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Journal articles on the topic 'FXYD proteins'

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Published: 2 February 2023

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1

Tipsmark, Christian Kølbæk. "Identification of FXYD protein genes in a teleost: tissue-specific expression and response to salinity change." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 294, no. 4 (April 2008): R1367—R1378. http://dx.doi.org/10.1152/ajpregu.00454.2007.

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It is increasingly clear that alterations in Na+-K+-ATPase kinetics to fit the demands in specialized cell types is vital for the enzyme to execute its different physiological roles in diverse tissues. In addition to tissue-dependent expression of isoforms of the conventional subunits, α and β, auxiliary FXYD proteins appear to be essential regulatory components. The present study identified genes belonging to this family in Atlantic salmon by analysis of expressed sequence tags. Based on the conserved domain of these small membrane proteins, eight expressed FXYD isoforms were identified. Phylogenetic analysis suggests that six isoforms are homologues to the previously identified FXYD2, FXYD5, FXYD6, FXYD7, FXYD8, and FXYD9, while two additional isoforms were found (FXYD11 and FXYD12). Using quantitative PCR, tissue-dependent expression of the different isoforms was analyzed in gill, kidney, intestine, heart, muscle, brain, and liver. Two isoforms were expressed in several tissues (FXYD5 and FXYD9), while six isoforms were distributed in a discrete manner. In excitable tissues, two isoforms were highly expressed in brain (FXYD6 and FXYD7) and one in skeletal muscle (FXYD8). In osmoregulatory tissues, one isoform was expressed predominantly in gill (FXYD11), one in kidney (FXYD2), and one equally in kidney and intestine (FXYD12). Expression of several FXYD genes in kidney and gill differed between fresh water and seawater salmon, suggesting significance during osmoregulatory adaptations. In addition to identifying novel FXYD isoforms, these studies are the first to show the tissue dependence in their expression and modulation by salinity in any teleosts.
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2

Geering, Käthi. "FXYD proteins: new regulators of Na-K-ATPase." American Journal of Physiology-Renal Physiology 290, no. 2 (February 2006): F241—F250. http://dx.doi.org/10.1152/ajprenal.00126.2005.

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FXYD proteins belong to a family of small-membrane proteins. Recent experimental evidence suggests that at least five of the seven members of this family, FXYD1 (phospholemman), FXYD2 (γ-subunit of Na-K-ATPase), FXYD3 (Mat-8), FXYD4 (CHIF), and FXYD7, are auxiliary subunits of Na-K-ATPase and regulate Na-K-ATPase activity in a tissue- and isoform-specific way. These results highlight the complexity of the regulation of Na+and K+handling by Na-K-ATPase, which is necessary to ensure appropriate tissue functions such as renal Na+reabsorption, muscle contractility, and neuronal excitability. Moreover, a mutation in FXYD2 has been linked to cases of human hypomagnesemia, indicating that perturbations in the regulation of Na-K-ATPase by FXYD proteins may be critically involved in pathophysiological states. A better understanding of this novel regulatory mechanism of Na-K-ATPase should help in learning more about its role in pathophysiological states. This review summarizes the present knowledge of the role of FXYD proteins in the modulation of Na-K-ATPase as well as of other proteins, their regulation, and their structure-function relationship.
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3

Arystarkhova, Elena, Claudia Donnet, Ana Muñoz-Matta, Susan C. Specht, and Kathleen J. Sweadner. "Multiplicity of expression of FXYD proteins in mammalian cells: dynamic exchange of phospholemman and γ-subunit in response to stress." American Journal of Physiology-Cell Physiology 292, no. 3 (March 2007): C1179—C1191. http://dx.doi.org/10.1152/ajpcell.00328.2006.

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Functional properties of Na-K-ATPase can be modified by association with FXYD proteins, expressed in a tissue-specific manner. Here we show that expression of FXYDs in cell lines does not necessarily parallel the expression pattern of FXYDs in the tissue(s) from which the cells originate. While being expressed only in lacis cells in the juxtaglomerular apparatus and in blood vessels in kidney, FXYD1 was abundant in renal cell lines of proximal tubule origin (NRK-52E, LLC-PK1, and OK cells). Authenticity of FXYD1 as a part of Na-K-ATPase in NRK-52E cells was demonstrated by co-purification, co-immunoprecipitation, and co-localization. Induction of FXYD2 by hypertonicity (500 mosmol/kgH2O with NaCl for 48 h or adaptation to 700 mosmol/kgH2O) correlated with downregulation of FXYD1 at mRNA and protein levels. The response to hypertonicity was influenced by serum factors and entailed, first, dephosphorylation of FXYD1 at Ser68 (1–5 h) and, second, induction of FXYD2a and a decrease in FXYD1 with longer exposure. FXYD1 was completely replaced with FXYD2a in cells adapted to 700 mosmol/kgH2O and showed a significantly decreased sodium affinity. Thus dephosphorylation of FXYD1 followed by exchange of regulatory subunits is utilized to make a smooth transition of properties of Na-K-ATPase. We also observed expression of mRNA for multiple FXYDs in various cell lines. The expression was dynamic and responsive to physiological stimuli. Moreover, we demonstrated expression of FXYD5 protein in HEK-293 and HeLa cells. The data imply that FXYDs are obligatory rather than auxiliary components of Na-K-ATPase, and their interchangeability underlies responses of Na-K-ATPase to cellular stress.
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4

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 expressed in Xenopus oocytes. However, in situ (stomach), FXYD3 is associated only with Na,K-ATPase because its expression is restricted to mucous cells in which H,K-ATPase is absent. Coexpressed in Xenopus oocytes, FXYD3 modulates the glycosylation processing of the β subunit of X,K-ATPase dependent on the presence of the signal peptide. Finally, FXYD3 decreases both the apparent affinity for Na+ and K+ of Na,K-ATPase.
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5

Cornelius, Flemming, and Yasser A. Mahmmoud. "Functional Modulation of the Sodium Pump: The Regulatory Proteins “Fixit”." Physiology 18, no. 3 (June 2003): 119–24. http://dx.doi.org/10.1152/nips.01434.2003.

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Proteins of the FXYD family act as tissue-specific regulators of the Na-K-ATPase. They are small hydrophobic type I proteins with a single-transmembrane span containing an extracellular invariant FXYD sequence. FXYD proteins are not an integral part of the Na-K-ATPase but function to modulate its catalytic properties by molecular interactions with specific Na-K-ATPase domains.
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6

Lubarski, Irina, Steven J. D. Karlish, and Haim Garty. "Structural and functional interactions between FXYD5 and the Na+-K+-ATPase." American Journal of Physiology-Renal Physiology 293, no. 6 (December 2007): F1818—F1826. http://dx.doi.org/10.1152/ajprenal.00367.2007.

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FXYD5 is a member of a family of tissue-specific regulators of the Na+-K+-ATPase expressed in kidney tubules. Previously, we have shown that FXYD5 interacts with the αβ-subunits of the Na+-K+-ATPase and increases its Vmax (Lubarski I, Pihakaski-Maunsbach K, Karlish SJ, Maunsbach AB, Garty H. J Biol Chem 280: 37717–37724, 2005). The current study further characterizes structural interaction and structure-function relationships of FXYD5. FXYD5/FXYD4 chimeras expressed in Xenopus laevis oocytes have been used to demonstrate that both the high-affinity association with the pump and the increase in Vmax are mediated by the transmembrane domain of FXYD5. Several amino acids that participate in the high-affinity interaction between FXYD5 and the α-subunit of the Na+-K+-ATPase have been identified. The data suggest that different FXYD proteins interact similarly with the Na+-K+-ATPase and their transmembrane domains play a key role in both the structural interactions and functional effects. Other experiments have identified at least one splice variant of FXYD5 with 10 additional amino acids at the COOH terminus, suggesting the possibility of other functional effects not mediated by the transmembrane domain. FXYD5 could be specifically bound to wheat germ agglutinin beads, indicating that it is glycosylated. However, unlike previous findings in metastatic cells, such glycosylation does not evoke a large increase in the size of the protein expressed in native epithelia and X. laevis oocytes.
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7

Mishra, Neeraj Kumar, Yoav Peleg, Erica Cirri, Talya Belogus, Yael Lifshitz, Dennis R. Voelker, Hans-Juergen Apell, Haim Garty, and Steven J. D. Karlish. "FXYD Proteins Stabilize Na,K-ATPase." Journal of Biological Chemistry 286, no. 11 (January 12, 2011): 9699–712. http://dx.doi.org/10.1074/jbc.m110.184234.

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8

Tipsmark, Christian K., Yasser A. Mahmmoud, Russell J. Borski, and Steffen S. Madsen. "FXYD-11 associates with Na+-K+-ATPase in the gill of Atlantic salmon: regulation and localization in relation to changed ion-regulatory status." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 299, no. 5 (November 2010): R1212—R1223. http://dx.doi.org/10.1152/ajpregu.00015.2010.

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The Na+-K+-ATPase is the primary electrogenic component driving transepithelial ion transport in the teleost gill; thus regulation of its level of activity is of critical importance for osmotic homeostasis. In the present study, we examined the dynamics of the gill-specific FXYD-11 protein, a putative regulatory subunit of the pump, in Atlantic salmon during seawater (SW) acclimation, smoltification, and treatment with cortisol, growth hormone, and prolactin. Dual-labeling immunohistochemistry showed that branchial FXYD-11 is localized in Na+-K+-ATPase immunoreactive cells, and coimmunoprecipitation experiments confirmed a direct association between FXYD-11 and the Na+-K+-ATPase α-subunit. Transfer of freshwater (FW)-acclimated salmon to SW induced a parallel increase in total α-subunit and FXYD-11 protein expression. A similar concurrent increase was seen during smoltification in FW. In FW fish, cortisol induced an increase in both α-subunit and FXYD-11 abundance, and growth hormone further stimulated FXYD-11 levels. In SW fish, prolactin induced a decrease in FXYD-11 and α-subunit protein levels. In vitro cortisol (18 h, 10 μg/ml) stimulated FXYD-11, but not FXYD-9, mRNA levels in gills from FW and SW salmon. The data show that Na+-K+-ATPase expressed in branchial mitochondrion-rich cells is accompanied by FXYD-11, and that regulation of the two proteins is highly coordinated. The demonstrated association of FXYD-11 and α-subunit strengthens our hypothesis that FXYD-11 has a role in modulating the pump's kinetic properties. The presence of putative phosphorylation sites on the intracellular domain of FXYD-11 suggests the possibility that this protein also may transmit external signals that regulate Na+-K+-ATPase activity.
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9

Zhu, Zhen-Long, Bao-Yong Yan, Yu Zhang, Yan-Hong Yang, Ming-Wei Wang, Hanswalter Zentgraf, Xiang-Hong Zhang, and Xiao-Feng Sun. "Overexpression of FXYD-3 Is Involved in the Tumorigenesis and Development of Esophageal Squamous Cell Carcinoma." Disease Markers 35 (2013): 195–202. http://dx.doi.org/10.1155/2013/740201.

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Objective.To investigate the association of FXYD-3 expression with clinicopathological variables and PINCH in patients with ESCC.Patients and Methods.Expression of FXYD-3 protein was immunohistochemically examined in normal esophageal mucous (n=20) and ESCC (n=64).Results.Expression of FXYD-3 in the cytoplasm markedly increased from normal esophageal epithelial cells to primary ESCC (P=0.001). The expression of FXYD-3 was correlated with TNM stages and depth of tumor invasion. Furthermore, the cases with lymph node metastasis tended to show a higher frequency of positive expression than those without metastasis (P=0.086), and FXYD-3 expression tended to be positively related to the expression of PINCH (P=0.063). Moreover, the cases positive for both proteins had the highest frequency of lymph node metastasis (P=0.001). However, FXYD-3 expression was not correlated with patient’s gender (P=0.847), age (P=0.876), tumor location (P=0.279), size (P=0.7710.771), grade of differentiation (P=0.279), and survival (P=0.113).Conclusion.Overexpression of FXYD-3 in the cytoplasm may play an important role in the tumorigenesis and development in the human ESCC, particularly in combination with PINCH expression.
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10

Garty, Haim, and Steven J. D. Karlish. "ROLE OF FXYD PROTEINS IN ION TRANSPORT." Annual Review of Physiology 68, no. 1 (January 2006): 431–59. http://dx.doi.org/10.1146/annurev.physiol.68.040104.131852.

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11

Lansbery, Kristan L., Lauren C. Burcea, Margaretta L. Mendenhall, and Robert W. Mercer. "Cytoplasmic targeting signals mediate delivery of phospholemman to the plasma membrane." American Journal of Physiology-Cell Physiology 290, no. 5 (May 2006): C1275—C1286. http://dx.doi.org/10.1152/ajpcell.00110.2005.

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The FXYD protein family consists of several small, single-span membrane proteins that exhibit a high degree of homology. The best-known members of the family include the γ-subunit of the Na+-K+-ATPase and phospholemman (PLM), a phosphoprotein of cardiac sarcolemma. Other members of the family include corticosteroid hormone-induced factor (CHIF), mammary tumor protein of 8 kDa (Mat-8), and related to ion channels (RIC). The exact physiological roles of the FXYD proteins remain unknown. To better characterize the function of the members of the FXYD protein family, we expressed several members of the family in Madin-Darby canine kidney (MDCK) cells. All of the FXYD proteins, with the exception of PLM, were primarily found in the basolateral plasma membrane. Surprisingly, PLM, a previously characterized plasma membrane protein, was found to colocalize with the endoplasmic reticulum marker protein disulfide isomerase. Treatment of MDCK cells expressing PLM with an agonist of PKC caused some of the PLM to be redistributed to the plasma membrane. Site-directed mutagenesis of residues within the cytoplasmic domain of PLM indicated that a negative charge at Ser69 is necessary to shift the localization of PLM to the plasma membrane. In addition, other regions of PLM necessary for either its endoplasmic reticulum or plasma membrane localization have been elucidated. In contrast to PLM, the plasma membrane localization of CHIF and RIC was not altered by mutation of potential cytoplasmic phosphorylation sites. Overall, these results suggest that phosphorylation of specific residues of PLM may direct PLM from an intracellular compartment to the plasma membrane.
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12

Seflova, Jaroslava, John Q. Yap, Christine E. Delligatti, Marsha P. Pribadi, Pablo Artigas, Julie Bossuyt, and Seth L. Robia. "Insight into Sodium Pump Regulation by FXYD Proteins." Biophysical Journal 120, no. 3 (February 2021): 75a. http://dx.doi.org/10.1016/j.bpj.2020.11.671.

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13

Lubarski, Irina, Carol Asher, and Haim Garty. "FXYD5 (dysadherin) regulates the paracellular permeability in cultured kidney collecting duct cells." American Journal of Physiology-Renal Physiology 301, no. 6 (December 2011): F1270—F1280. http://dx.doi.org/10.1152/ajprenal.00142.2011.

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FXYD5 (dysadherin or RIC) is a member of the FXYD family of single-span transmembrane proteins associated with the Na+-K+-ATPase. Several studies have demonstrated enhanced expression of FXYD5 during metastasis and effects on cell adhesion and motility. The current study examines effects of FXYD5 on the paracellular permeability in the mouse kidney collecting duct cell line M1. Expressing FXYD5 in these cells leads to a large decrease in amiloride-insensitive transepithelial electrical resistance as well as increased permeability to 4-kDa dextran. Impairment of cell-cell contact was also demonstrated by staining cells for the tight and adherence junction markers zonula occludens-1 and β-catenin, respectively. This is further supported by large expansions of the interstitial spaces, visualized in electron microscope images. Expressing FXYD5 in M1 cells resulted in a decrease in N-glycosylation of β1 Na+-K+-ATPase, while silencing it in H1299 cells had an opposite effect. This may provide a mechanism for the above effects, since normal glycosylation of β1 plays an important role in cell-cell contact formation (Vagin O, Tokhtaeva E, Sachs G. J Biol Chem 281: 39573–39587, 2006).
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14

Boon, Hanneke, Emil Kostovski, Sergej Pirkmajer, Moshi Song, Irina Lubarski, Per O. Iversen, Nils Hjeltnes, Ulrika Widegren, and Alexander V. Chibalin. "Influence of chronic and acute spinal cord injury on skeletal muscle Na+-K+-ATPase and phospholemman expression in humans." American Journal of Physiology-Endocrinology and Metabolism 302, no. 7 (April 1, 2012): E864—E871. http://dx.doi.org/10.1152/ajpendo.00625.2011.

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Na+-K+-ATPase is an integral membrane protein crucial for the maintenance of ion homeostasis and skeletal muscle contractibility. Skeletal muscle Na+-K+-ATPase content displays remarkable plasticity in response to long-term increase in physiological demand, such as exercise training. However, the adaptations in Na+-K+-ATPase function in response to a suddenly decreased and/or habitually low level of physical activity, especially after a spinal cord injury (SCI), are incompletely known. We tested the hypothesis that skeletal muscle content of Na+-K+-ATPase and the associated regulatory proteins from the FXYD family is altered in SCI patients in a manner dependent on the severity of the spinal cord lesion and postinjury level of physical activity. Three different groups were studied: 1) six subjects with chronic complete cervical SCI, 2) seven subjects with acute, complete cervical SCI, and 3) six subjects with acute, incomplete cervical SCI. The individuals in groups 2 and 3 were studied at months 1, 3, and 12 postinjury, whereas individuals with chronic SCI were compared with an able-bodied control group. Chronic complete SCI was associated with a marked decrease in [3H]ouabain binding site concentration in skeletal muscle as well as reduced protein content of the α1-, α2-, and β1-subunit of the Na+-K+-ATPase. In line with this finding, expression of the Na+-K+-ATPase α1- and α2-subunits progressively decreased during the first year after complete but not after incomplete SCI. The expression of the regulatory protein phospholemman (PLM or FXYD1) was attenuated after complete, but not incomplete, cervical SCI. In contrast, FXYD5 was substantially upregulated in patients with complete SCI. In conclusion, the severity of the spinal cord lesion and the level of postinjury physical activity in patients with SCI are important factors controlling the expression of Na+-K+-ATPase and its regulatory proteins PLM and FXYD5.
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15

Lindzen, Moshit, Kay-Eberhard Gottschalk, Maria Füzesi, Haim Garty, and Steven J. D. Karlish. "Structural Interactions between FXYD Proteins and Na+,K+-ATPase." Journal of Biological Chemistry 281, no. 9 (December 21, 2005): 5947–55. http://dx.doi.org/10.1074/jbc.m512063200.

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16

Geering, Käthi. "Function of FXYD Proteins, Regulators of Na, K-ATPase." Journal of Bioenergetics and Biomembranes 37, no. 6 (December 2005): 387–92. http://dx.doi.org/10.1007/s10863-005-9476-x.

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17

Franzin, Carla M., Xiao-Min Gong, Khang Thai, Jinghua Yu, and Francesca M. Marassi. "NMR of membrane proteins in micelles and bilayers: The FXYD family proteins." Methods 41, no. 4 (April 2007): 398–408. http://dx.doi.org/10.1016/j.ymeth.2006.08.011.

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18

Pihakaski-Maunsbach, Kaarina, Henrik Vorum, Bent Honoré, Shigeki Tokonabe, Jørgen Frøkiær, Haim Garty, Steven J. D. Karlish, and Arvid B. Maunsbach. "Locations, abundances, and possible functions of FXYD ion transport regulators in rat renal medulla." American Journal of Physiology-Renal Physiology 291, no. 5 (November 2006): F1033—F1044. http://dx.doi.org/10.1152/ajprenal.00086.2006.

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The γ-subunit of Na-K-ATPase (FXYD2) and corticosteroid hormone-induced factor (CHIF; FXYD4) are considered pump regulators in kidney tubules. The aim of this study was to expand the information about their locations in the kidney medulla and to evaluate their importance for electrolyte excretion in an animal model. The cellular and subcellular locations and abundances of γ and CHIF in the medulla of control and sodium-depleted rats were analyzed by immunofluorescence and immunoelectron microscopy and semiquantitative Western blotting. The results showed that antibodies against the γ-subunit COOH terminus and splice variant γa, but not splice variant γb, labeled intercalated cells, but not principal cells, in the initial part of the inner medullary collecting duct (IMCD1). In subsequent segments (IMCD2 and IMCD3), all principal cells exhibited distinct basolateral labeling for both the γ-subunit COOH terminus, splice variant γa, and CHIF. Splice variant γb was abundant in the inner stripe of the outer medulla but absent in the inner medulla (IM). Double labeling by high-resolution immunoelectron microscopy showed close structural association between CHIF and the Na-K-ATPase α1-subunit in basolateral membranes. The present observations provide new information about the cellular and subcellular locations of γ and CHIF in the renal medulla and show a new γ variant in the IM. Extensive NaCl depletion did not induce significant changes in the locations or abundances of the γ-subunit COOH terminus and CHIF in different kidney zones. We conclude that the unchanged levels of these two FXYD proteins suggest that they are not primary determinants for urine electrolyte composition during NaCl depletion.
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19

Garty, Haim, and Steven J. D. Karlish. "FXYD Proteins: Tissue-Specific Regulators of the Na,K-ATPase." Seminars in Nephrology 25, no. 5 (September 2005): 304–11. http://dx.doi.org/10.1016/j.semnephrol.2005.03.005.

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20

Franzin, Carla M., Jinghua Yu, Khang Thai, Jungyuen Choi, and Francesca M. Marassi. "Correlation of Gene and Protein Structures in the FXYD Family Proteins." Journal of Molecular Biology 354, no. 4 (December 2005): 743–50. http://dx.doi.org/10.1016/j.jmb.2005.10.018.

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21

Franzin, Carla M., Xiao-Min Gong, Peter Teriete, and Francesca M. Marassi. "Structures of the FXYD regulatory proteins in lipid micelles and membranes." Journal of Bioenergetics and Biomembranes 39, no. 5-6 (November 14, 2007): 379–83. http://dx.doi.org/10.1007/s10863-007-9105-y.

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22

Garty, Haim, Moshit Lindzen, Rosemarie Scanzano, Roman Aizman, Maria Füzesi, Rivka Goldshleger, Nicolette Farman, Rhoda Blostein, and Steven J. D. Karlish. "A functional interaction between CHIF and Na-K-ATPase: implication for regulation by FXYD proteins." American Journal of Physiology-Renal Physiology 283, no. 4 (October 1, 2002): F607—F615. http://dx.doi.org/10.1152/ajprenal.00112.2002.

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Like the γ-subunit of Na-K-ATPase, the corticosteroid hormone-induced factor (CHIF) is a member of the FXYD family of one-transmembrane-segment proteins. Both CHIF and two splice variants of γ, γa and γb, are expressed in the kidney. Immunolocalization experiments demonstrate mutually exclusive expression of CHIF and γ in different nephron segments. Specific coimmunoprecipitation experiments demonstrate the existence in kidney membranes of the complexes α/β/γa, α/β/γb, and α/β/CHIF and exclude mixed complexes such as α/β/γa/γb and α/β/γ/CHIF. CHIF has been expressed in HeLa cells harboring the rat α1-subunit of Na-K-ATPase. 86Rb flux experiments demonstrate that CHIF induces a two- to threefold increase in apparent affinity for cytoplasmic Na ( K′Na) but does not affect affinity for extracellular K (Rb) ions ( K′K) or V max. Measurements of Na-K-ATPase using isolated membranes show similar but smaller effects of CHIF on K′Na, whereas K′K and K′ATP are unaffected. The functional effects of CHIF differ from those of γ. An implication of these findings is that other FXYD proteins could act as tissue-specific modulators of Na-K-ATPase.
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23

Li, Ciming, Aurelien Grosdidier, Gilles Crambert, Jean-Daniel Horisberger, Olivier Michielin, and Käthi Geering. "Structural and Functional Interaction Sites between Na,K-ATPase and FXYD Proteins." Journal of Biological Chemistry 279, no. 37 (July 2, 2004): 38895–902. http://dx.doi.org/10.1074/jbc.m406697200.

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24

SWEADNER, KATHLEEN J., ELENA ARYSTARKHOVA, CLAUDIA DONNET, and RANDALL K. WETZEL. "FXYD Proteins as Regulators of the Na,K-ATPase in the Kidney." Annals of the New York Academy of Sciences 986, no. 1 (April 2003): 382–87. http://dx.doi.org/10.1111/j.1749-6632.2003.tb07218.x.

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GEERING, KÄTHI, PASCAL BÉGUIN, HAIM GARTY, STEVEN KARLISH, MARIA FÜZESI, JEAN-DANIEL HORISBERGER, and GILLES CRAMBERT. "FXYD Proteins: New Tissue- and Isoform-Specific Regulators of Na,K-ATPase." Annals of the New York Academy of Sciences 986, no. 1 (April 2003): 388–94. http://dx.doi.org/10.1111/j.1749-6632.2003.tb07219.x.

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26

Crambert, G., and K. Geering. "FXYD Proteins: New Tissue-Specific Regulators of the Ubiquitous Na,K-ATPase." Science Signaling 2003, no. 166 (January 21, 2003): re1. http://dx.doi.org/10.1126/stke.2003.166.re1.

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27

Madsen, Steffen S., Rebecca J. Bollinger, Melanie Brauckhoff, and Morten Buch Engelund. "Gene expression profiling of proximal and distal renal tubules in Atlantic salmon (Salmo salar) acclimated to fresh water and seawater." American Journal of Physiology-Renal Physiology 319, no. 3 (September 1, 2020): F380—F393. http://dx.doi.org/10.1152/ajprenal.00557.2019.

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Euryhaline teleost kidneys undergo a major functional switch from being filtratory in freshwater (FW) to being predominantly secretory in seawater (SW) conditions. The transition involves both vascular and tubular effects. There is consensus that the glomerular filtration rate is greatly reduced upon exposure to hyperosmotic conditions. Yet, regulation at the tubular level has only been examined sporadically in a few different species. This study aimed to obtain a broader understanding of transcriptional regulation in proximal versus distal tubular segments during osmotic transitions. Proximal and distal tubule cells were dissected separately by laser capture microdissection, RNA was extracted, and relative mRNA expression levels of >30 targets involved in solute and water transport were quantified by quantitative PCR in relation to segment type in fish acclimated to FW or SW. The gene categories were aquaporins, solute transporters, fxyd proteins, and tight junction proteins. aqp8bb1, aqp10b1, nhe3, sglt1, slc41a1, cnnm3, fxyd12a, cldn3b, cldn10b, cldn15a, and cldn12 were expressed at a higher level in proximal compared with distal tubules. aqp1aa, aqp1ab, nka-a1a, nka-a1b, nkcc1a, nkcc2, ncc, clc-k, slc26a6C, sglt2, fxyd2, cldn3a, and occln were expressed at a higher level in distal compared with proximal tubules. Expression of aqp1aa, aqp3a1, aqp10b1, ncc, nhe3, cftr, sglt1, slc41a1, fxyd12a, cldn3a, cldn3b, cldn3c, cldn10b, cldn10e, cldn28a, and cldn30c was higher in SW- than in FW-acclimated salmon, whereas the opposite was the case for aqp1ab, slc26a6C, and fxyd2. The data show distinct segmental distribution of transport genes and a significant regulation of tubular transcripts when kidney function is modulated during salinity transitions.
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FÜZESI, MARIA, RIVKA GOLDSHLEGER, HAIM GARTY, and STEVEN J. D. KARLISH. "Defining the Nature and Sites of Interaction between FXYD Proteins and Na,K-ATPase." Annals of the New York Academy of Sciences 986, no. 1 (April 2003): 532–33. http://dx.doi.org/10.1111/j.1749-6632.2003.tb07243.x.

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Bibert, Stéphanie, Chia-Chi Liu, Gemma A. Figtree, Alvaro Garcia, Elisha J. Hamilton, Francesca M. Marassi, Kathleen J. Sweadner, Flemming Cornelius, Käthi Geering, and Helge H. Rasmussen. "FXYD Proteins Reverse Inhibition of the Na+-K+Pump Mediated by Glutathionylation of Its β1Subunit." Journal of Biological Chemistry 286, no. 21 (March 30, 2011): 18562–72. http://dx.doi.org/10.1074/jbc.m110.184101.

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Tulloch, Lindsay B., Jacqueline Howie, Krzysztof J. Wypijewski, Catherine R. Wilson, William G. Bernard, Michael J. Shattock, and William Fuller. "The Inhibitory Effect of Phospholemman on the Sodium Pump Requires Its Palmitoylation." Journal of Biological Chemistry 286, no. 41 (August 25, 2011): 36020–31. http://dx.doi.org/10.1074/jbc.m111.282145.

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Phospholemman (PLM), the principal sarcolemmal substrate for protein kinases A and C in the heart, regulates the cardiac sodium pump. We investigated post-translational modifications of PLM additional to phosphorylation in adult rat ventricular myocytes (ARVM). LC-MS/MS of tryptically digested PLM immunoprecipitated from ARVM identified cysteine 40 as palmitoylated in some peptides, but no information was obtained regarding the palmitoylation status of cysteine 42. PLM palmitoylation was confirmed by immunoprecipitating PLM from ARVM loaded with [3H]palmitic acid and immunoblotting following streptavidin affinity purification from ARVM lysates subjected to fatty acyl biotin exchange. Mutagenesis identified both Cys-40 and Cys-42 of PLM as palmitoylated. Phosphorylation of PLM at serine 68 by PKA in ARVM or transiently transfected HEK cells increased its palmitoylation, but PKA activation did not increase the palmitoylation of S68A PLM-YFP in HEK cells. Wild type and unpalmitoylatable PLM-YFP were all correctly targeted to the cell surface membrane, but the half-life of unpalmitoylatable PLM was reduced compared with wild type. In cells stably expressing inducible PLM, PLM expression inhibited the sodium pump, but PLM did not inhibit the sodium pump when palmitoylation was inhibited. Hence, palmitoylation of PLM controls its turnover, and palmitoylated PLM inhibits the sodium pump. Surprisingly, phosphorylation of PLM enhances its palmitoylation, probably through the enhanced mobility of the phosphorylated intracellular domain increasing the accessibility of cysteines for the palmitoylating enzyme, with interesting theoretical implications. All FXYD proteins have conserved intracellular cysteines, so FXYD protein palmitoylation may be a universal means to regulate the sodium pump.
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Aizman, Roman, Carol Asher, Maria Füzesi, Hedva Latter, Peter Lonai, Steven J. D. Karlish, and Haim Garty. "Generation and phenotypic analysis of CHIF knockout mice." American Journal of Physiology-Renal Physiology 283, no. 3 (September 1, 2002): F569—F577. http://dx.doi.org/10.1152/ajprenal.00376.2001.

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Corticosteroid hormone-induced factor (CHIF) is a short epithelial-specific protein that is independently induced by aldosterone and a high-K+ diet. It is a member of the FXYD family of single-span transmembrane proteins that include phospholemman, Mat-8, and the γ-subunit of Na+-K+-ATPase. A number of studies have suggested that these proteins are involved in the regulation of ion transport and, in particular, functionally interact with the Na+-K+-ATPase. The present study describes the characterization, targeted disruption, and phenotypic analysis of the mouse CHIF gene. The CHIF knockout mice are viable and not distinguishable from wild-type littermates under normal conditions. Under K+ loading, they have a twofold higher urine volume and an increased glomerular filtration rate. Similar but smaller effects are observed in mice fed a low-Na+ diet. Treating K+-loaded mice for 10 days with furosemide resulted in lethality in the knockout mice (17 of 39) but not in the wild-type group (1 of 39). The data are consistent with an effect of CHIF on the Na+-K+-ATPase that is specific to the outer and inner medullary duct, its major expression site.
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Yang, Wen-Kai, Chao-Kai Kang, Chia-Hao Chang, An-Di Hsu, Tsung-Han Lee, and Pung-Pung Hwang. "Expression Profiles of Branchial FXYD Proteins in the Brackish Medaka Oryzias dancena: A Potential Saltwater Fish Model for Studies of Osmoregulation." PLoS ONE 8, no. 1 (January 31, 2013): e55470. http://dx.doi.org/10.1371/journal.pone.0055470.

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33

Yang, Wen-Kai, I.-Chan Yang, Hsin-Ju Chuang, Tse-Lih Chao, Yau-Chung Hu, Wen-Yi Wu, Yu-Chun Wang, Cheng-Hao Tang, and Tsung-Han Lee. "Positive correlation of gene expression between branchial FXYD proteins and Na+/K+-ATPase of euryhaline milkfish in response to hypoosmotic challenges." Comparative Biochemistry and Physiology Part A: Molecular & Integrative Physiology 231 (May 2019): 177–87. http://dx.doi.org/10.1016/j.cbpa.2019.02.023.

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34

Yang, Wen-Kai, Tse-Lih Chao, Hsin-Ju Chuang, Yao-Chung Hu, Catherine Lorin-Nebel, Eva Blondeau-Bidet, Wen-Yi Wu, Cheng-Hao Tang, Shu-Chuan Tsai, and Tsung-Han Lee. "Gene expression of Na+/K+-ATPase α-isoforms and FXYD proteins and potential modulatory mechanisms in euryhaline milkfish kidneys upon hypoosmotic challenges." Aquaculture 504 (April 2019): 59–69. http://dx.doi.org/10.1016/j.aquaculture.2019.01.046.

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35

Cornelius, Flemming, Yasser A. Mahmmoud, Lara Meischke, and Gordon Cramb. "Functional Significance of the Shark Na,K-ATPase N-Terminal Domain. Is the Structurally Variable N-Terminus Involved in Tissue-Specific Regulation by FXYD Proteins?†." Biochemistry 44, no. 39 (October 2005): 13051–62. http://dx.doi.org/10.1021/bi0504456.

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36

Moshitzky, Shiri, Carol Asher, and Haim Garty. "Intracellular Trafficking of FXYD1 (Phospholemman) and FXYD7 Proteins inXenopusOocytes and Mammalian Cells." Journal of Biological Chemistry 287, no. 25 (April 25, 2012): 21130–41. http://dx.doi.org/10.1074/jbc.m112.347807.

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37

Zhang, Xue-Qian, J. Randall Moorman, Belinda A. Ahlers, Lois L. Carl, Douglas E. Lake, Jianliang Song, J. Paul Mounsey, et al. "Phospholemman overexpression inhibits Na+-K+-ATPase in adult rat cardiac myocytes: relevance to decreased Na+ pump activity in postinfarction myocytes." Journal of Applied Physiology 100, no. 1 (January 2006): 212–20. http://dx.doi.org/10.1152/japplphysiol.00757.2005.

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Messenger RNA levels of phospholemman (PLM), a member of the FXYD family of small single-span membrane proteins with putative ion-transport regulatory properties, were increased in postmyocardial infarction (MI) rat myocytes. We tested the hypothesis that the previously observed reduction in Na+-K+-ATPase activity in MI rat myocytes was due to PLM overexpression. In rat hearts harvested 3 and 7 days post-MI, PLM protein expression was increased by two- and fourfold, respectively. To simulate increased PLM expression post-MI, PLM was overexpressed in normal adult rat myocytes by adenovirus-mediated gene transfer. PLM overexpression did not affect the relative level of phosphorylation on serine68 of PLM. Na+-K+-ATPase activity was measured as ouabain-sensitive Na+-K+ pump current (Ip). Compared with control myocytes overexpressing green fluorescent protein alone, Ip measured in myocytes overexpressing PLM was significantly ( P < 0.0001) lower at similar membrane voltages, pipette Na+ ([Na+]pip) and extracellular K+ ([K+]o) concentrations. From −70 to +60 mV, neither [Na+]pip nor [K+]o required to attain half-maximal Ip was significantly different between control and PLM myocytes. This phenotype of decreased Vmax without appreciable changes in Km for Na+ and K+ in PLM-overexpressed myocytes was similar to that observed in MI rat myocytes. Inhibition of Ip by PLM overexpression was not due to decreased Na+-K+-ATPase expression because there were no changes in either protein or messenger RNA levels of either α1- or α2-isoforms of Na+-K+-ATPase. In native rat cardiac myocytes, PLM coimmunoprecipitated with α-subunits of Na+-K+-ATPase. Inhibition of Na+-K+-ATPase by PLM overexpression, in addition to previously reported decrease in Na+-K+-ATPase expression, may explain altered Vmax but not Km of Na+-K+-ATPase in postinfarction rat myocytes.
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38

Lubarski, Irina, Carol Asher, and Haim Garty. "Modulation of cell polarization by the Na+-K+-ATPase-associated protein FXYD5 (dysadherin)." American Journal of Physiology-Cell Physiology 306, no. 11 (June 1, 2014): C1080—C1088. http://dx.doi.org/10.1152/ajpcell.00042.2014.

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FXYD5 (dysadherin or also called a related to ion channel, RIC) is a transmembrane auxiliary subunit of the Na+-K+-ATPase shown to increase its maximal velocity ( Vmax). FXYD5 has also been identified as a cancer-associated protein whose expression in tumor-derived cell lines impairs cytoskeletal organization and increases cell motility. Previously, we have demonstrated that the expression of FXYD5 in M1 cells derived from mouse kidney collecting duct impairs the formation of tight and adherence junctions. The current study aimed to further explore effects of FXYD5 at a single cell level. It was found that in M1, as well as three other cell lines, FXYD5 inhibits transformation of adhered single cells from the initial radial shape to a flattened, elongated shape in the first stage of monolayer formation. This is also correlated to less ordered actin cables and fewer focal points. Structure-function analysis has demonstrated that the transmembrane domain of FXYD5, and not its unique extracellular segment, mediates the inhibition of change in cell shape. This domain has been shown before to be involved in the association of FXYD5 with the Na+-K+-ATPase, which leads to the increase in Vmax. Furthermore, specific transmembrane point mutations in FXYD5 that either increase or decrease its effect on cell elongation had a corresponding effect on the coimmunoprecipitation of FXYD5 with α Na+-K+-ATPase. These findings lend support to the possibility that FXYD5 affects cell polarization through its transmembrane domain interaction with the Na+-K+-ATPase. Yet interaction of FXYD5 with other proteins cannot be excluded.
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Sha, Qun, Wade Pearson, Lauren C. Burcea, Darian A. Wigfall, Paul H. Schlesinger, Colin G. Nichols, and Robert W. Mercer. "Human FXYD2 G41R mutation responsible for renal hypomagnesemia behaves as an inward-rectifying cation channel." American Journal of Physiology-Renal Physiology 295, no. 1 (July 2008): F91—F99. http://dx.doi.org/10.1152/ajprenal.00519.2007.

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A mutation in the human FXYD2 polypeptide (Na-K-ATPase γ subunit) that changes a conserved transmembrane glycine to arginine is linked to dominant renal hypomagnesemia. Xenopus laevis oocytes injected with wild-type FXYD2 or the mutant G41R cRNAs expressed large nonselective ion currents. However, in contrast to the wild-type FXYD2 currents, inward rectifying cation currents were induced by hyperpolarization pulses in oocytes expressing the G41R mutant. Injection of EDTA into the oocyte removed inward rectification in the oocytes expressing the mutant, but did not alter the nonlinear current-voltage relationship of the wild-type FXYD2 pseudo-steady-state currents. Extracellular divalent ions, Ca2+ and Ba2+, and trivalent cations, La3+, blocked both the wild-type and mutant FXYD2 currents. Site-directed mutagenesis of G41 demonstrated that a positive charge at this site is required for the inward rectification. When the wild-type FXYD2 was expressed in Madin-Darby canine kidney cells, the cells in the presence of a large apical-to-basolateral Mg2+ gradient and at negative potentials had an increase in transepithelial current compared with cells expressing the G41R mutant or control transfected cells. Moreover, this current was inhibited by extracellular Ba2+ at the basolateral surface. These results suggest that FXYD2 can mediate basolateral extrusion of magnesium from cultured renal epithelial cells and provide new insights into the understanding of the possible physiological roles of FXYD2 wild-type and mutant proteins.
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Bibert, Stéphanie, David Aebischer, Florian Desgranges, Sophie Roy, Danièle Schaer, Solange Kharoubi-Hess, Jean-Daniel Horisberger, and Käthi Geering. "A Link between FXYD3 (Mat-8)-mediated Na,K-ATPase Regulation and Differentiation of Caco-2 Intestinal Epithelial Cells." Molecular Biology of the Cell 20, no. 4 (February 15, 2009): 1132–40. http://dx.doi.org/10.1091/mbc.e08-10-0999.

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FXYD3 (Mat-8) proteins are regulators of Na,K-ATPase. In normal tissue, FXYD3 is mainly expressed in stomach and colon, but it is also overexpressed in cancer cells, suggesting a role in tumorogenesis. We show that FXYD3 silencing has no effect on cell proliferation but promotes cell apoptosis and prevents cell differentiation of human colon adenocarcinoma cells (Caco-2), which is reflected by a reduction in alkaline phosphatase and villin expression, a change in several other differentiation markers, and a decrease in transepithelial resistance. Inhibition of cell differentiation in FXYD3-deficient cells is accompanied by an increase in the apparent Na+ and K+ affinities of Na,K-ATPase, reflecting the absence of Na,K-pump regulation by FXYD3. In addition, we observe a decrease in the maximal Na,K-ATPase activity due to a decrease in its turnover number, which correlates with a change in Na,K-ATPase isozyme expression that is characteristic of cancer cells. Overall, our results suggest an important role of FXYD3 in cell differentiation of Caco-2 cells. One possibility is that FXYD3 silencing prevents proper regulation of Na,K-ATPase, which leads to perturbation of cellular Na+ and K+ homeostasis and changes in the expression of Na,K-ATPase isozymes, whose functional properties are incompatible with Caco-2 cell differentiation.
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Okuda, Jun, Naoki Hayashi, Masashi Okamoto, Shinji Sawada, Shu Minagawa, Yoshitaka Yano, and Naomasa Gotoh. "Translocation of Pseudomonas aeruginosa from the Intestinal Tract Is Mediated by the Binding of ExoS to an Na,K-ATPase Regulator, FXYD3." Infection and Immunity 78, no. 11 (August 30, 2010): 4511–22. http://dx.doi.org/10.1128/iai.00428-10.

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ABSTRACT The intestinal tract is considered the most important reservoir of Pseudomonas aeruginosa in intensive care units (ICUs). Gut colonization by P. aeruginosa underlies the development of invasive infections such as gut-derived sepsis. Intestinal colonization by P. aeruginosa is associated with higher ICU mortality rates. The translocation of endogenous P. aeruginosa from the colonized intestinal tract is an important pathogenic phenomenon. Here we identify bacterial and host proteins associated with bacterial penetration through the intestinal epithelial barrier. We first show by comparative genomic hybridization analysis that the exoS gene, encoding the type III effector protein, ExoS, was specifically detected in a clinical isolate that showed higher virulence in silkworms following midgut injection. We further show using a silkworm oral infection model that exoS is required both for virulence and for bacterial translocation from the midgut to the hemolymph. Using a bacterial two-hybrid screen, we show that the mammalian factor FXYD3, which colocalizes with and regulates the function of Na,K-ATPase, directly binds ExoS. A pulldown assay revealed that ExoS binds to the transmembrane domain of FXYD3, which also interacts with Na,K-ATPase. Na,K-ATPase controls the structure and barrier function of tight junctions in epithelial cells. Collectively, our results suggest that ExoS facilitates P. aeruginosa penetration through the intestinal epithelial barrier by binding to FXYD3 and thereby impairing the defense function of tight junctions against bacterial penetration.
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42

Kaneko, Satoshi, Shinnosuke Iwamatsu, Atsushi Kuno, Zui Fujimoto, Yoko Sato, Kei Yura, Mitiko Go, et al. "Module shuffling of a family F/10 xylanase: replacement of modules M4 and M5 of the FXYN of Streptomyces olivaceoviridis E-86 with those of the Cex of Cellulomonas fimi." Protein Engineering, Design and Selection 13, no. 12 (December 2000): 873–79. http://dx.doi.org/10.1093/protein/13.12.873.

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43

Wen, Ru M., Jessica C. Stark C. Stark, Fernando García-Marqués, Hongjuan Zhao, Rosie Nolley, Carolyn R. Bertozzi, Sharon J. Pitteri, and James D. Brooks. "Abstract A13: Siglec-7/9-sialic acid interactions inhibit T cell immune response in prostate cancer." Cancer Immunology Research 10, no. 12_Supplement (December 1, 2022): A13. http://dx.doi.org/10.1158/2326-6074.tumimm22-a13.

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Abstract Immunotherapy has rapidly expanded in the care of patients with cancer with the discovery of immune checkpoints like PD-1 and CTLA-4. However, current immune checkpoint inhibitors are largely ineffective for prostate cancer. Recent studies suggest an alternative immune evasion pathway through the interactions between Sialic acid-binding immunoglobulin-type lectin proteins (Siglec) and their ligands, sialylated glycoprotein. Siglec-7/9-sialic acid interactions are reported to inhibit the immune cell response in several cancer types including leukemia, melanoma, and non-small cell lung cancer. Here, we demonstrated that Siglec-7/9 ligands were expressed in both prostate cancer tumor tissues and cell lines. We promoted T cell-mediated cytotoxicity of cancer cells by disrupting the interactions between Siglec-7/9 and their ligands. We discovered that FXYD5 and CD59 are potential Siglec-7 and Siglec-9 ligands, respectively, with CRISPRi screen. We then found that FXYD5 and CD59 knockout cells had reduced Siglec-7/9 binding capacity and enhanced T cells mediated killing effects on prostate cancer cells. These results provide a rationale for novel immune checkpoints and potential approaches for targeting Siglec-7/FXYD5 and Siglec-9/CD59 immune checkpoints for prostate cancer. Citation Format: Ru M Wen, Jessica C. Stark C Stark, Fernando García-Marqués, Hongjuan Zhao, Rosie Nolley, Carolyn R Bertozzi, Sharon J Pitteri, James D. Brooks. Siglec-7/9-sialic acid interactions inhibit T cell immune response in prostate cancer [abstract]. In: Proceedings of the AACR Special Conference: Tumor Immunology and Immunotherapy; 2022 Oct 21-24; Boston, MA. Philadelphia (PA): AACR; Cancer Immunol Res 2022;10(12 Suppl):Abstract nr A13.
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44

Christiansen, Danny, David J. Bishop, James R. Broatch, Jens Bangsbo, Michael J. McKenna, and Robyn M. Murphy. "Cold-water immersion after training sessions: effects on fiber type-specific adaptations in muscle K+ transport proteins to sprint-interval training in men." Journal of Applied Physiology 125, no. 2 (August 1, 2018): 429–44. http://dx.doi.org/10.1152/japplphysiol.00259.2018.

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Effects of regular use of cold-water immersion (CWI) on fiber type-specific adaptations in muscle K+ transport proteins to intense training, along with their relationship to changes in mRNA levels after the first training session, were investigated in humans. Nineteen recreationally active men (24 ± 6 yr, 79.5 ± 10.8 kg, 44.6 ± 5.8 ml·kg−1·min−1) completed six weeks of sprint-interval cycling, either without (passive rest; CON) or with training sessions followed by CWI (15 min at 10°C; COLD). Muscle biopsies were obtained before and after training to determine abundance of Na+, K+-ATPase isoforms (α1–3, β1–3) and phospholemman (FXYD1) and after recovery treatments (+0 h and +3 h) on the first day of training to measure mRNA content. Training increased ( P < 0.05) the abundance of α1 and β3 in both fiber types and β1 in type-II fibers and decreased FXYD1 in type-I fibers, whereas α2 and α3 abundance was not altered by training ( P > 0.05). CWI after each session did not influence responses to training ( P > 0.05). However, α2 mRNA increased after the first session in COLD (+0 h, P < 0.05) but not in CON ( P > 0.05). In both conditions, α1 and β3 mRNA increased (+3 h; P < 0.05) and β2 mRNA decreased (+3 h; P < 0.05), whereas α3, β1, and FXYD1 mRNA remained unchanged ( P > 0.05) after the first session. In summary, Na+,K+-ATPase isoforms are differently regulated in type I and II muscle fibers by sprint-interval training in humans, which, for most isoforms, do not associate with changes in mRNA levels after the first training session. CWI neither impairs nor improves protein adaptations to intense training of importance for muscle K+ regulation. NEW & NOTEWORTHY Although cold-water immersion (CWI) after training and competition has become a routine for many athletes, limited published evidence exists regarding its impact on training adaptation. Here, we show that CWI can be performed regularly without impairing training-induced adaptations at the fiber-type level important for muscle K+ handling. Furthermore, sprint-interval training invoked fiber type-specific adaptations in K+ transport proteins, which may explain the dissociated responses of whole-muscle protein levels and K+ transport function to training previously reported.
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45

Skovgaard, Casper, Nicki Winfield Almquist, and Jens Bangsbo. "Effect of increased and maintained frequency of speed endurance training on performance and muscle adaptations in runners." Journal of Applied Physiology 122, no. 1 (January 1, 2017): 48–59. http://dx.doi.org/10.1152/japplphysiol.00537.2016.

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The aim of the study was, in runners accustomed to speed endurance training (SET), to examine the effect of increased and maintained frequency of SET on performance and muscular adaptations. After familiarization (FAM) to SET, 18 male ( n = 14) and female ( n = 4) runners (V̇o2max: 57.3 ± 3.4 ml/min; means ± SD) completed 20 sessions of maintained low-frequency (LF; every fourth day; n = 7) or high-frequency (HF; every second day; n = 11) SET. Before FAM as well as before and after an intervention period (INT), subjects completed a series of running tests and a biopsy from m. vastus lateralis was collected. Ten-kilometer performance improved ( P < 0.05) ~3.5% during FAM with no further change during INT. Time to exhaustion at 90% vV̇o2max was 15 and 22% longer ( P < 0.05) during FAM and a further 12 and 16% longer ( P < 0.05) during INT in HF and LF, respectively. During FAM, muscle expression of NHE1 and maximal activity of citrate synthase (CS) and phosphofructokinase (PFK) increased ( P < 0.05), running economy (RE) improved ( P < 0.05), and V̇o2max was unchanged. During INT, both HF and LF increased ( P < 0.05) muscle expression of NKAβ1, whereas maximal activity of CS and PFK, RE, and V̇o2max were unchanged. Furthermore, during INT, muscle expression of FXYD1 and SERCA1, and FXYD1 activity increased ( P < 0.05) in HF, while muscle expression of SERCA2 decreased ( P < 0.05) in LF. Thus increased or maintained frequency of SET leads to further improvements in short-term exercise capacity, but not in 10-km running performance. The better short-term exercise capacity may be associated with elevated expression of muscle proteins related to Na+/K+ transportation and Ca2+ reuptake. NEW & NOTEWORTHY Ten speed endurance training (SET) sessions improved short-term exercise capacity and 10-km performance, which was followed by further improved short-term exercise capacity, but unchanged 10-km performance after 20 SET sessions performed with either high frequency (4 per 8 days) or continued low frequency (2 per 8 days) in trained runners. The further gain in short-term exercise capacity was associated with changes in muscle expression of proteins of importance for the development of fatigue.
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Skovgaard, Casper, Nicki Winfield Almquist, Thue Kvorning, Peter Møller Christensen, and Jens Bangsbo. "Effect of tapering after a period of high-volume sprint interval training on running performance and muscular adaptations in moderately trained runners." Journal of Applied Physiology 124, no. 2 (February 1, 2018): 259–67. http://dx.doi.org/10.1152/japplphysiol.00472.2017.

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The effect of tapering following a period of high-volume sprint interval training (SIT) and a basic volume of aerobic training on performance and muscle adaptations in moderately trained runners was examined. Eleven (8 men, 3 women) runners [maximum oxygen uptake (V̇o2max): 56.8 ± 2.9 ml·min−1·kg−1; mean ± SD] conducted high-volume SIT (HV; 20 SIT sessions; 8–12 × 30 s all-out) for 40 days followed by 18 days of tapering (TAP; 4 SIT sessions; 4 × 30 s all-out). Before and after HV as well as midway through and at the end of TAP, the subjects completed a 10-km running test and a repeated running test at 90% of vV̇o2max to exhaustion (RRT). In addition, a biopsy from the vastus lateralis muscle was obtained at rest. Performance during RRT was better ( P < 0.01) at the end of TAP than before HV (6.8 ± 0.5 vs. 5.6 ± 0.5 min; means ± SE), and 10-km performance was 2.7% better ( P < 0.05) midway through (40.7 ± 0.7 min) and at the end of (40.7 ± 0.6 min) TAP than after HV (41.8 ± 0.9 min). The expression of muscle Na+-K+-ATPase (NKA)α1, NKAβ1, phospholemman (FXYD1), and sarcoplasmic reticulum calcium transport ATPase (SERCA1) increased ( P < 0.05) during HV and remained higher during TAP. In addition, oxygen uptake at 60% of vV̇o2max was lower ( P < 0.05) at the end of TAP than before and after HV. Thus short-duration exercise capacity and running economy were better than before the HV period together with higher expression of muscle proteins related to Na+/K+ transport and Ca2+ reuptake, while 10-km performance was not significantly improved by the combination of HV and tapering. NEW & NOTEWORTHY Short-duration performance became better after 18 days of tapering from ~6 wk of high-volume sprint interval training (SIT), whereas 10-km performance was not significantly affected by the combination of high-volume SIT and tapering. Higher expression of muscle NKAα1, NKAβ1, FXYD1, and SERCA1 may reflect faster Na+/K+ transport and Ca2+ reuptake that could explain the better short-duration performance. These results suggest that the type of competition should determine the duration of tapering to optimize performance.
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Dimke, Henrik, Joost G. Hoenderop, and René J. Bindels. "Hereditary tubular transport disorders: implications for renal handling of Ca2+ and Mg2+." Clinical Science 118, no. 1 (September 28, 2009): 1–18. http://dx.doi.org/10.1042/cs20090086.

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The kidney plays an important role in maintaining the systemic Ca2+ and Mg2+ balance. Thus the renal reabsorptive capacity of these cations can be amended to adapt to disturbances in plasma Ca2+ and Mg2+ concentrations. The reabsorption of Ca2+ and Mg2+ is driven by transport of other electrolytes, sometimes through selective channels and often supported by hormonal stimuli. It is, therefore, not surprising that monogenic disorders affecting such renal processes may impose a shift in, or even completely blunt, the reabsorptive capacity of these divalent cations within the kidney. Accordingly, in Dent's disease, a disorder with defective proximal tubular transport, hypercalciuria is frequently observed. Dysfunctional thick ascending limb transport in Bartter's syndrome, familial hypomagnesaemia with hypercalciuria and nephrocalcinosis, and diseases associated with Ca2+-sensing receptor defects, markedly change tubular transport of Ca2+ and Mg2+. In the distal convolutions, several proteins involved in Mg2+ transport have been identified [TRPM6 (transient receptor potential melastatin 6), proEGF (pro-epidermal growth factor) and FXYD2 (Na+/K+-ATPase γ-subunit)]. In addition, conditions such as Gitelman's syndrome, distal renal tubular acidosis and pseudohypoaldosteronism type II, as well as a mitochondrial defect associated with hypomagnesaemia, all change the renal handling of divalent cations. These hereditary disorders have, in many cases, substantially increased our understanding of the complex transport processes in the kidney and their contribution to the regulation of overall Ca2+ and Mg2+ balance.
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48

Zhao, Xiaonan, Huiyan Lu, and Karen Usdin. "FAN1’s protection against CGG repeat expansion requires its nuclease activity and is FANCD2-independent." Nucleic Acids Research 49, no. 20 (October 28, 2021): 11643–52. http://dx.doi.org/10.1093/nar/gkab899.

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Abstract The Repeat Expansion Diseases, a large group of human diseases that includes the fragile X-related disorders (FXDs) and Huntington's disease (HD), all result from expansion of a disease-specific microsatellite via a mechanism that is not fully understood. We have previously shown that mismatch repair (MMR) proteins are required for expansion in a mouse model of the FXDs, but that the FANCD2 and FANCI associated nuclease 1 (FAN1), a component of the Fanconi anemia (FA) DNA repair pathway, is protective. FAN1’s nuclease activity has been reported to be dispensable for protection against expansion in an HD cell model. However, we show here that in a FXD mouse model a point mutation in the nuclease domain of FAN1 has the same effect on expansion as a null mutation. Furthermore, we show that FAN1 and another nuclease, EXO1, have an additive effect in protecting against MSH3-dependent expansions. Lastly, we show that the loss of FANCD2, a vital component of the Fanconi anemia DNA repair pathway, has no effect on expansions. Thus, FAN1 protects against MSH3-dependent expansions without diverting the expansion intermediates into the canonical FA pathway and this protection depends on FAN1 having an intact nuclease domain.
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49

Bossuyt, Julie, Sanda Despa, Jody L. Martin, and Donald M. Bers. "Phospholemman Phosphorylation Alters Its Fluorescence Resonance Energy Transfer with the Na/K-ATPase Pump." Journal of Biological Chemistry 281, no. 43 (August 30, 2006): 32765–73. http://dx.doi.org/10.1074/jbc.m606254200.

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Phospholemman (PLM) or FXYD1 is a major cardiac myocyte phosphorylation target upon adrenergic stimulation. Prior immunoprecipitation and functional studies suggest that phospholemman associates with the Na/K-pump (NKA) and mediates adrenergic Na/K-pump regulation. Here, we tested whether the NKA-PLM interaction is close enough to allow fluorescence resonance energy transfer (FRET) between cyan and yellow fluorescent (CFP/YFP) fusion proteins of Na/K pump and phospholemman and whether phospholemman phosphorylation alters such FRET. Co-expressed NKA-CFP and PLM-YFP in HEK293 cells co-localized in the plasma membrane and exhibited robust FRET. Selective acceptor photobleach increased donor fluorescence (FCFP) by 21.5 ± 4.1% (n = 13), an effect nearly abolished when co-expressing excess phospholemman lacking YFP. Activation of protein kinase C or A progressively and reversibly decreased FRET assessed by either the fluorescence ratio (FYFP/FCFP) or the enhancement of donor fluorescence after acceptor bleach. After protein kinase C activation, forskolin did not further reduce FRET, but after forskolin pretreatment, protein kinase C could still reduce FRET. This agreed with phospholemman phosphorylation measurements: by protein kinase C at both Ser-63 and Ser-68, but by protein kinase A only at Ser-68. Expression of PLM-YFP and PLM-CFP resulted in even stronger FRET than for NKA-PLM (FCFP increased by 37 ± 1% upon YFP photobleach), and this FRET was enhanced by phospholemman phosphorylation, consistent with phospholemman multimerization. Co-expressed PLM-CFP and Na/Ca exchange-YFP were highly membrane co-localized, but FRET was undetectable. We conclude that phospholemman and Na/K-pump are in very close proximity (FRET occurs) and that phospholemman phosphorylation alters the interaction of Na/K-pump and phospholemman.
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50

Jia, Xinjian, Hai Lei, Xuemei Jiang, Ying Yi, Xue Luo, Junyan Li, Yu Chen, Sha Liu, and Chengcheng Yang. "Identification of Crucial lncRNAs for Luminal A Breast Cancer through RNA Sequencing." International Journal of Endocrinology 2022 (June 2, 2022): 1–14. http://dx.doi.org/10.1155/2022/6577942.

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Background. The growing body of evidence indicates aberrant expression of long noncoding RNAs (lncRNAs) in breast cancer. Nevertheless, a few studies have focused on identifying key lncRNAs for patients with luminal A breast cancer. In our study, we tried to find key lncRNAs and mRNAs in luminal A breast cancer. Methods. RNA sequencing was performed to identify differentially expressed mRNAs (DEmRNAs) and differentially expressed lncRNAs (DElncRNAs) in luminal A breast cancer. The protein-protein interaction (PPI), DElncRNA-DEmRNA coexpression, DElncRNA-nearby DEmRNA interaction networks, and functional annotation were performed to uncover the function of DEmRNAs. Online databases were used to validate the RNA sequencing result. The diagnostic value of candidate mRNAs was evaluated by receiver operating characteristic (ROC) curve analysis. Results. A total number of 1451 DEmRNAs and 272 DElncRNAs were identified. Several hub proteins were identified in the PPI network, including TUBB3, HIST2H3C, MCM2, MYOC, NEK2, LIPE, FN1, FOXJ1, S100A7, and DLK1. In the DElncRNA-DEmRNA coexpression, some hub lncRNAs were identified, including AP001528.2, LINC00968, LINC02202, TRHDE-AS1, LINC01140, AL354707.1, AC097534.1, MIR222HG, and AL662844.4. The mRNA expression result of TFF1, COL10A1, LEP, PLIN1, PGM5-AS1, and TRHDE-AD1 in the GSE98793 was consistent with the RNA sequencing result. The protein expression results of TUBB3, MCM2, MYOC, FN1, S100A7, and TFF1 were consistent with the mRNA expression result COL10A1, LEP, PLIN1, PGM5-AS1, and TRHDE-AD1 were capable of discriminating luminal A breast cancer and normal controls. Four lncRNA-nearby and coexpressed mRNA pairs of HOXC-AS3-HOXC10, AC020907.2-FXYD1, AC026461.1-MT1X, and AC132217.1-IGF2 were identified. AMPK (involved LIPE and LEP) and PPAR (involved PLIN1) were two significantly enriched pathways in luminal A breast cancer. Conclusion. This study could be helpful in unraveling the pathogenesis and providing novel therapeutic strategies for luminal A breast cancer.
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