The highly conserved, cardiotonic steroid binding site (also termed ouabain binding site) on the primary α subunit of Na,K-ATPase plays a receptor signaling role in a range of vital cell processes and is a therapeutic target for human disease. Mouse lines with altered affinity for cardiotonic steroids on the α1 or α2 subunit isoform of Na,K-ATPase, without any change in pump activity, were developed by the late Jerry B Lingrel and are a valuable tool for studying its physiological roles and drug actions. In one model, the normally ouabain resistant α1 isoform was rendered sensitive to ouabain binding. In a second model, the normally sensitive α2 isoform was rendered resistant to ouabain binding. Additional useful models are obtained by mating these mice. To further advance their use, we developed a rapid, real-time PCR method that detects mutant alleles using specific primers and fluorescent probes. PCR is performed in fast mode with up to 15 samples processed in 40 min. The method was validated by Sanger sequencing using mice of known genotype, and by comparing results with a previous two-step method that used PCR amplification followed by gel electrophoresis. In addition, we clarified inconsistencies in published sequences, updated numbering to current reference sequences, and confirmed the continued presence of the mutations in the colony. It is expected that a wider availability of these models and a more efficient genotyping protocol will advance studies of the Na,K-ATPase and its cardiotonic steroid receptor.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9022855PMC
http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0267348PLOS

Publication Analysis

Top Keywords

ouabain binding
12
real-time pcr
8
pcr method
8
altered affinity
8
affinity cardiotonic
8
cardiotonic steroids
8
cardiotonic steroid
8
binding site
8
isoform rendered
8
method
4

Similar Publications

Na,K-ATPase is the active ion transport system that maintains the electrochemical gradients for Na and K across the plasma membrane of most animal cells. Na,K-ATPase is constituted by the association of two major subunits, a catalytic α and a glycosylated β subunit, both of which exist as different isoforms (in mammals known as α1, α2, α3, α4, β1, β2 and β3). Na,K-ATPase α and β isoforms assemble in different combinations to produce various isozymes with tissue specific expression and distinct biochemical properties.

View Article and Find Full Text PDF
Article Synopsis
  • - The study examined how the Na,K-ATPase inhibitor digoxin affects muscle content, potassium levels, and fatigue during intense exercise in healthy adults, using a double-blind crossover design with a placebo.
  • - Results showed that while muscle Na,K-ATPase binding increased with digoxin treatment, muscle isoform levels did not change, suggesting a potential adaptation mechanism to maintain Na,K-ATPase function despite the drug's effects.
  • - Exercise produced significant shifts in potassium levels, with digoxin leading to earlier fatigue and altered potassium responses compared to the placebo, highlighting digoxin's impact on muscle performance during high-intensity activities.
View Article and Find Full Text PDF

Role of Na-K ATPase Alterations in the Development of Heart Failure.

Int J Mol Sci

October 2024

Department of Pharmacology and Toxicology, Faculty of Pharmacy, Comenius University, 83232 Bratislava, Slovakia.

Article Synopsis
  • - Na-K ATPase is crucial for heart function, consisting of three subunits that help transport sodium and potassium ions, maintaining the balance of these cations in heart cells and influencing heart contractions.
  • - This enzyme also acts as a receptor for certain glycosides and steroids, regulating heart metabolism and cell survival, with its activity affected by various hormones through modifications of its associated protein, phospholemman.
  • - In heart failure, Na-K ATPase activity can change in different ways, leading to either adaptive mechanisms for maintaining function or issues like calcium overload and arrhythmias, ultimately impacting heart health based on the enzyme's isoform composition and oxidative stress.
View Article and Find Full Text PDF

Kinetic properties of gill (Na, K)-ATPase in the Pacific whiteleg shrimp Penaeus vannamei (Decapoda, Penaeidae).

Comp Biochem Physiol B Biochem Mol Biol

January 2025

Departamento de Química, Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto, Universidade de São Paulo, Ribeirão Preto, Brazil. Electronic address:

Article Synopsis
  • Penaeus vannamei is a rapidly growing shrimp species native to the Eastern Pacific, now found in tropical waters of Asia and the Americas, notable for its adaptability and disease resistance.
  • Research focused on its osmoregulatory mechanisms highlights the role of the enzyme (Na, K)-ATPase, which is crucial for maintaining ionic balance, yet its modulation by different ligands is poorly understood.
  • This study identifies important kinetic properties of the (Na, K)-ATPase in P. vannamei, revealing differences in enzyme behavior compared to other crustaceans, potentially aiding in understanding how these shrimp adapt to diverse salinity environments.
View Article and Find Full Text PDF

Antifungal metabolites of biocontrol stain LB-1 and their inhibition mechanism against .

Front Microbiol

September 2024

University Characteristic Laboratory of Precision Cultivation and Germplasm Innovation of Horticultural Crops in Shandong, School of Advanced Agricultural Sciences, Weifang University, Weifang, Shandong, China.

Introduction: LB-1 is a novel biocontrol strain that produces non-volatile metabolites that inhibit the growth of . However, the specific metabolites and antimicrobial mechanism of the strain LB-1 remains unclear.

Methods: In this study, the antifungal substances produced by strain LB-1, as well as the underlying mechanism of its inhibitory effect against , were explored using metabolomic and transcriptomic analysis.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!