2 edition of Na⁺/K⁺ ATPase Ü Subunit and Ü Subunit mRNA levels in preimplantation mouse and rabbit embryos found in the catalog.
Na⁺/K⁺ ATPase Ü Subunit and Ü Subunit mRNA levels in preimplantation mouse and rabbit embryos
Catherine S. Gardiner
Written in English
|Statement||by Catherine S. Gardiner.|
|The Physical Object|
|Pagination||118 leaves, bound :|
|Number of Pages||118|
Preimplantation embryo programming: Transcription epigenetics, and culture environment Article Literature Review (PDF Available) in Reproduction (Cambridge, England) (2) March Normally the Na/K ATPase will have it's most rapid activity after a depolarization. (I know, duh!) The important thing to remember is that there are K leak channels, but the flow is very small. So, Imagine that your Na/K pumps have just repolarized a neuron by puming 3 Na out, and 2 K in until you see that potential (or whatever it is).
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The Na,K-ATPase consists of an α- and β-subunit. Moloney sarcoma virus-transformed MDCK cells (MSV-MDCK) express low levels of Na,K-ATPase β c expression of Na,K-ATPase β 1-subunit in these cells increased the protein levels of the α 1-subunit of Na, increase was not due to altered transcription of the α 1-subunit gene or half-life of the α 1-subunit protein.
Na⁺/K⁺ ATPase Ü Subunit and Ü Subunit mRNA levels in preimplantation mouse and rabbit embryos by Catherine S. Gardiner 2 editions - first published in Not in Library. Renal cortex Na+,K+-ATPase activity was higher in placebo-treated adults and newborns than fetuses.
Cerebral cortex Na+,K+-ATPase activity was higher in dexamethasone- than placebo-treated adults, and α1-expression higher in fetuses of dexamethasone- than placebo-treated ewes at 60% and 80% by: 3.
The main finding of the present study is that mRNA levels of the Na +:K +:ATPase α 1-subunit in the renal cortex and outer and inner medulla did not change during modifications of salt intake or administration of the loop diuretic, furosemide, from 1 to 7 by: 3.
Expression of Na/K-ATPase subunits in the human cochlea: a confocal and super-resolution microscopy study with special reference to auditory nerve excitation and cochlear implantation.
Upsala Journal of Medical Sciences: Vol. No. 3, pp. Author: Wei Liu, Maria Luque, Rudolf Glueckert, Niklas Danckwardt-Lillieström, Charlotta Kämpfe Nordström, A. Introduction. The Na,K‐ATPase is a ubiquitous cation pump of the plasma membrane that uses the energy of ATP hydrolysis to transport Na + ions out of and K + ions into the cell.
The resulting Na + gradient provides the energy for the transport activity of other transporters involved in basic and specialized cellular functions (for review, see Horisberger, ).Cited by: 1.
Introduction. The Na + /K +-ATPase enzyme is a transmembrane heterodimer composed of two α-subunits (ca kDa) and two β-subunits (ca 40 kDa).The α-subunits are the catalytic components containing an intracellular ATP binding site, a phosphorylation site, and an extracellular site where ouabain, a highly specific inhibitor, binds (Skou and Esmann, ).Cited by: 5.
Na(+), K(+)-ATPase: the new face of an old player in pathogenesis and apoptotic/hybrid cell death Article Literature Review in Biochemical Pharmacology 66(8) November with 49 Reads. Na⁺/K⁺-ATPase is an enzyme found in the membrane of all animal cells.
It performs several functions in cell physiology. The Na+ /K+ -ATPase enzyme is active. For every ATP molecule that the pump uses, three sodium ions are exported and two potassium ions are imported; there is hence a net export of a single positive charge per pump cycle.
The sodium–potassium pump was discovered in by the BRENDA: BRENDA entry. It has been believed that inhibition of the Na,K-ATPase in cardiomyocytes raises cytoplasmic sodium levels, thereby inhibiting the sodium-calcium exchanger and raising cytoplasmic calcium levels, which is imagined to have a direct effect on the heart's contractility, but there is also evidence to suggest that digitalis strengthens the parasympathetic nervous system by Cited by: Na +/K -ATPase is an ion pump that translocates Na and K ions against the electrochemical gradients across the plasma membrane (Skou, ).
The enzyme is composed of a large catalytic subunit (α-subunit), a membrane-spanning auxiliary subunit (β-subunit) and a small regulatory subunit (γ-subunit). The α-subunit contains theCited by: Since Na,K-ATPase β 1 can function as a cell–cell adhesion molecule and loss of adhesion molecules may lead to EMT we next tested whether knockdown of the β 1 subunit can induce EMT in ARPE cells.
Using a shRNA approach Na⁺/K⁺ ATPase Ü Subunit and Ü Subunit mRNA levels in preimplantation mouse and rabbit embryos book selected three stable Na,K-ATPase β 1 knockdown clones, Na,K-β 1 KD clone 8, 9 which expressed 77%, 64% and 4% of the β 1-subunit compared to cells Cited by: The -subunit of Na-K-ATPase is incorporated into plasma membranes of mouse IMCD3 cells in response to hypertonicity Kaarina Pihakaski-Maunsbach,1 Shigeki Tokonabe,1 Henrik Vorum,2 Christopher J.
Rivard,3 Juan M. Capasso,3 Tomas Berl,3 and Arvid B. Maunsbach1 1The Water and Salt Research Center, Department of Cell Biology, Institute of Anatomy, and 2InstituteCited by: The Na,K-ATPase is an αβ heterodimer responsible for maintaining fluid and electrolyte homeostasis in mammalian cells.
We engineered Madin-Darby canine kidney cell lines expressing α 1 FLAG, β 1 FLAG, or β 2 MYC subunits via a tetracycline-regulated promoter and a line expressing both stable β 1 MYC and tetracycline-regulated β 1 FLAG to examine regulatory mechanisms of sodium Cited by: 6.
The Na,K-ATPase classically serves as an ion pump creating an electrochemical gradient across the plasma membrane that is essential for transepithelial transport, nutrient uptake and membrane potential.
In addition, Na,K-ATPase also functions as a receptor, a signal transducer and a Cited by: The vital gradients of Na+ and K+ across the plasma membrane of animal cells are maintained by the Na,K-ATPase, an αβ enzyme complex, whose α subunit Cited by: The band corresponding to the Na,K ATPase-subunit (96 kDa) is indicated by the arrows on the left.
(A) Total ouabain-sensitive Na,K-ATPase activity is elevated in CHO cells expressing the PC Role of Na,K-ATPase a1 and a2 Isoforms in the Support of Astrocyte Glutamate Uptake Nina B.
Illarionava1, Hjalmar Brismar1,2, Anita Aperia1, Eli Gunnarson1* 1Department of Women’s and Children’s Health, Karolinska Institutet, Stockholm, Sweden, 2Science for Life Laboratory, Department of Cell Physics, Royal Institute of.
Expression of Na + /K +-ATPase α subunit isoforms in rat salivary glands: (pH ) containing % hydrogen peroxide.
As a control, the primary antibody was substituted by preimmune-rabbit or mouse serum. Western blot analysis We examined the mRNA levels of Na + /K +-ATPase α subunit isoforms in various tissues of rat.
α1 mRNA Cited by: 4. Synthesis of the Na-K-ATPase -subunit is regulated at both the transcriptional and translational levels in IMCD3 cells Juan M. Capasso, Christopher J. Rivard, and Tomas Berl University of Colorado Health Sciences Center, Division of Renal Diseases and Hypertension, School of Medicine, Denver, ColoradoCited by: Localization of the Na,K-ATPase β 2 subunit in nerve sections is similar to that of the Na,K-ATPase α 2 subunit, but not of the Na,K-ATPase α 1 subunit or β 1 subunit.
A, frozen sections of rat sciatic nerve were double stained by using mouse antibodies against α 1 subunit (green) and either rabbit antibodies against α 2 subunit (red Cited by: Mouse preimplantation embryo responses to culture medium osmolarity include increased expression of CCM2 and p38 MAPK Available via license: CC BY Content may be subject to.
This review summarizes our experiments on the significance of the β-subunit in the functional expression of Na + /K + β-subunit acts like a receptor for the α-subunit in the biogenesis of Na + /K +-ATPase and facilitates the correct folding of the α-subunit in the α-subunit synthesized in the absence of the β-subunit is subjected to rapid degradation in the Cited by: ELSEVIER Neuroscience Letters () H[UROSH[ LETTERS Na,K-ATPase/3 subunit isoform expression in the peripheral nervous system of the rat David J.
Fink*, DaNan Fang, TieDong Li, Marina Mata Department of Neurology, University of Michigan and GRECC, VAMC, Ann Arbor, MI, USA Received 25 July ; revised version received 4 November ; accepted 4 November Cited by: Abstract.
Assembly of catalytic α-subunits of Na +,K +-ATPase with β-subunits is a prerequisite for the structural and functional maturation of newly synthesized α-subunit and its intracellular transport from the ER to the plasma membrane (2).Little is known on the structural domains in α- and β-subunits that are involved in subunit : A.
Beggah, P. Beguin, P. Jaunin, M. Peitsch, K. Geering. The γ subunit of the Na,K-ATPase is a small, single transmembrane protein (mass ≈ 7 kDa) expressed primarily in renal tissue, in approximately equimolar amounts compared with the α and β subunits ().It has substantial homology to CHIF (corticosteroid-induced factor) (), mat 8 (), and phospholemman (), which have similar trans-membrane organization (C terminus in, N terminus out).
Sodium/potassium-transporting ATPase subunit betainteracting protein 2 Add BLAST: The sodium/potassium-transporting ATPase is composed of a catalytic alpha subunit, an auxiliary non-catalytic beta subunit and an additional regulatory subunit.
Interacts with regulatory subunit FXYD1 (PubMed, PubMed, PubMed). Interacts with regulatory subunit FXYD3 (PubMed). Both Na +,K +-ATPase and H +,K +-ATPase belong to the family of P-type ATPases, which transport ions across the plasma membrane ().The Na +,K +-ATPase is found in almost all animal cells and is essential for the maintenance of cellular ion gradients, whereas the gastric H +,K +-ATPase is located in parietal cells of the gastric mucosa, where it is responsible for acid secretion by the.
Molecules22, 2 of 20 U.S. scientists in red blood cells [14–16]. Finally, cardiac glycosides were found to be speciﬁc inhibitors of such active transport in red blood cells , and the requirement of ATP for K+ uptake in these cells further supported and linked the transport system to membrane-bound ATPase sensitive to cardiacCited by: Low magnification images of the same fields are shown in the far right panels.
C, the Na,K-ATPase 1 subunit, like YFP-1, is resistant to extraction by Triton X and is co-localized with YFP The sodium/potassium-transporting ATPase is composed of a catalytic alpha subunit, an auxiliary non-catalytic beta subunit and an additional regulatory subunit.
Interacts with regulatory subunit FXYD1 (By similarity). Interacts with regulatory subunit FXYD3 (PubMed). Interacts with SIK1 (By. There are multiple isoforms of the Na,K-ATPase in the nervous system, three isoforms of the α subunit, and at least two of the β subunit. The α subunit is the catalytic subunit.
The β subunit has several roles. It is required for enzyme assembly, it has been implicated in neuron-glia adhesion, and the experimental exchange of β subunit isoforms modifies enzyme kinetics, implying that it Cited by: In contrast, ectopic expression of both E-cadherin and Na,K-ATPase β 1-subunit in MSV-MDCK cells induced junctional complexes, reestablished epithelial polarity, and suppressed invasiveness and motility, indicating that Na,K-ATPase β 1-subunit function is necessary for induction of a polarized phenotype and invasion suppression of MSV-MDCK cells.
including that of Na/K-ATPase a 3 subunit, in cultured neonatal rat cardiac myocytes. The aim of this work was to determine whether ouabain and other hypertrophic stimuli affect Na/K-ATPase b 1 subunit gene expression. When myocytes were ex-posed to non-toxic concentrations of ouabain, ouabain increased b 1 subunit mRNA in a dose- and time.
Abstract. Based on recent data showing that overexpression of the Na,K-ATPase β 1 subunit increased cell-cell adhesion of nonpolarized cells, we hypothesized that the β 1 subunit can also be involved in the formation of cell-cell contacts in highly polarized epithelial cells.
In support of this hypothesis, in Madin-Darby canine kidney (MDCK) cells, the Na,K-ATPase α 1 and β 1 subunits were Cited by: International Journal of Molecular Sciences Article K+ and Rb+ Afﬁnities of the Na,K-ATPase 1 and 2 Isozymes: An Application of ICP-MS for Quantiﬁcation of Na+ Pump Kinetics in Myoﬁbers Hesamedin Hakimjavadi 1, Cory A.
Stiner 1,2,3, Tatiana L. Radzyukevich 1, Jerry B. Lingrel 4, Natalie Norman 1, Julio A. Landero Figueroa 1,2,3 and Judith A. Heiny 1,* 1 Department of Pharmacology and Cited by: 1. Entry name i: NKAI2_HUMAN: Accession i: Q5VXU1 Primary (citable) accession number: Q5VXU1 Secondary accession number(s): Q8IYR4, Q8TF Entry history i: Integrated into UniProtKB/Swiss-Prot:: Decem Last sequence update:: December 7, Last modified:: Ap This is version of the entry and version 1 of the sequence.
See complete history.: Entry status i. Expression of the a-subunit of Na/K-ATPase in renal collecting duct epithelium during development. Aldosterone enhances synthesis and enzyme activity of NaJK-ATPase and has been found to stimulate sodium reabsorption by the renal cortical collecting duct.
Moreover, chronic exposure to aldosterone is associated with a remarkable. Quantitative Na, K-ATPase receptor catalytic subunit α1, α2 and α3 mRNA expression was determined by solution hybridization. No cross-reactivity occurred between the three probes.
α1 mRNA was expressed at about 5 and 10 times higher (pmRNA, respectively, and α2 mRNA higher (pCited by: 5.
Acute lung injury (ALI) and acute respiratory distress syndrome (ARDS) are characterized by acute respiratory failure and associated with diverse disorders. Gene therapy is a potentially powerful approach to treat ALI and ARDS through repair of alveolar epithelial function.
We previously showed that electroporation-mediated gene transfer of the b1 subunit of the Na,K-ATPase to the lung not Author: Xin Lin, Michael Barravecchia, David A. Dean. The α and β subunits of Na-K-ATPase are up-regulated by hypertonicity in inner-medullary collecting duct cells adapted to survive in hypertonic conditions.
We examined the regulation of the γ subunit by hypertonicity. Although cultured inner-medullary collecting duct cells lacked the γ subunits, both variants γa and γb were expressed in cells adapted to and mosmol/ by: During the normal catalytic cycle of the Na,K-ATPase, the alpha-subunit is transiently phosphorylated by ATP at an aspartate residue.
This phosphorylation requires Na+, in the presence of K+ the enzyme undergoes rapid dephosphorylation. In contrast, phosphorylation of the independent alpha-subunit by ATP occurs in the presence of Mg2+, does not.