An Ultra-Low Modulus of Ductile TiZrHfTa Biomedical High-Entropy Alloys through Deformation Induced Martensitic Transformation/Twinning/Amorphization.

Biomedical alloys are paramount materials in biomedical applications, particularly in crafting biological artificial replacements. In traditional biomedical alloys, a significant challenge is simultaneously achieving an ultra-low Young's modulus, excellent biocompatibility, and acceptable ductility. A multi-component body-centered cubic (BCC) biomedical high-entropy alloy (Bio-HEA), which is composed of non-toxic elements, is noteworthy for its outstanding biocompatibility and compositional tuning capabilities.

Pharmacological suppression of Nedd4-2 rescues the reduction of Kv11.1 channels in pathological cardiac hypertrophy.

The human gene (hERG) encodes the pore-forming subunit (Kv11.1), conducting a rapidly delayed rectifier K current ( ). Reduction of in pathological cardiac hypertrophy (pCH) contributes to increased susceptibility to arrhythmias.

Inhibitory G-protein-mediated modulation of slow delayed rectifier potassium channels contributes to increased susceptibility to arrhythmogenesis in aging heart.

Background: Slow delayed rectifier potassium current (I) is an important component of repolarization reserve during sympathetic nerve excitement. However, little is known about age-related functional changes of I and its involvement in age-dependent arrhythmogenesis.

Objective: The purpose of this study was to investigate age-related alteration of the I response to β-adrenergic receptor (βAR) activation.

Protein kinase C epsilon mediates the inhibition of angiotensin II on the slowly activating delayed-rectifier potassium current through channel phosphorylation.

The slowly activating delayed rectifier K current (I) is one of the main repolarizing currents in the human heart. Evidence has shown that angiotensin II (Ang II) regulates I through the protein kinase C (PKC) pathway, but the related results are controversial. This study was designed to identify PKC isoenzymes involved in the regulation of I by Ang II and the underlying molecular mechanism.