Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Essential Opposite Roles of ERK and Akt Signaling in Cardiac Steroid-Induced Increase in Heart Contractility.

The Journal of pharmacology and experimental therapeutics - 1 May 2016

Buzaglo Nahum, Rosen Haim, Ben Ami Hagit Cohen, Inbal Adi, Lichtstein David

Abstract excerpt

Interaction of cardiac steroids (CS) with the Na(+), K(+)-ATPase elicits, in addition to inhibition of the enzyme's activity, the activation of intracellular signaling such as extracellular signal-regulated (ERK) and protein kinase B (Akt). We hypothesized that the activities of these pathways are involved in CS-induced increase in heart contractility. This hypothesis was tested using in vivo and ex vivo wild...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Calcium Signaling
Share to Cardiotonic Agents

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Mitogen-Activated Protein Kinases

Share to Myocardial Contraction

Share to Myocytes, Cardiac

Share to Oncogene Protein v-akt

Share to Sarcoplasmic Reticulum Calcium-Transporting ATPases

Share to Steroids

Source

Identifiers

PMID: 26941172
DOI: 10.1124/jpet.115.230763

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Essential Opposite Roles of ERK and Akt Signaling in Cardiac Steroid-Induced Increase in Heart Contractility.PMID 26941172Read ↗

Cardiac-specific overexpression of a high Ca2+ affinity mutant of SERCA2a attenuates in vivo pressure overload cardiac hypertrophy.Semantic proximity Read ↗

Cardiac β2-Adrenergic Receptor Phosphorylation at Ser355/356 Regulates Receptor Internalization and Functional Resensitization.Semantic proximity Read ↗

PKCepsilon-PKD1 signaling complex at Z-discs plays a pivotal role in the cardiac hypertrophy induced by G-protein coupling receptor agonists.Semantic proximity Read ↗

The alpha2 isoform of Na,K-ATPase mediates ouabain-induced cardiac inotropy in mice.Semantic proximity Read ↗

Ca(2+)-sensitive tyrosine kinase Pyk2/CAK beta-dependent signaling is essential for G-protein-coupled receptor agonist-induced hypertrophy.Semantic proximity Read ↗

(-)-Adrenaline elicits positive inotropic, lusitropic, and biochemical effects through beta2 -adrenoceptors in human atrial myocardium from nonfailing and failing hearts, consistent with Gs coupling but not with Gi coupling.Semantic proximity Read ↗

A novel interaction mechanism accounting for different acylphosphatase effects on cardiac and fast twitch skeletal muscle sarcoplasmic reticulum calcium pumps.Semantic proximity Read ↗

PKCdelta mediates testosterone-induced increases in coronary smooth muscle Cav1.2.Semantic proximity Read ↗

Dichloroacetate selectively improves cardiac function and metabolism in female and male rainbow trout.Semantic proximity Read ↗

accordion, a zebrafish behavioral mutant, has a muscle relaxation defect due to a mutation in the ATPase Ca2+ pump SERCA1.Semantic proximity Read ↗

A novel protein kinase A-independent, beta-arrestin-1-dependent signaling pathway for p38 mitogen-activated protein kinase activation by beta2-adrenergic receptors.Semantic proximity Read ↗

The alpha(1)-adrenoceptor subtype- and protein kinase C isoform-dependence of Norepinephrine's actions in cardiomyocytes.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.