ArticleThe Journal of biological chemistry2009
Agrin regulation of alpha3 sodium-potassium ATPase activity modulates cardiac myocyte contraction.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 32 citations in OpenAlex.
- Article
- Post-translational modifications of na+/K+-atpase subunits: regulatory mechanisms and functional implications.Frontiers in cell and developmental biology · 2026Review
- Clinical rationale for dietary lutein supplementation in long COVID and mRNA vaccine injury syndromes.F1000Research · 2024Review
- Article
- Identification of two variants inClinical case reports · 2022Article
- Determination of Agrin and Related Proteins Levels as a Function of Age in Human Hearts.Frontiers in cardiovascular medicine · 2022Article
- Article
- Basic Biology of Extracellular Matrix in the Cardiovascular System, Part 1/4: JACC Focus Seminar.Journal of the American College of Cardiology · 2020Review
- Profiling of the muscle-specific dystroglycan interactome reveals the role of Hippo signaling in muscular dystrophy and age-dependent muscle atrophy.BMC medicine · 2020Article
- Preconditioning and Postconditioning by Cardiac Glycosides in the Mouse Heart.Journal of cardiovascular pharmacology · 2018Article
- The expanding spectrum of neurological phenotypes in children with ATP1A3 mutations, Alternating Hemiplegia of Childhood, Rapid-onset Dystonia-Parkinsonism, CAPOS and beyond.Pediatric neurology · 2015Review
- Extracellular matrix and heart development.Birth defects research. Part A, Clinical and molecular teratology · 2011Review
- A structural overview of the plasma membrane Na+,K+-ATPase and H+-ATPase ion pumps.Nature reviews. Molecular cell biology · 2011Review
- New role for Agrin in T cells and its potential importance in immune system regulation.Arthritis research & therapy · 2010Review
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Drugs that inhibit Na,K-ATPases, such as digoxin and ouabain, alter cardiac myocyte contractility. We recently demonstrated that agrin, a protein first identified at the vertebrate neuromuscular junction, binds to and regulates the activity of alpha3 subunit-containing isoforms of the Na,K-ATPase in the mammalian brain. Both agrin and the alpha3 Na,K-ATPase are expressed in heart, but their potential for interaction and effect on cardiac myocyte function was unknown. Here we show that agrin binds to the alpha3 subunit of the Na,K-ATPase in cardiac myocyte membranes, inducing tyrosine phosphorylation and inhibiting activity of the pump. Agrin also triggers a rapid increase in cytoplasmic Na(+) in cardiac myocytes, suggesting a role in cardiac myocyte function. Consistent with this hypothesis, spontaneous contraction frequencies of cultured cardiac myocytes prepared from mice in which agrin expression is blocked by mutation of the Agrn gene are significantly higher than in the wild type. The Agrn mutant phenotype is rescued by acute treatment with recombinant agrin. Furthermore, exposure of wild type myocytes to an agrin antagonist phenocopies the Agrn mutation. These data demonstrate that the basal frequency of myocyte contraction depends on endogenous agrin-alpha3 Na,K-ATPase interaction and suggest that agrin modulation of the alpha3 Na,K-ATPase is important in regulating heart function.
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Registered trials
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