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Journal articles on the topic '(Na+,K+)-dependent ATPase'

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Published: 4 June 2021

Last updated: 20 February 2023

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1

Aizman, R. I., G. Celsi, L. Grahnquist, Z. M. Wang, Y. Finkel, and A. Aperia. "Ontogeny of K+ transport in rat distal colon." American Journal of Physiology-Gastrointestinal and Liver Physiology 271, no. 2 (August 1, 1996): G268—G274. http://dx.doi.org/10.1152/ajpgi.1996.271.2.g268.

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Infants need to retain more K+ than adults to avoid growth retardation. Since the K+ requirements are different in infants (I) and in adults (A), the mechanisms regulating K+ homeostasis should also be different. The colon plays an important role for the regulation of K+ homeostasis. Colonic K+ transport is bidirectional. In this study we have examined the development of colonic K+ transport with special reference to the contribution of different K(+)-transporting pathways. The net colonic K+ uptake, as determined by in vivo perfusion studies and by 86Rb uptake, was significantly higher in I t

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2

Benders, A. A., J. A. Timmermans, A. Oosterhof, H. J. Ter Laak, T. H. M. S. M. van Kuppevelt, R. A. Wevers, and J. H. Veerkamp. "Deficiency of Na+/K+-ATPase and sarcoplasmic reticulum Ca2+-ATPase in skeletal muscle and cultured muscle cells of myotonic dystrophy patients." Biochemical Journal 293, no. 1 (July 1, 1993): 269–74. http://dx.doi.org/10.1042/bj2930269.

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Since defective regulation of ion transport could initiate or contribute to the abnormal cellular function in myotonic dystrophy (MyD), Na+/K(+)-ATPase and sarcoplasmic reticulum (SR) Ca(2+)-ATPase were examined in skeletal muscle and cultured skeletal muscle cells of controls and MyD patients. Na+/K(+)-ATPase was investigated by measuring ouabain binding and the activities of Na+/K(+)-ATPase and K(+)-dependent 3-O-methylfluorescein phosphate (3-O-MFPase). SR Ca(2+)-ATPase was analysed by e.l.i.s.a., Ca(2+)-dependent phosphorylation and its activities with ATP and 3-O-methylfluorescein phospha

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3

Mathews, P. M., D. Claeys, F. Jaisser, K. Geering, J. D. Horisberger, J. P. Kraehenbuhl, and B. C. Rossier. "Primary structure and functional expression of the mouse and frog alpha-subunit of the gastric H(+)-K(+)-ATPase." American Journal of Physiology-Cell Physiology 268, no. 5 (May 1, 1995): C1207—C1214. http://dx.doi.org/10.1152/ajpcell.1995.268.5.c1207.

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The H(+)-K(+)-ATPase of the gastric parietal cells is responsible for the acidification of the stomach lumen. This heterodimeric protein belongs to the family of cation-translocating P-type ATPases, which includes the closely related Na(+)-ATPase. We have cloned the alpha-subunit cDNA of the Xenopus and murine gastric H(+)-K(+)-ATPase (alpha H-K). We have expressed Xenopus and murine alpha H-K along with the previously cloned gastric H(+)-K(+)-ATPase beta-subunit of rabbit (beta H-K) in Xenopus oocytes by cRNA injection. An antibody directed against the beta H-K coimmunoprecipitates under nond

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4

Missiaen, L., F. Wuytack, H. De Smedt, M. Vrolix, and R. Casteels. "AlF4- reversibly inhibits ‘P’-type cation-transport ATPases, possibly by interacting with the phosphate-binding site of the ATPase." Biochemical Journal 253, no. 3 (August 1, 1988): 827–33. http://dx.doi.org/10.1042/bj2530827.

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The only known cellular action of AlF4- is to stimulate the G-proteins. The aim of the present work is to demonstrate that AlF4- also inhibits ‘P’-type cation-transport ATPases. NaF plus AlCl3 completely and reversibly inhibits the activity of the purified (Na+ + K+)-ATPase (Na+- and K+-activated ATPase) and of the purified plasmalemmal (Ca2+ + Mg2+)-ATPase (Ca2+-stimulated and Mg2+-dependent ATPase). It partially inhibits the activity of the sarcoplasmic-reticulum (Ca2+ + Mg2+)-ATPase, whereas it does not affect the mitochondrial H+-transporting ATPase. The inhibitory substances are neither F

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5

Asano, Shinji, Satomi Hoshina, Yumi Nakaie, Toshiyuki Watanabe, Michihiko Sato, Yuichi Suzuki, and Noriaki Takeguchi. "Functional expression of putative H+-K+-ATPase from guinea pig distal colon." American Journal of Physiology-Cell Physiology 275, no. 3 (September 1, 1998): C669—C674. http://dx.doi.org/10.1152/ajpcell.1998.275.3.c669.

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A guinea pig cDNA encoding the putative colonic H+-K+-ATPase α-subunit (T. Watanabe, M. Sato, K. Kaneko, T. Suzuki, T. Yoshida, and Y. Suzuki; GenBank accession no. D21854 ) was functionally expressed in HEK-293, a human kidney cell line. The cDNA for the putative colonic H+-K+-ATPase was cotransfected with cDNA for either rabbit gastric H+-K+-ATPase or TorpedoNa+-K+-ATPase β-subunit. In both expressions, Na+-independent, K+-dependent ATPase (K+-ATPase) activity was detected in the membrane fraction of the cells, with a Michaelis-Menten constant for K+ of 0.68 mM. The expressed K+-ATPase activ

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6

Kraut, J. A., F. Starr, G. Sachs, and M. Reuben. "Expression of gastric and colonic H(+)-K(+)-ATPase in the rat kidney." American Journal of Physiology-Renal Physiology 268, no. 4 (April 1, 1995): F581—F587. http://dx.doi.org/10.1152/ajprenal.1995.268.4.f581.

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Enzymatic and microperfusion studies have indicated that an ATP-dependent H+/K+ exchange process is present in the collecting duct of the mammalian kidney. Immunochemical staining has also provided evidence for expression of a gastric-type H(+)-K+ adenosine triphosphatase (H(+)-K(+)-ATPase). Rat kidney mRNA was probed with use of the polymerase chain reaction (PCR) to determine the presence of an H(+)-K(+)-ATPase. cDNA made with mRNA isolated from the kidneys of rats maintained on a low-K diet was used as template in PCR reactions with primers encompassing the cDNA sequence of the alpha-subuni

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7

Crambert, Gilles, Ciming Li, Dirk Claeys, and Käthi Geering. "FXYD3 (Mat-8), a New Regulator of Na,K-ATPase." Molecular Biology of the Cell 16, no. 5 (May 2005): 2363–71. http://dx.doi.org/10.1091/mbc.e04-10-0878.

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Four of the seven members of the FXYD protein family have been identified as specific regulators of Na,K-ATPase. In this study, we show that FXYD3, also known as Mat-8, is able to associate with and to modify the transport properties of Na,K-ATPase. In addition to this shared function, FXYD3 displays some uncommon characteristics. First, in contrast to other FXYD proteins, which were shown to be type I membrane proteins, FXYD3 may have a second transmembrane-like domain because of the presence of a noncleavable signal peptide. Second, FXYD3 can associate with Na,K- as well as H,K-ATPases when

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8

Ono, S., J. Guntupalli, and T. D. DuBose. "Role of H(+)-K(+)-ATPase in pHi regulation in inner medullary collecting duct cells in culture." American Journal of Physiology-Renal Physiology 270, no. 5 (May 1, 1996): F852—F861. http://dx.doi.org/10.1152/ajprenal.1996.270.5.f852.

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Studies in inner medullary collecting duct (IMCD) cells in primary culture have proposed two mechanisms for Na(+)-independent hydrogen ion transport: an H(+)-adenosinetriphosphatase (H(+)-ATPase) and an H(+)-K(+)-ATPase. In the present study, we have employed two sources of IMCD cells, cells in primary culture derived from the terminal papilla of the Munich-Wistar rat (IMCDp) and an established murine cell line (mIMCD-3), to define the predominant mechanism(s) of Na(+)-independent intracellular pH (pHi) recovery in the IMCD. In confluent monolayers of IMCDp and mIMCD-3 cells, pHi was measured

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9

Vujisic, Ljubica, Danijela Krstic, and Jovan Vucetic. "Chemical aspect of the influence of cobalt ions on atpase activity." Journal of the Serbian Chemical Society 65, no. 7 (2000): 507–15. http://dx.doi.org/10.2298/jsc0007507v.

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The influence of Co 2+ ions on the activities of Na+/K+-ATPase and Mg2+ -ATPase, enzymes from rat brain synaptic plasma membrane, was studied. The aim of this study was to investigate the inhibition of both ATPases activities byexposure tocobalt ions as a function of experimentally added CoSO4. The "free" Co2+ concentrations in the reaction mixturewere also calculated and discussed. CoSO4 induced a dose-dependent inhibition of both enzymes. The IC50 values of Co 2+, as calculated from the experimental curves, were 168 mM for Na+/K+-ATPase and 262 mMfor Mg 2+-ATPase, and for the recalculated fr

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10

Reinhardt, J., M. Kosch, M. Lerner, H. Bertram, D. Lemke, and H. Oberleithner. "Stimulation of protein kinase C pathway mediates endocytosis of human nongastric H+-K+-ATPase, ATP1AL1." American Journal of Physiology-Renal Physiology 283, no. 2 (August 1, 2002): F335—F343. http://dx.doi.org/10.1152/ajprenal.00226.2001.

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The human nongastric H+-K+-ATPase, ATP1AL1, shown to reabsorb K+ in exchange for H+ or Na+, is localized in the luminal plasma membrane of renal epithelial cells. It is presumed that renal H+-K+-ATPases can be regulated by endocytosis. However, little is known about the molecular mechanisms that control plasma membrane expression of renal H+-K+-ATPases. In our study, activation of protein kinase C (PKC) using phorbol esters (phorbol 12-myristate 13-acetate) leads to clathrin-dependent internalization and intracellular accumulation of the ion pump in stably transfected Madin-Darby canine kidney

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11

Crambert, Gilles, Jean-Daniel Horisberger, Nikolai N. Modyanov та Käthi Geering. "Human nongastric H+-K+-ATPase: transport properties of ATP1al1 assembled with different β-subunits". American Journal of Physiology-Cell Physiology 283, № 1 (1 липня 2002): C305—C314. http://dx.doi.org/10.1152/ajpcell.00590.2001.

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To investigate whether nongastric H+-K+-ATPases transport Na+ in exchange for K+ and whether different β-isoforms influence their transport properties, we compared the functional properties of the catalytic subunit of human nongastric H+-K+-ATPase, ATP1al1 (AL1), and of the Na+-K+-ATPase α1-subunit (α1) expressed in Xenopus oocytes, with different β-subunits. Our results show that βHK and β1-NK can produce functional AL1/β complexes at the oocyte cell surface that, in contrast to α1/β1 NK and α1/βHK complexes, exhibit a similar apparent K+ affinity. Similar to Na+-K+-ATPase, AL1/β complexes ar

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12

McBride, B. W., and L. P. Milligan. "Influence of feed intake and starvation on the magnitude of Na+,K+-ATPase(EC 3.6.1.3)-dependent respiration in duodenal mucosa of sheep." British Journal of Nutrition 53, no. 3 (May 1985): 605–14. http://dx.doi.org/10.1079/bjn19850070.

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1. Oxygen consumption and Na+,K+-ATPase(EC 3.6.1.3)-dependent (ouabain-sensitive) and -independent respiration were measured for duodenal mucosa biopsies from 10-month-old sheep given two levels of digestible energy (DE) intake (7.6–7.7 and 14.8 MJ lucerne (Medicago sativa) pellets/d) and following 48 h of starvation.2. The mucosal biopsies were determined to be structurally intact and free of adherent bacteria on histological and scanning-electron-microscope examinations.3. The use of D-glucose as a substrate during incubations did not elevate (P > 0.05) the respiration indices of the biop

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13

Sabolic, I., D. Brown, J. M. Verbavatz, and J. Kleinman. "H(+)-ATPases of renal cortical and medullary endosomes are differentially sensitive to Sch-28080 and omeprazole." American Journal of Physiology-Renal Physiology 266, no. 6 (June 1, 1994): F868—F877. http://dx.doi.org/10.1152/ajprenal.1994.266.6.f868.

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Adenosinetriphosphatase (ATPase) activity stimulated by K+ and inhibited by Sch-28080 (SCH), omeprazole (OME), and vanadate has been measured in microsomes from mammalian renal medulla and attributed to a kidney isoform of the H(+)-K(+)-ATPase. To determine whether the H(+)-K(+)-ATPase inhibitors could also inhibit the vacuolar (V)-type H(+)-adenosinetriphosphatase (H(+)-ATPase, i.e., H+ pump) in mammalian intracellular vesicles, we examined their effects on bafilomycin-sensitive acidification in renal cortical vesicles (CEV) and medullary endocytic vesicles (MEV). Rats were injected with fluo

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14

Modyanov, N. N., P. M. Mathews, A. V. Grishin, P. Beguin, A. T. Beggah, B. C. Rossier, J. D. Horisberger, and K. Geering. "Human ATP1AL1 gene encodes a ouabain-sensitive H-K-ATPase." American Journal of Physiology-Cell Physiology 269, no. 4 (October 1, 1995): C992—C997. http://dx.doi.org/10.1152/ajpcell.1995.269.4.c992.

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The cDNA for ATP1AL1, the fifth member of the human Na-K-adenosinetriphosphatase (ATPase)/H-K-ATPase gene family, was recently cloned (A. V. Grishin, V. E. Sverdlov, M. B. Kostina, and N. N. Modyanov. FEBS Lett. 349: 144-150, 1994). The encoded protein (ATP1AL1) has all the primary structural features common to the catalytic alpha-subunit of ion-transporting P-type ATPases and is similar (63-64% identity) to the Na-K-ATPase alpha-subunit isoforms and the gastric H-K-ATPase alpha-subunit. In this study, ATP1AL1 was expressed in Xenopus laevis oocytes in combination with the beta-subunit of rabb

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15

Feraille, E., M. L. Carranza, B. Buffin-Meyer, M. Rousselot, A. Doucet, and H. Favre. "Protein kinase C-dependent stimulation of Na(+)-K(+)-ATP epsilon in rat proximal convoluted tubules." American Journal of Physiology-Cell Physiology 268, no. 5 (May 1, 1995): C1277—C1283. http://dx.doi.org/10.1152/ajpcell.1995.268.5.c1277.

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In rat proximal convoluted tubule (PCT), activation of protein kinase C (PKC) by phorbol 12,13-dibutyrate (PDBu) was previously reported to inhibit Na(+)-K(+)-ATPase, a paradoxical finding in view of the known stimulatory effect of PKC on Na+ reabsorption. Because this inhibition occurs via phospholipase A2 activation, a pathway stimulated by hypoxia, we evaluated the influence of oxygen supply on PKC action on Na(+)-K(+)-ATPase. Results confirmed that PDBu inhibited PCT Na(+)-K(+)-ATPase activity under usual conditions. In contrast, when oxygen supply was increased, PDBu had no effect on Na(+

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16

Haley, C., and M. Donnell. "K+ reabsorption by the lower Malpighian tubule of Rhodnius prolixus: inhibition by Ba2+ and blockers of H+/K+-ATPases." Journal of Experimental Biology 200, no. 1 (January 1, 1997): 139–47. http://dx.doi.org/10.1242/jeb.200.1.139.

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Active K+ reabsorption by the lower Malpighian tubule of the blood-feeding hemipteran Rhodnius prolixus does not involve the amiloride-sensitive K+/H+ exchangers or V-type H+-ATPases implicated in secretion of ions from haemolymph to lumen in the upper tubule. Amiloride, N-ethylmaleimide, 4-chloro-7-nitrobenzo-2-oxa-1,3-diazol and bafilomycin A1 inhibit haemolymph-to-lumen secretion of Na+ and K+ by the upper Malpighian tubule, but have little or no effect on lumen-to-haemolymph reabsorption of K+ by the lower tubule. The effects of inhibitors of H+/K+-ATPases, including omeprazole and SCH 280

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17

Rajendran, Vazhaikkurichi M., Satish K. Singh, John Geibel, and Henry J. Binder. "Differential localization of colonic H+-K+-ATPase isoforms in surface and crypt cells." American Journal of Physiology-Gastrointestinal and Liver Physiology 274, no. 2 (February 1, 1998): G424—G429. http://dx.doi.org/10.1152/ajpgi.1998.274.2.g424.

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Two distinct colonic H+-K+-adenosinetriphosphatase (H+-K+-ATPase) isoforms can be identified in part on the basis of their sensitivity to ouabain. The colonic H+-K+-ATPase α-subunit (HKcα) was recently cloned, and its message and protein are present in surface (and the upper 20% of crypt) cells in the rat distal colon. These studies were performed to establish the spatial distribution of the ouabain-sensitive and ouabain-insensitive components of both H+-K+-ATPase activity in apical membranes prepared from surface and crypt cells and K+-dependent intracellular pH (pHi) recovery from an acid lo

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18

Van der Hijden, H. T. W. M., S. Kramer-Schmitt, E. Grell, and J. J. H. H. M. de Pont. "The basal Mg2+-dependent ATPase activity is not part of the (H++K+)-transporting ATPase reaction cycle." Biochemical Journal 267, no. 3 (May 1, 1990): 565–72. http://dx.doi.org/10.1042/bj2670565.

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Purified gastric (H(+)+K+)-transporting ATPase [(H(+)+K+)-ATPase] from the parietal cells always contains a certain amount of basal Mg2(+)-dependent ATPase (Mg2(+)-ATPase) activity. lin-Benzo-ATP (the prefix lin refers to the linear disposition of the pyrimidine, benzene and imidazole rings in the ‘stretched-out’ version of the adenine nucleus), an ATP analogue with a benzene ring formally inserted between the two rings composing the adenosine moiety, is an interesting substrate not only because of its fluorescent behaviour, but also because of its geometric properties. lin-Benzo-ATP was used

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19

Marciniak, Andrzej, Anna Jamroz-Wiśniewska, Ewelina Borkowska, and Jerzy Bełtowski. "Time-dependent effect of leptin on renal Na+,K+-ATPase activity." Acta Biochimica Polonica 52, no. 4 (August 4, 2005): 803–10. http://dx.doi.org/10.18388/abp.2005_3392.

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Leptin, secreted by adipose tissue, is involved in the pathogenesis of arterial hypertension, however, the mechanisms through which leptin increases blood pressure are incompletely elucidated. We investigated the effect of leptin, administered for different time periods, on renal Na(+),K(+)-ATPase activity in the rat. Leptin was infused under anesthesia into the abdominal aorta proximally to the renal arteries for 0.5-3 h. Leptin administered at doses of 1 and 10 microg/min per kg for 30 min decreased the Na(+),K(+)-ATPase activity in the renal medulla. This effect disappeared when the hormone

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20

Lei, Jianxun, Cary N. Mariash, Maneesh Bhargava, Elizabeth V. Wattenberg, and David H. Ingbar. "T3 increases Na-K-ATPase activity via a MAPK/ERK1/2-dependent pathway in rat adult alveolar epithelial cells." American Journal of Physiology-Lung Cellular and Molecular Physiology 294, no. 4 (April 2008): L749—L754. http://dx.doi.org/10.1152/ajplung.00335.2007.

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Thyroid hormone (T3) increases Na-K-ATPase activity in rat adult alveolar type II cells via a PI3K-dependent pathway. In these cells, dopamine and β-adrenergic agonists can stimulate Na-K-ATPase activity through either PI3K or MAPK pathways. We assessed the role of the MAPK pathway in the stimulation of Na-K-ATPase by T3. In the adult rat alveolar type II-like cell line MP48, T3 enhanced MAPK/ERK1/2 activity in a dose-dependent manner. Increased ERK1/2 phosphorylation was observed within 5 min, peaked at 20 min, and then decreased. Two MEK1/2 inhibitors, U0126 and PD-98059, each abolished the

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21

Carranza, M. L., E. Feraille, and H. Favre. "Protein kinase C-dependent phosphorylation of Na(+)-K(+)-ATPase alpha-subunit in rat kidney cortical tubules." American Journal of Physiology-Cell Physiology 271, no. 1 (July 1, 1996): C136—C143. http://dx.doi.org/10.1152/ajpcell.1996.271.1.c136.

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We have previously shown that, in oxygenated rat kidney proximal convoluted tubules (PCT), activation of protein kinase C (PKC) by phorbol 12,13-dibutyrate (PDBu) directly stimulates Na(+)-K(+)-adenosinetriphosphatase (ATPase) activity. PKC modulation of Na(+)-K(+)-ATPase activity by phosphorylation of its alpha-subunit was the postulated mechanism. The present study was therefore designed to investigate the relationship between PKC-mediated phosphorylation of the catalytic alpha-subunit and the cation transport activity of the Na(+)-K(+)-ATPase. In a suspension of rat kidney cortical tubules,

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22

Casare, Fernando, Daiane Milan, and Ricardo Fernandez. "Stimulation of calcium-sensing receptor increases biochemical H+-ATPase activity in mouse cortex and outer medullary regions." Canadian Journal of Physiology and Pharmacology 92, no. 3 (March 2014): 181–88. http://dx.doi.org/10.1139/cjpp-2013-0256.

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The aim of this project was to investigate the interaction between the calcium-sensing receptor (CaSR) and proton extrusion by the V-ATPase and gastric-like isoform of the H+/K+-ATPase in the mouse nephron. Biochemical activity of H+- ATPases was analysed using a partially purified membrane fraction of mouse cortex and outer medullary region. The V-ATPase activity (sensitive to 10−7 mol·L−1 bafilomycin) from the cortical and outer medullary region was significantly stimulated by increasing the [Formula: see text] (outside Ca2+), in a dose-dependent pattern. Gastric H+/K+-ATPase activity (sensi

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23

Urushidani, T., and J. G. Forte. "Stimulation-associated redistribution of H+-K+-ATPase activity in isolated gastric glands." American Journal of Physiology-Gastrointestinal and Liver Physiology 252, no. 4 (April 1, 1987): G458—G465. http://dx.doi.org/10.1152/ajpgi.1987.252.4.g458.

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The objective of this work is to establish a procedure to study the stimulation-dependent membrane redistribution and properties of H+-K+-ATPase in an in vitro model system, rabbit isolated gastric glands. Stimulated (10(-4) M histamine plus 10(-5) M forskolin) and resting (10(-4) M metiamide) glands were homogenized and fractionated into PO (40 g, 5 min), P1 (400 g, 10 min), P2 (14,500 g, 10 min), P3 (48,200 g, 90 min), and supernatant, S3. Significant changes occurred in the distribution of our marker for H+-K+-ATPase (K+-p-nitrophenyl phosphatase) activity: a reduction in activity of P3 and

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Alves, Daiane S., Glen A. Farr, Patricia Seo-Mayer, and Michael J. Caplan. "AS160 Associates with the Na+,K+-ATPase and Mediates the Adenosine Monophosphate-stimulated Protein Kinase-dependent Regulation of Sodium Pump Surface Expression." Molecular Biology of the Cell 21, no. 24 (December 15, 2010): 4400–4408. http://dx.doi.org/10.1091/mbc.e10-06-0507.

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The Na+,K+-ATPase is the major active transport protein found in the plasma membranes of most epithelial cell types. The regulation of Na+,K+-ATPase activity involves a variety of mechanisms, including regulated endocytosis and recycling. Our efforts to identify novel Na+,K+-ATPase binding partners revealed a direct association between the Na+,K+-ATPase and AS160, a Rab-GTPase-activating protein. In COS cells, coexpression of AS160 and Na+,K+-ATPase led to the intracellular retention of the sodium pump. We find that AS160 interacts with the large cytoplasmic NP domain of the α-subunit of the N

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Anner, B. M., M. Moosmayer, and E. Imesch. "Mercury blocks Na-K-ATPase by a ligand-dependent and reversible mechanism." American Journal of Physiology-Renal Physiology 262, no. 5 (May 1, 1992): F830—F836. http://dx.doi.org/10.1152/ajprenal.1992.262.5.f830.

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An inhibitory receptor for cardioactive steroids such as digoxin and ouabain is located at the extracellular surface of the Na-K-adenosinetriphosphatase (ATPase) molecule. Besides cardioactive steroids, mercury is a potent inhibitor of the Na-K-ATPase activity. The half-maximal inhibitory concentration (IC50), determined within 30 min at 37 degrees C at 1 microgram protein/ml, was 200 nM, despite the presence of 1 mM EDTA; the IC50 decreased with increasing protein/inhibitor ratio, and it reached 2.7 microM at 0.1 mg protein/ml and 20 microM at 1 mg protein/ml. The IC50 for Na-K-ATPase inhibit

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26

Khundmiri, Syed J., Mohammed Ameen, Nicholas A. Delamere, and Eleanor D. Lederer. "PTH-mediated regulation of Na+-K+-ATPase requires Src kinase-dependent ERK phosphorylation." American Journal of Physiology-Renal Physiology 295, no. 2 (August 2008): F426—F437. http://dx.doi.org/10.1152/ajprenal.00516.2007.

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Parathyroid hormone (PTH) inhibits Na+-K+-ATPase activity by serine phosphorylation of the α1-subunit through ERK-dependent phosphorylation and translocation of protein kinase Cα (PKCα). On the basis of previous studies, we postulated that PTH regulates sodium pump activity through Src kinase, PLC, and calcium-dependent ERK phosphorylation. In the present work utilizing opossum kidney cells, a model of renal proximal tubule, PTH-stimulated ERK phosphorylation and membrane translocation of PKCα were prevented by inhibition of Src kinase, PLC, and calcium entry. Pharmacological inhibition of PLA

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27

Holthouser, Kristine A., Amritlal Mandal, Michael L. Merchant, Jeffrey R. Schelling, Nicholas A. Delamere, Ronald R. Valdes, Suresh C. Tyagi, Eleanor D. Lederer, and Syed J. Khundmiri. "Ouabain stimulates Na-K-ATPase through a sodium/hydrogen exchanger-1 (NHE-1)-dependent mechanism in human kidney proximal tubule cells." American Journal of Physiology-Renal Physiology 299, no. 1 (July 2010): F77—F90. http://dx.doi.org/10.1152/ajprenal.00581.2009.

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Recent investigations demonstrate increased Na/H exchanger-1 (NHE-1) activity and plasma levels of ouabain-like factor in spontaneously hypertensive rats. At nanomolar concentrations, ouabain increases Na-K-ATPase activity, induces cell proliferation, and activates complex signaling cascades. We hypothesize that the activity of NHE-1 and Na-K-ATPase are interdependent. To test whether treatment with picomolar ouabain regulates Na-K-ATPase through an NHE-1-dependent mechanism, we examined the role of NHE-1 in ouabain-mediated stimulation of Na-K-ATPase in kidney proximal tubule cell lines [opos

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Akopova, O. V., O. N. Kharlamova, A. V. Kotsiuruba, Yu P. Korkach, and V. F. Sagach. "THE STUDY OF NITRIC OXIDE ACTION IN VIVO ON NA+ , K+ -ÀÒPASE IN RAT AORTA." Fiziolohichnyĭ zhurnal 55, no. 1 (February 4, 2009): 27–35. http://dx.doi.org/10.15407/fz55.01.027.

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The influence of nitric oxide on Na+,K+-ATPase activity in rat aorta was studied by means of stimulation of endogenous NO synthesis after injections of bacterial lipopolysaccharide (LPS) and pharmacological NO donor nitroglycerine (NG). It was shown that NO action on Na+,K+-ATPase in vivo is dose-dependent. Stimulation of the endogenous NO synthesis by LPS as well as the administration of low doses of NG lead to the activation of Na+,K+-ATPase and favor the conclusion that NO-dependent Na+,K+-ATPase stimulation mediates vasodilatory and hypotensive action of nitric oxide. The Na+,K+-ATPase ac

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29

Klein, U. "THE INSECT V-ATPase, A PLASMA MEMBRANE PROTON PUMP ENERGIZING SECONDARY ACTIVE TRANSPORT: IMMUNOLOGICAL EVIDENCE FOR THE OCCURRENCE OF A V-ATPase IN INSECT ION-TRANSPORTING EPITHELIA." Journal of Experimental Biology 172, no. 1 (November 1, 1992): 345–54. http://dx.doi.org/10.1242/jeb.172.1.345.

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Active electrogenic K+ transport in insects serves as the energy source for secretion or absorption in gastrointestinal epithelia or for the receptor current in sensory epithelia. In the larval midgut of the tobacco hornworm Manduca sexta, a vacuolar-type proton pump (V-ATPase) and a K+/nH+ antiport represent the functional elements of the potassium pump. Several immunological findings support the hypothesis that active K+ transport in other insect epithelia may also be energized by a V-ATPase. In immunoblots, crude homogenates of sensilla-rich antennae and Malpighian tubules of M. sexta cross

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30

Michea, Luis, Verónica Irribarra, I. Annelise Goecke, and Elisa T. Marusic. "Reduced Na-K pump but increased Na-K-2Cl cotransporter in aorta of streptozotocin-induced diabetic rat." American Journal of Physiology-Heart and Circulatory Physiology 280, no. 2 (February 1, 2001): H851—H858. http://dx.doi.org/10.1152/ajpheart.2001.280.2.h851.

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The activities of Na-K-ATPase and Na-K-2Cl cotransporter (NKCC1) were studied in the aorta, heart, and skeletal muscle of streptozotocin (STZ)-induced diabetic rats and control rats. In the aortic rings of STZ rats, the Na-K-ATPase-dependent 86Rb/K uptake was reduced to 60.0 ± 5.5% of the control value ( P < 0.01). However, Na-K-ATPase activity in soleus skeletal muscle fibers of STZ rats and paired control rats was similar, showing that the reduction of Na-K-ATPase activity in aortas of STZ rats is tissue specific. To functionally distinguish the contributions of ouabain-resistant (α1) and

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31

Bertorello, A., and A. Aperia. "Regulation of Na+-K+-ATPase activity in kidney proximal tubules: involvement of GTP binding proteins." American Journal of Physiology-Renal Physiology 256, no. 1 (January 1, 1989): F57—F62. http://dx.doi.org/10.1152/ajprenal.1989.256.1.f57.

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This study evaluates the involvement of GTP-dependent regulatory proteins (G-proteins) in the regulation of Na+-K+-ATPase activity in proximal convoluted tubule (PCT) segments. Single PCT segments were dissected from rat kidney and permeabilized to allow nucleotides and medium free access to the interior of the cell. A GDP analogue that blocks GTP-dependent activation of the G-protein, GDP beta S (400 microM) significantly inhibited PCT Na+-K+-ATPase activity when Na in the medium (Nam) was greater than or equal to 70 mM. The inhibition was attenuated when Nam was 55 and 35 mM and was no longe

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32

Dong, J., N. A. Delamere, and M. Coca-Prados. "Inhibition of Na(+)-K(+)-ATPase activates Na(+)-K(+)-2Cl- cotransporter activity in cultured ciliary epithelium." American Journal of Physiology-Cell Physiology 266, no. 1 (January 1, 1994): C198—C205. http://dx.doi.org/10.1152/ajpcell.1994.266.1.c198.

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Inhibition of Na(+)-K(+)-ATPase activates Na(+)-K(+)-2Cl- cotransporter activity in cultured ciliary epithelium. Am. J. Physiol. 266 (Cell Physiol. 35): C198-C205, 1994.--86Rb uptake experiments were conducted to measure Na(+)-K(+)-ATPase activity and Na(+)-K(+)-2Cl- cotransporter activity in a cell line derived from rabbit nonpigmented ciliary epithelium. The presence of a Na(+)-K(+)-2Cl- cotransporter was supported by the observation of a bumetanide-sensitive 86Rb uptake component that was dependent on the extracellular concentration of both sodium and chloride. Potassium influx mediated by

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33

Koenderink, Jan B., Herman G. P. Swarts, H. Christiaan Stronks, Harm P. H. Hermsen, Peter H. G. M. Willems, and Jan Joep H. H. M. De Pont. "Chimeras of X+,K+-ATPases." Journal of Biological Chemistry 276, no. 15 (January 16, 2001): 11705–11. http://dx.doi.org/10.1074/jbc.m010804200.

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In this study we reveal regions of Na+,K+-ATPase and H+,K+-ATPase that are involved in cation selectivity. A chimeric enzyme in which transmembrane hairpin M5-M6 of H+,K+-ATPase was replaced by that of Na+,K+-ATPase was phosphorylated in the absence of Na+and showed no K+-dependent reactions. Next, the part originating from Na+,K+-ATPase was gradually increased in the N-terminal direction. We demonstrate that chimera HN16, containing the transmembrane segments one to six and intermediate loops of Na+,K+-ATPase, harbors the amino acids responsible for Na+specificity. Compared with Na+,K+-ATPase

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34

Bełtowski, Jerzy, Andrzej Marciniak, Grazyna Wójcicka, and Dionizy Górny. "Regulation of renal Na(+),K(+)-ATPase and ouabain-sensitive H(+),K(+)-ATPase by the cyclic AMP-protein kinase A signal transduction pathway." Acta Biochimica Polonica 50, no. 1 (March 31, 2003): 103–14. http://dx.doi.org/10.18388/abp.2003_3717.

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We investigated the effect of the cyclic AMP-protein kinase A (PKA) signalling pathway on renal Na(+),K(+)-ATPase and ouabain-sensitive H(+),K(+)-ATPase. Male Wistar rats were anaesthetized and catheter was inserted through the femoral artery into the abdominal aorta proximally to the renal arteries for infusion of the investigated substances. Na(+),K(+)-ATPase activity was measured in the presence of Sch 28080 to block ouabain-sensitive H(+),K(+)-ATPase and improve specificity of the assay. Dibutyryl-cyclic AMP (db-cAMP) administered at a dose of 10(-7) mol/kg per min and 10(-6) mol/kg per mi

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35

Kjeldsen, K. "Complete quantification of the total concentration of rat skeletal-muscle Na+ + K+-dependent ATPase by measurements of [3H]ouabain binding." Biochemical Journal 240, no. 3 (December 15, 1986): 725–30. http://dx.doi.org/10.1042/bj2400725.

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In the standard [3H]ouabain-binding assay for quantification of the Na,K-ATPase (Na+ + K+-dependent ATPase) concentration in rat skeletal muscles, samples are incubated for 2 × 60 min in 1 microM-[3H]ouabain at 37 degrees C followed by a wash-out for 4 × 30 min at 0 degree C. To obtain accurate determinations, values determined by this standard assay should be corrected for non-specific uptake and retention of [3H]ouabain (11% overestimation), loss of specifically bound [3H]ouabain during wash-out (21% underestimation), evaporation from muscle samples during weighing (4% overestimation), impur

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36

Del Castillo, J. R., M. C. Sulbaran-Carrasco, and L. Burguillos. "K+ transport in isolated guinea pig colonocytes: evidence for Na(+)-independent ouabain-sensitive K+ pump." American Journal of Physiology-Gastrointestinal and Liver Physiology 266, no. 6 (June 1, 1994): G1083—G1089. http://dx.doi.org/10.1152/ajpgi.1994.266.6.g1083.

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K+ transport mechanisms in epithelial cells isolated from guinea pig distal colon have been studied using 86Rb as a tracer. A transport pathway has been identified that is proposed to be identical to the mechanism mediating transepithelial K+ absorption. Guinea pig colonocytes take up K+ through at least three separate mechanisms: 1) a Na(+)-dependent, ouabain-sensitive influx that is consistent with the Na(+)-K+ pump, 2) a Na(+)-dependent bumetanide-sensitive influx consistent with the Na(+)-K(+)-2Cl- cotransporter, and 3) a Na(+)-independent ouabain-sensitive influx, consistent with an apica

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Singh, H., and S. L. Linas. "Role of protein kinase C in beta 2-adrenoceptor function in cultured rat proximal tubule epithelial cells." American Journal of Physiology-Renal Physiology 273, no. 2 (August 1, 1997): F193—F199. http://dx.doi.org/10.1152/ajprenal.1997.273.2.f193.

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Renal sodium excretion is regulated by the adrenergic system. We recently demonstrated the presence of functional beta 2-adrenoceptors (beta 2-AR) in cultured rat proximal tubule epithelial cells beta 2-AR activation resulted in increases in Na-K-adenosinetriphosphatase (Na-K-ATPase) activity and transcellular sodium transport as a consequence of increased apical sodium entry. The purpose of this study was to determine the role of protein kinase C (PKC) on beta 2-AR-dependent increases in Na-K-ATPase activity and sodium transport in proximal tubules. To determine the effect of PKC on basal fun

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Tamiya, Shigeo, Mansim C. Okafor, and Nicholas A. Delamere. "Purinergic agonists stimulate lens Na-K-ATPase-mediated transport via a Src tyrosine kinase-dependent pathway." American Journal of Physiology-Cell Physiology 293, no. 2 (August 2007): C790—C796. http://dx.doi.org/10.1152/ajpcell.00579.2006.

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The Na-K-ATPase is vital for maintenance of lens transparency. Past studies using intact lens suggested the involvement of tyrosine kinases in short-term regulation of Na-K-ATPase. Furthermore, in vitro phosphorylation of a lens epithelial membrane preparation by Src family kinases (SFKs), a family of nonreceptor tyrosine kinases, resulted in modification of Na-K-ATPase activity. Here, the effect of purinergic agonists, ATP and UTP, on Na-K-ATPase function and SFK activation was examined in the rabbit lens. Na-K-ATPase function was examined using two different approaches, measurement of ouabai

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39

Zhou, Xiaoming, I. Jeanette Lynch, Shen-Ling Xia, and Charles S. Wingo. "Activation of H+-K+-ATPase by CO2 requires a basolateral Ba2+-sensitive pathway during K restriction." American Journal of Physiology-Renal Physiology 279, no. 1 (July 1, 2000): F153—F160. http://dx.doi.org/10.1152/ajprenal.2000.279.1.f153.

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We studied the activation of H+-K+-ATPase by CO2 in the renal cortical collecting duct (CCD) of K-restricted animals. Exposure of microperfused CCD to 10% CO2 increased net total CO2 flux ( J t CO2 ) from 4.9 ± 2.1 to 14.7 ± 4 pmol · mm−1· min−1 ( P < 0.05), and this effect was blocked by luminal application of the H+-K+-ATPase inhibitor Sch-28080. In the presence of luminal Ba, a K channel blocker, exposure to CO2 still stimulated J t CO2 from 6.0 ± 1.0 to 16.8 ± 2.8 pmol · mm−1 · min−1 ( P < 0.01), but peritubular application of Ba inhibited the stimulation. CO2substantially increased

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40

Juel, Carsten, Nikolai B. Nordsborg, and Jens Bangsbo. "Exercise-induced increase in maximal in vitro Na-K-ATPase activity in human skeletal muscle." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 304, no. 12 (June 15, 2013): R1161—R1165. http://dx.doi.org/10.1152/ajpregu.00591.2012.

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The present study investigated whether maximal in vitro Na-K-ATPase activity in human skeletal muscle is changed with exercise and whether it was altered by acute hypoxia. Needle biopsies from 14 subjects were obtained from vastus lateralis before and after 4 min of intense muscle activity. In addition, six subjects exercised also in hypoxia (12.5% oxygen). The Na-K-ATPase assay revealed a 19% increase ( P < 0.05) in maximal velocity ( Vmax) for Na+-dependent Na-K-ATPase activity after exercise and a tendency ( P < 0.1) toward a decrease in Km for Na+ (increased Na+ affinity) in both nor

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41

Nepal, Niraj, Subha Arthur, and Uma Sundaram. "Unique Regulation of Na-K-ATPase during Growth and Maturation of Intestinal Epithelial Cells." Cells 8, no. 6 (June 15, 2019): 593. http://dx.doi.org/10.3390/cells8060593.

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Na-K-ATPase on the basolateral membrane provides the favorable transcellular Na gradient for the proper functioning of Na-dependent nutrient co-transporters on the brush border membrane (BBM) of enterocytes. As cells mature from crypts to villus, Na-K-ATPase activity doubles, to accommodate for the increased BBM Na-dependent nutrient absorption. However, the mechanism of increased Na-K-ATPase activity during the maturation of enterocytes is not known. Therefore, this study aimed to determine the mechanisms involved in the functional transition of Na-K-ATPase during the maturation of crypts to

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42

Hayhurst, R. A., and R. G. O'Neil. "Time-dependent actions of aldosterone and amiloride on Na+-K+-ATPase of cortical collecting duct." American Journal of Physiology-Renal Physiology 254, no. 5 (May 1, 1988): F689—F696. http://dx.doi.org/10.1152/ajprenal.1988.254.5.f689.

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The actions of aldosterone on Vmax Na+-K+-ATPase activity and length of latent period were assessed for the rabbit cortical collecting duct (CCD). Initially, animals were moderately aldosterone depleted and then treated with a constant infusion of physiological doses of aldosterone. Aldosterone administration had no influence after 3 h but caused a detectable increase with 6 (borderline significance) or more hours. An apparent plateau was reached between 24 and 48 h at twice the initial activity. This aldosterone-induced stimulation could be abolished by simultaneous treatment of the animals w

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43

Mordasini, David, Mauro Bustamante, Martine Rousselot, Pierre-Yves Martin, Udo Hasler, and Eric Féraille. "Stimulation of Na+ transport by AVP is independent of PKA phosphorylation of the Na-K-ATPase in collecting duct principal cells." American Journal of Physiology-Renal Physiology 289, no. 5 (November 2005): F1031—F1039. http://dx.doi.org/10.1152/ajprenal.00128.2005.

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Arginine-vasopressin (AVP) stimulates Na+ transport and Na-K-ATPase activity via cAMP-dependent PKA activation in the renal cortical collecting duct (CCD). We investigated the role of the Na-K-ATPase in the AVP-induced stimulation of transepithelial Na+ transport using the mpkCCDc14 cell model of mammalian collecting duct principal cells. AVP (10−9 M) stimulated both the amiloride-sensitive transepithelial Na+ transport measured in intact cells and the maximal Na pump current measured by the ouabain-sensitive short-circuit current in apically permeabilized cells. These effects were associated

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Nepal, Niraj, Subha Arthur, Molly R. Butts, Soudamani Singh, Balasubramanian Palaniappan, and Uma Sundaram. "Molecular Mechanism of Stimulation of Na-K-ATPase by Leukotriene D4 in Intestinal Epithelial Cells." International Journal of Molecular Sciences 22, no. 14 (July 15, 2021): 7569. http://dx.doi.org/10.3390/ijms22147569.

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Na-K-ATPase provides a favorable transcellular Na gradient required for the functioning of Na-dependent nutrient transporters in intestinal epithelial cells. The primary metabolite for enterocytes is glutamine, which is absorbed via Na-glutamine co-transporter (SN2; SLC38A5) in intestinal crypt cells. SN2 activity is stimulated during chronic intestinal inflammation, at least in part, secondarily to the stimulation of Na-K-ATPase activity. Leukotriene D4 (LTD4) is known to be elevated in the mucosa during chronic enteritis, but the way in which it may regulate Na-K-ATPase is not known. In an i

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45

Féraille, Eric, Pascal Béguin, Maria-Luisa Carranza, Sandrine Gonin, Martine Rousselot, Pierre-Yves Martin, Hervé Favre та Käthi Geering. "Is Phosphorylation of the α1 Subunit at Ser-16 Involved in the Control of Na,K-ATPase Activity by Phorbol Ester–activated Protein Kinase C?" Molecular Biology of the Cell 11, № 1 (січень 2000): 39–50. http://dx.doi.org/10.1091/mbc.11.1.39.

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The α1 subunit of Na,K-ATPase is phosphorylated at Ser-16 by phorbol ester-sensitive protein kinase(s) C (PKC). The role of Ser-16 phosphorylation was analyzed in COS-7 cells stably expressing wild-type or mutant (T15A/S16A and S16D-E) ouabain-resistant Bufoα1 subunits. In cells incubated at 37°C, phorbol 12,13-dibutyrate (PDBu) inhibited the transport activity and decreased the cell surface expression of wild-type and mutant Na,K-pumps equally (∼20–30%). This effect of PDBu was mimicked by arachidonic acid and was dependent on PKC, phospholipase A2, and cytochrome P450-dependent monooxygenase

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46

Schmidt, T. A., S. Hasselbalch, P. A. Farrell, H. Vestergaard, and K. Kjeldsen. "Human and rodent muscle Na(+)-K(+)-ATPase in diabetes related to insulin, starvation, and training." Journal of Applied Physiology 76, no. 5 (May 1, 1994): 2140–46. http://dx.doi.org/10.1152/jappl.1994.76.5.2140.

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As determined by vanadate-facilitated [3H]ouabain binding to intact samples, semistarvation and untreated streptozotocin- or partial pancreatectomy-induced diabetes reduced rat soleus muscle Na(+)-K(+)-adenosinetriphosphatase (Na(+)-K(+)-ATPase) concentration by 12–21% (P < 0.05). Conversely, insulin treatment of rats with streptozotocin-induced diabetes induced an increase of 18-26% above control (P < 0.05). Treadmill training diminished the reduction in muscle [3H]ouabain binding site concentration induced by untreated diabetes to only 2–5%. No significant variation was observed in rat

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Tomita, K., A. Owada, Y. Iino, N. Yoshiyama, and T. Shiigai. "Effect of vasopressin on Na+-K+-ATPase activity in rat cortical collecting duct." American Journal of Physiology-Renal Physiology 253, no. 5 (November 1, 1987): F874—F879. http://dx.doi.org/10.1152/ajprenal.1987.253.5.f874.

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Vasopressin (V) causes a sustained increase in Na reabsorption and K secretion in isolated cortical collecting ducts (CCD) from rats. Because increased Na reabsorption may be associated with increased Na+-K+-ATPase activity, we investigated effects of V, given either in vivo or in vitro, on Na+-K+-ATPase activity in isolated nephron segments of rats. Na+-K+-ATPase activities were measured by coupling the hydrolysis of ATP to the production of a fluorescent nucleotide. In addition to CCD, other microdissected structures were medullary thick ascending limbs of Henle's loop, cortical thick ascend

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48

Sarkar, Pradip K., Avijit Biswas, Arun K. Ray, and Joseph V. Martin. "Mechanisms of L-Triiodothyronine-Induced Inhibition of Synaptosomal Na+-K+-ATPase Activity in Young Adult Rat Brain Cerebral Cortex." Journal of Thyroid Research 2013 (2013): 1–9. http://dx.doi.org/10.1155/2013/457953.

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The role of thyroid hormones (TH) in the normal functioning of adult mammalian brain is unclear. Our studies have identified synaptosomal Na+-K+-ATPase as a TH-responsive physiological parameter in adult rat cerebral cortex. L-triiodothyronine (T3) and L-thyroxine (T4) both inhibited Na+-K+-ATPase activity (but not Mg2+-ATPase activity) in similar dose-dependent fashions, while other metabolites of TH were less effective. Although both T3and theβ-adrenergic agonist isoproterenol inhibited Na+-K+-ATPase activity in cerebrocortical synaptosomes in similar ways, theβ-adrenergic receptor blocker p

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Cai, Ting, Haojie Wang, Yiliang Chen, Lijun Liu, William T. Gunning, Luis Eduardo M. Quintas, and Zi-Jian Xie. "Regulation of caveolin-1 membrane trafficking by the Na/K-ATPase." Journal of Cell Biology 182, no. 6 (September 15, 2008): 1153–69. http://dx.doi.org/10.1083/jcb.200712022.

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Here, we show that the Na/K-ATPase interacts with caveolin-1 (Cav1) and regulates Cav1 trafficking. Graded knockdown of Na/K-ATPase decreases the plasma membrane pool of Cav1, which results in a significant reduction in the number of caveolae on the cell surface. These effects are independent of the pumping function of Na/K-ATPase, and instead depend on interaction between Na/K-ATPase and Cav1 mediated by an N-terminal caveolin-binding motif within the ATPase α1 subunit. Moreover, knockdown of the Na/K-ATPase increases basal levels of active Src and stimulates endocytosis of Cav1 from the plas

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Vinciguerra, Manlio, Georges Deschênes, Udo Hasler, David Mordasini, Martine Rousselot, Alain Doucet, Alain Vandewalle, Pierre-Yves Martin, and Eric Féraille. "Intracellular Na+ Controls Cell Surface Expression of Na,K-ATPase via a cAMP-independent PKA Pathway in Mammalian Kidney Collecting Duct Cells." Molecular Biology of the Cell 14, no. 7 (July 2003): 2677–88. http://dx.doi.org/10.1091/mbc.e02-11-0720.

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In the mammalian kidney the fine control of Na+ reabsorption takes place in collecting duct principal cells where basolateral Na,K-ATPase provides the driving force for vectorial Na+ transport. In the cortical collecting duct (CCD), a rise in intracellular Na+ concentration ([Na+]i) was shown to increase Na,K-ATPase activity and the number of ouabain binding sites, but the mechanism responsible for this event has not yet been elucidated. A rise in [Na+]i caused by incubation with the Na+ ionophore nystatin, increased Na,K-ATPase activity and cell surface expression to the same extent in isolat

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