Cargando…

K(+) and Rb(+) Affinities of the Na,K-ATPase α(1) and α(2) Isozymes: An Application of ICP-MS for Quantification of Na(+) Pump Kinetics in Myofibers

The potassium affinities of Na,K-ATPase isozymes are important determinants of their physiological roles in skeletal muscle. This study measured the apparent K(+) and Rb(+) affinities of the Na,K-ATPase α(1) and α(2) isozymes in intact, dissociated myofibers obtained from WT and genetically altered...

Descripción completa

Detalles Bibliográficos
Autores principales:	Hakimjavadi, Hesamedin, Stiner, Cory A., Radzyukevich, Tatiana L., Lingrel, Jerry B., Norman, Natalie, Landero Figueroa, Julio A., Heiny, Judith A.
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	MDPI 2018
Materias:	Article
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6165224/ https://www.ncbi.nlm.nih.gov/pubmed/30213059 http://dx.doi.org/10.3390/ijms19092725

Ejemplares similares

Na,K-ATPase α2 activity in mammalian skeletal muscle T-tubules is acutely stimulated by extracellular K(+)
por: DiFranco, Marino, et al.
Publicado: (2015)

Metal ion transport quantified by ICP-MS in intact cells
por: Figueroa, Julio A. Landero, et al.
Publicado: (2016)

Na,K-ATPase Isozymes in Colorectal Cancer and Liver Metastases
por: Baker Bechmann, Marc, et al.
Publicado: (2016)

β subunit affects Na(+) and K(+) affinities of Na(+)/K(+)-ATPase: Na(+) and K(+) affinities of a hybrid Na(+)/K(+)-ATPase composed of insect α and mammalian β subunits
por: Homareda, Haruo, et al.
Publicado: (2022)

Anti–Na(+)/K(+)-ATPase immunotherapy ameliorates α-synuclein pathology through activation of Na(+)/K(+)-ATPase α1–dependent autophagy
por: Cao, Lei, et al.
Publicado: (2021)

Na(+)/Ca(2+) exchange and Na(+)/K(+)-ATPase in the heart
por: Shattock, Michael J, et al.
Publicado: (2015)

The α(2) Na(+)/K(+)-ATPase isoform mediates LPS-induced neuroinflammation
por: Leite, J. A., et al.
Publicado: (2020)

Cardiac Oxidative Signaling and Physiological Hypertrophy in the Na/K-ATPase α1(s/s)α2(s/s) Mouse Model of High Affinity for Cardiotonic Steroids
por: Marck, Pauline V., et al.
Publicado: (2021)

Distinct α2 Na,K-ATPase membrane pools are differently involved in early skeletal muscle remodeling during disuse
por: Kravtsova, Violetta V., et al.
Publicado: (2016)

Protein Carbonylation of an Amino Acid Residue of the Na/K‐ATPase α1 Subunit Determines Na/K‐ATPase Signaling and Sodium Transport in Renal Proximal Tubular Cells
por: Yan, Yanling, et al.
Publicado: (2016)

Role of Na,K-ATPase α1 and α2 Isoforms in the Support of Astrocyte Glutamate Uptake
por: Illarionava, Nina B., et al.
Publicado: (2014)

Kinetics of Na-ATPase activity by the Na,K pump. Interactions of the phosphorylated intermediates with Na+, Tris+, and K+
Publicado: (1983)

The Role of Na,k-Atpase α Subunit Serine 775 and Glutamate 779 in Determining the Extracellular K(+)And Membrane Potential–Dependent Properties of the Na,k -Pump
por: Peluffo, R. Daniel, et al.
Publicado: (2000)

Flexible selection of diversified Na(+)/K(+)-ATPase α-subunit isoforms for osmoregulation in teleosts
por: Wong, Marty Kwok-Shing, et al.
Publicado: (2016)

Na(+)/K(+)-ATPase α isoform deficiency results in distinct spreading depolarization phenotypes
por: Reiffurth, Clemens, et al.
Publicado: (2019)

Genetic Ablation of Na,K-ATPase α4 Results in Sperm Energetic Defects
por: Numata, September, et al.
Publicado: (2022)

Transcriptional regulators of Na,K-ATPase subunits
por: Li, Zhiqin, et al.
Publicado: (2015)

Ultrastructure of Na,K-transport vesicles reconstituted with purified renal Na,K-ATPase
Publicado: (1980)

Na/K Pump and Beyond: Na/K-ATPase as a Modulator of Apoptosis and Autophagy
por: Felippe Gonçalves-de-Albuquerque, Cassiano, et al.
Publicado: (2017)

Correction: Role of Na,K-ATPase α1 and α2 Isoforms in the Support of Astrocyte Glutamate Uptake
Publicado: (2014)

Isoform-Specific Na,K-ATPase Alterations Precede Disuse-Induced Atrophy of Rat Soleus Muscle
por: Kravtsova, Violetta V., et al.
Publicado: (2015)

Electrogenic Sodium–Sodium Exchange Carried Out by Na,k -Atpase Containing the Amino Acid Substitution Glu779ala
por: Peluffo, R. Daniel, et al.
Publicado: (2000)

Sodium Kinetics of Na,K-ATPase α Isoforms in Intact Transfected HeLa Cells
por: Zahler, Raphael, et al.
Publicado: (1997)

Na(+)/K(+)-ATPase α1 subunit, a novel therapeutic target for hepatocellular carcinoma
por: Zhuang, Liping, et al.
Publicado: (2015)

Cognitive deficits caused by a disease-mutation in the α(3) Na(+)/K(+)-ATPase isoform
por: Holm, Thomas Hellesøe, et al.
Publicado: (2016)

A metabolic link between the astrocytic α2-Na/K ATPase and episodic paralysis
por: Inglis, George Andrew S.
Publicado: (2021)

Na+ and K+ transport at basolateral membranes of epithelial cells. I. Stoichiometry of the Na,K-ATPase
Publicado: (1986)

C-peptide, Na(+),K(+)-ATPase, and Diabetes
por: Vague, P., et al.
Publicado: (2004)

Tuning of the Na,K-ATPase by the beta subunit
por: Hilbers, Florian, et al.
Publicado: (2016)

Na(+), K(+)-ATPase Signaling and Bipolar Disorder
por: Lichtstein, David, et al.
Publicado: (2018)

Na/K-ATPase and Regulation of Sperm Function
por: Thundathil, Jacob C., et al.
Publicado: (2018)

The role of Na(+)‐K(+)‐ATPase in the epileptic brain
por: Sun, Jinyi, et al.
Publicado: (2022)

Na+ and K+ transport at basolateral membranes of epithelial cells. II. K+ efflux and stoichiometry of the Na,K-ATPase
Publicado: (1986)

A real-time PCR method to genotype mutant mouse models with altered affinity for cardiotonic steroids on the Na,K-ATPase
por: Chomczynski, Peter W., et al.
Publicado: (2022)

The Na(+), K(+)-ATPase β1 subunit regulates epithelial tight junctions via MRCKα
por: Bai, Haiqing, et al.
Publicado: (2021)

Ouabain-Induced Cell Death and Survival. Role of α1-Na,K-ATPase-Mediated Signaling and [Na(+)](i)/[K(+)](i)-Dependent Gene Expression
por: Lopina, Olga Dmitrievna, et al.
Publicado: (2020)

Tumor-Suppressor Role of the α1-Na/K-ATPase Signalosome in NASH Related Hepatocellular Carcinoma †
por: Udoh, Utibe-Abasi S., et al.
Publicado: (2022)

Basal Glutathionylation of Na,K-ATPase α-Subunit Depends on Redox Status of Cells during the Enzyme Biosynthesis
por: Mitkevich, Vladimir A., et al.
Publicado: (2016)

Effect of Reduction of Redox Modifications of Cys-Residues in the Na,K-ATPase α1-Subunit on Its Activity
por: Dergousova, Elena A., et al.
Publicado: (2017)

Glutamate Water Gates in the Ion Binding Pocket of Na(+) Bound Na(+), K(+)-ATPase
por: Han, Minwoo, et al.
Publicado: (2017)

Cannot write session to /tmp/vufind_sessions/sess_l1lj3lp6fsqepe9d336a1oh11q