative larval characteristics was conducted using the program PAUP*. The 11 most parsimonious trees support a monophyletic origin of the genera Antiporus Sharp, Nebrioporus Régimbart, Scarodytes Gozis, and Stictotarsus Zimmermann. Unambiguous synapomorphies supp

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36

Lepier, A., M. Azuma, W. R. Harvey, and H. Wieczorek. "K+/H+ antiport in the tobacco hornworm midgut: the K(+)-transporting component of the K+ pump." Journal of Experimental Biology 196, no. 1 (1994): 361–73. http://dx.doi.org/10.1242/jeb.196.1.361.

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The midgut of the tobacco hornworm secretes K+ across the apical plasma membrane of its goblet cells. This secondary K+ transport results from K+/H+ antiport energized by the proton-motive force generated by a primary, H(+)-transporting plasma membrane V-ATPase. Thus, the lepidopteran midgut constitutes a well-established example of the emerging concept that the proton-motive force is an alternative to the classical sodium-motive force for the energization of animal plasma membranes. K+/H+ antiport in the tobacco hornworm midgut is electrophoretic, exchanging 2H+ for 1K+. Under physiological c

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37

Ho, A. K., and C. L. Chik. "Inhibitors of Na(+)-H+ exchange block stimulus-provoked pineal melatonin synthesis." American Journal of Physiology-Endocrinology and Metabolism 263, no. 3 (1992): E481—E488. http://dx.doi.org/10.1152/ajpendo.1992.263.3.e481.

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In rat pinealocytes, amiloride can modulate adrenergic-stimulated cyclic nucleotide accumulation. In this study, the effect of amiloride on melatonin production was characterized. Addition of 5-(N,N-hexamethylene)amiloride, a potent inhibitor of the Na(+)-H+ antiport, dose dependently inhibited norepinephrine- and isoproterenol-stimulated N-acetyltransferase (NAT) activity and melatonin production. Similar inhibition was also observed when pineal melatonin synthesis was stimulated directly with forskolin or dibutyryl adenosine 3',5'-cyclic monophosphate (cAMP), suggesting that the site of inhi

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38

Gunby, P. "Worldwide antipolio campaign strategy evolving." JAMA: The Journal of the American Medical Association 267, no. 4 (1992): 479a—479. http://dx.doi.org/10.1001/jama.267.4.479a.

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Gunby, Phil. "Worldwide Antipolio Campaign Strategy Evolving." JAMA: The Journal of the American Medical Association 267, no. 4 (1992): 479. http://dx.doi.org/10.1001/jama.1992.03480040027004.

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40

Michnowska, M., M. Smogorzewski, and S. G. Massry. "Impaired Na(+)-H+ exchanger activity of hepatocytes in chronic renal failure." Journal of the American Society of Nephrology 8, no. 6 (1997): 929–34. http://dx.doi.org/10.1681/asn.v86929.

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Available data indicate that cation transport is impaired in many cells in chronic renal failure (CRF). The information on the activity of the Na(+)-H+ exchanger in CRF is variable, and both increased and reduced activity have been reported. The mechanisms through which CRF may exert an effect on the Na(+)-H+ transport are not known. Data exist indicating that PTH inhibits the Na(+)-H+ exchange in kidney and liver, and this action of hormone is most likely due to its ability to raise cytosolic calcium ([Ca2+]i). Therefore, it is possible that excess PTH in CRF may adversely affect the activity

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41

Mackovic-Basic, M., R. Fan, and I. Kurtz. "Denervation inhibits early increase in Na(+)-H+ exchange after uninephrectomy but does not suppress hypertrophy." American Journal of Physiology-Renal Physiology 263, no. 2 (1992): F328—F334. http://dx.doi.org/10.1152/ajprenal.1992.263.2.f328.

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Na(+)-H+ exchange in the rat proximal tubule luminal membrane increases approximately 30% within 15 min after the contralateral uninephrectomy. The present study was designed to test whether altered renal sympathetic nerve outflow to the remaining kidney is the underlying mechanism of increased antiport activity and whether suppression of Na(+)-H+ antiport activity by renal denervation inhibits renal hypertrophy in the remaining kidney after uninephrectomy. Sprague-Dawley rats were divided into four groups: 1) sham operated, 2) uninephrectomized, 3) uninephrectomized with prior denervation of

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42

Hoffmann, G., Y. Ko, A. Sachinidis, et al. "Kinetics of Na+/H+ exchange in vascular smooth muscle cells from WKY and SHR: effects of phorbol ester." American Journal of Physiology-Cell Physiology 268, no. 1 (1995): C14—C20. http://dx.doi.org/10.1152/ajpcell.1995.268.1.c14.

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The kinetic properties of Na+/H+ exchange were investigated in vascular smooth muscle cells (VSMC) in culture from normotensive Wistar-Kyoto (WKY) and spontaneously hypertensive rats (SHR). Antiport activity was measured in 2',7'-bis(carboxyethyl)-5(6)-carboxyfluorescein-loaded cells after nigericin-induced cytosolic acidification. Studies were performed without (control) and with pretreatment of the cells with phorbol 12-myristate 13-acetate (PMA; 200 nM). Na+/H+ exchange markedly differed between the two strains with lower Hill coefficients [1.56 +/- 0.17 (SE) vs. 2.62 +/- 0.36] and higher m

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43

Ullmann, Roland, Roland Gross, Jörg Simon, Gottfried Unden, and Achim Kröger. "Transport of C4-Dicarboxylates inWolinella succinogenes." Journal of Bacteriology 182, no. 20 (2000): 5757–64. http://dx.doi.org/10.1128/jb.182.20.5757-5764.2000.

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ABSTRACT C4-dicarboxylate transport is a prerequisite for anaerobic respiration with fumarate in Wolinella succinogenes, since the substrate site of fumarate reductase is oriented towards the cytoplasmic side of the membrane. W. succinogenes was found to transport C4-dicarboxylates (fumarate, succinate, malate, and aspartate) across the cytoplasmic membrane by antiport and uniport mechanisms. The electrogenic uniport resulted in dicarboxylate accumulation driven by anaerobic respiration. The molar ratio of internal to external dicarboxylate concentration was up to 103. The dicarboxylate antipo

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44

Baysal, K., D. W. Jung, K. K. Gunter, T. E. Gunter, and G. P. Brierley. "Na(+)-dependent Ca2+ efflux mechanism of heart mitochondria is not a passive Ca2+/2Na+ exchanger." American Journal of Physiology-Cell Physiology 266, no. 3 (1994): C800—C808. http://dx.doi.org/10.1152/ajpcell.1994.266.3.c800.

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Net Ca2+ flux across the inner membrane of respiring heart mitochondria was evaluated under conditions in which virtually all Ca2+ movement can be attributed to the Na+/Ca2+ antiport. If this antiport promotes a passive electroneutral exchange of Ca2+ for 2Na+, the Ca2+ gradient should be equal to the square of the Na+ gradient at equilibrium. Because the mitochondrial Na+/H+ antiport equilibrates the Na+ and H+ gradients, the Ca2+ gradient should also equal the square of the H+ gradient. In a series of > 20 determinations at different matrix [Ca2+], different delta pH, and varying membrane

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Zhang, Siyun, Ming Cheng, Manivannan Kalavathi Dhinakaran, Yue Sun, and Haibing Li. "Enantioselective Antiport in Asymmetric Nanochannels." ACS Nano 15, no. 8 (2021): 13148–54. http://dx.doi.org/10.1021/acsnano.1c02630.

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46

Poolman, B. "Precursor/product antiport in bacteria." Molecular Microbiology 4, no. 10 (1990): 1629–36. http://dx.doi.org/10.1111/j.1365-2958.1990.tb00539.x.

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Brierley, Gerald P., and Dennis W. Jung. "K+/H+ antiport in mitochondria." Journal of Bioenergetics and Biomembranes 20, no. 2 (1988): 193–209. http://dx.doi.org/10.1007/bf00768394.

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Frisco, Pierluigi. "P systems with symport-antiport." Scholarpedia 6, no. 10 (2011): 11704. http://dx.doi.org/10.4249/scholarpedia.11704.

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Grinstein, S., and H. Wieczorek. "Cation antiports of animal plasma membranes." Journal of Experimental Biology 196, no. 1 (1994): 307–18. http://dx.doi.org/10.1242/jeb.196.1.307.

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Rosengren, S., P. M. Henson, and G. S. Worthen. "Migration-associated volume changes in neutrophils facilitate the migratory process in vitro." American Journal of Physiology-Cell Physiology 267, no. 6 (1994): C1623—C1632. http://dx.doi.org/10.1152/ajpcell.1994.267.6.c1623.

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Neutrophil granulocytes, while migrating, undergo substantial shape changes from the round, resting state to a polarized phenotype. In the present study, we monitored cell volume changes in neutrophils migrating toward the chemotactic agent N-formyl-methionyl-leucyl-phenylalanine (FMLP) in collagen gels. Neutrophil volume was measured through optical sectioning on a confocal microscope and three-dimensional reconstruction. This method correlated well with Coulter counter volume measurements. Migrating neutrophils displayed a significant volume increase of 35-60%. The cell swelling appeared to

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