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Potassium channels are present in most mammalian cells, where they participate in a wide range of physiologic responses. Additionally we are shipping KCNJ2 Antibodies (94) and many more products for this protein.
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We report a novel KCNJ2 sequence variant (p.Y145C) in a family with diagnosed Andersen-Tawil syndrome.
Combined inhibition of IKr and IKur produced a synergistic anti-arrhythmic effect in both forms of SQT3. In conclusion, this study provides mechanistic insights into atrial proarrhythmia with SQT3 Kir2.1 mutations and highlights possible pharmacological strategies for management of SQT3-linked AF.
Data suggest that an R204A mutation disrupts the characteristic cytoplasmic domain subunit interface salt bridges in Kir2.1 reducing apparent sensitivity of channel activity to ligand PIP2 (phosphatidylinositol bisphosphate).
These findings suggest that KCNJ2 plays an important role in the pathophysiology of Thyrotoxic Periodic Paralysis in Korean Graves' Disease patients with Thyrotoxic Periodic Paralysis .
Nav1.5 (show SCN5A Proteins) N-terminal domain binding to alpha1-syntrophin (show SNTA1 Proteins) increases membrane density of human Kir2.1, Kir2.2 (show KCNJ12 Proteins) and Nav1.5 (show SCN5A Proteins) channels
Kir2.1 may participate in macrophage maturation and differentiation, and play a key role in lipid uptake and foam cell formation through modulating the expression of scavenger receptors.
a Korean family with Andersen-Tawil syndrome with a G215D mutation of the KCNJ2 gene revealed by diagnostic exome sequencing, is reported.
Chloroethylclonidine interact with Kir2.1 channels in the cytoplasmic pore.
Variability has been found in a three-generation family with Pierre Robin sequence, acampomelic campomelic dysplasia, and intellectual disability due to a novel approximately 1 Mb deletion upstream of SOX9 (show SOX9 Proteins), and including KCNJ2 and KCNJ16 (show KCNJ16 Proteins).
Patients with Dilated Cardiomyopathy and Sustained Monomorphic Ventricular Tachycardia Show Up-Regulation of KCNN3 and KCNJ2 Genes and CACNG8-Linked Left Ventricular Dysfunction
Following differentiation with LPS (show TLR4 Proteins) or a combination of LPS (show TLR4 Proteins) and IFN-gamma (show IFNG Proteins) microglia exhibited high KV 1.3 current densities ( approximately 50 pA/pF at 40 mV) and virtually no KCa (show CSN3 Proteins) 3.1 and Kir (show GEM Proteins) currents, while microglia differentiated with IL-4 (show IL4 Proteins) exhibited large Kir (show GEM Proteins) 2.1 currents ( approximately 10 pA/pF at -120 mV). KCa (show CSN3 Proteins) 3.1 currents were generally low
Cellular electrophysiology assays of mouse Kir2.1 and human Kir2.2 indicated that, consistent with simulations, the Leu residue increased the channel responses to phosphatidylinositol diphosphate (PIP2) through increased binding affinity and faster activation kinetics, and the deactivation kinetics decreased upon PIP2 inhibition.
histone H4 hyperacetylation induced by Class I HDACs inhibitors promoted the expression profiles of potassium channels (Kcnj2, Kcnj3 (show KCNJ3 Proteins), Kcnj5 (show KCNJ5 Proteins), Kcnj11 (show KCNJ11 Proteins), and Kcnh2 (show KCNH2 Proteins))
Our results support the concept that endothelial cell Kir2 channels boost vasodilatory signals that are generated by Ca(2 (show CA2 Proteins)+) -dependent activation of IK and SK channels.
Results suggest that a promyogenic cell adhesion molecule (show MCAM Proteins) Cdo (show CDO1 Proteins) signaling is critical for Inward rectifier potassium channel Kir2.1 activities in the induction of myogenic differentiation.
The data suggest that microglial Kir2.1 channels may represent novel therapeutic targets to inhibit excessive reactive oxygen species production by primed microglia in brain pathology.
Three pairs of weak interactions precisely regulate the G-loop gate of Kir2.1 channel.
Suggest that Kir2.1 channels, in part, account for hyperpolarization and associated absence of tone in urinary bladder arterioles.
This finding represents the first functional evidence for a significant role of the dystrophin (show DMD Proteins)-associated protein complex in the regulation of Kir2.x channels.
Intracellular Mg(2 (show MCOLN1 Proteins)+) and SPM (show NPC1 Proteins) therefore may have a synergistic action on the pore-blocking effect, presumably via prohibition of the outward exit of the higher-affinity blocking SPM (show NPC1 Proteins) by the lower-affinity Mg(2 (show MCOLN1 Proteins)+).
Hypoxic stress up-regulates Kir2.1 expression and facilitates cell proliferation in brain capillary endothelial cells.
Kir2.1 may mediate native Kir currents responsible for setting resting membrane potential in bovine parotid cells and might be, at least in part, involved in spontaneous secretion in ruminant parotid glands.
There were substantial transmural gradients in Cav1.2, KChIP2, ERG, KvLQT1, Kir2.1, NCX1, SERCA2a and RyR2 at the mRNA and, in some cases, protein level-in every case the mRNA or protein was more abundant in the epicardium than the endocardium.
Potassium channels are present in most mammalian cells, where they participate in a wide range of physiologic responses. The protein encoded by this gene is an integral membrane protein and inward-rectifier type potassium channel. The encoded protein, which has a greater tendency to allow potassium to flow into a cell rather than out of a cell, probably participates in establishing action potential waveform and excitability of neuronal and muscle tissues. Mutations in this gene have been associated with Andersen syndrome, which is characterized by periodic paralysis, cardiac arrhythmias, and dysmorphic features.
, inward rectifier K(+) channel Kir2.1
, inward rectifier potassium channel 2
, potassium channel, inwardly rectifying subfamily J member 2
, cardiac inward rectifier potassium channel
, inward rectifier K+ channel KIR2.1
, inward rectifier potassium channel cIRK1
, cardiac inward rectifier KIR2.1
, inwardly rectifying potassium channel Kir2.1
, inward rectifier potassium channel Kir2.1
, inwardly-rectifying potassium channel Kir2.1