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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 Potassium Inwardly-Rectifying Channel, Subfamily J, Member 3 Antibodies (105) and Potassium Inwardly-Rectifying Channel, Subfamily J, Member 3 Kits (5) and many more products for this protein.
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Results clearly corroborate that overexpression of GIRK1 protein exerts profound effects on wound healing, chemoinvasion and cellular motility in the MCF-7 breast cancer cell line suggesting a role to promote invasion and metastasis.
GIRK1/GIRK4 (show KCNJ5 Proteins) hetero-tetramers are not activated by Na+, but rather are in a permanent state of high responsiveness to G proteins beta-gamma, suggesting that the GIRK1 subunit functions like a GIRK4 (show KCNJ5 Proteins) subunit with Na+ permanently bound.
The findings of this study suggest that variations in KCNJ3 genes are associated with both mild and severe persistent breast pain after breast cancer surgery.
For KCNJ3 rs7574878, individuals who were heterozygous or homozygous for the rare G allele (TT versus TG+ GG) had a 48% reduction in the odds of reporting preoperative breast pain.
we show that Kir3.1, in the absence of trafficking partner subunits, can exit the endoplasmic reticulum (ER) and reach the Golgi (though not the plasma membrane)
Conformational changes at the Gbetagamma/Kir3 interface were lost when Kir3.1 subunits were replaced.
These data suggest that the KCNJ3 gene is genetically associated with schizophrenia in Asian populations and add further evidence to the "channelopathy theory of psychiatric illnesses".
Kir3.1 channel is involved in the TLR4 (show TLR4 Proteins)-mediated signal at an early event by facilitating the recruitment of TLR4 (show TLR4 Proteins) into lipid raft.
halothane (show RYR1 Proteins) predominantly interferes with Gbetagamma-mediated Kir3 currents, such as those functioning during inhibitory synaptic activity
The very high abundance of mRNA's encoding GIRK1 together with the presence of GIRK1 protein suggests a pathophysiological role in breast cancer
Kir 3.1 channels are important for supraspinal antinociception and presynaptic GABA release inhibition by oxycodone in the femur bone cancer model
GABA neurons in the ventral tegmental area express GIRK1 (and GIRK2 (show KCNJ6 Proteins)) subunits.
siRNA knock-down of NgR1 (show NEUROG1 Proteins) resulted in a selective increase of GABAB R1 and GABAB R2 protein and an increase in GIRK1.
Discontinuous and sometime opposing elements in Girk1 underlie the Girk1-dependent potentiation of receptor-dependent and receptor-independent heteromeric channel activity.
Mechanism for functional dysregulation in the dorsal raphe follows tyrosine phosphorylation of repeated stress-activated Kir3.1 channels.
NMR analyses of the Gbetagamma binding and conformational rearrangements of the cytoplasmic pore of G protein-activated inwardly rectifying potassium channel 1 (show KCNA5 Proteins) (GIRK1).
Agonist-induced localization of Gq-coupled receptors and G protein-gated inwardly rectifying K+ (GIRK) channels to caveolae determines receptor specificity of phosphatidylinositol 4,5-bisphosphate signaling
The atrial potassium channel (show KCNAB2 Proteins), I(KACH), ion channel gating is accelerated in atrial myocytes through the RGS6 (show RGS6 Proteins)/Gbeta5 (show GNB5 Proteins) complex.
Dopamine neurons from Girk1 knock-out mice (and Girk2 (show KCNJ6 Proteins)) exhibited elevated glutamatergic neurotransmission and increased synaptic levels of AMPA (show GRIA3 Proteins) glutamate (show GRIN1 Proteins) receptors.
Data suggest HL-1 (show ASGR1 Proteins) cells express GIRK1/4 and M2 muscarinic receptors and are a good model to study acetylcholine-activated potassium currents.
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, is controlled by G-proteins and plays an important role in regulating heartbeat. It associates with three other G-protein-activated potassium channels to form a heteromultimeric pore-forming complex that also couples to neurotransmitter receptors in the brain and whereby channel activation can inhibit action potential firing by hyperpolarizing the plasma membrane. These multimeric G-protein-gated inwardly-rectifying potassium (GIRK) channels may play a role in the pathophysiology of epilepsy, addiction, Down's syndrome, ataxia, and Parkinson's disease. Alternative splicing results in multiple transcript variants encoding distinct proteins.
G protein-activated inward rectifier potassium channel 1
, inward rectifier K(+) channel Kir3.1
, inward rectifier K+ channel KIR3.1
, potassium channel, inwardly rectifying subfamily J member 3
, potassium inwardly-rectifying channel subfamily J member 3 splice variant 1e
, potassium inwardly-rectifying channel J3
, potassium channel inwarding rectifying channel subfamily J member 3
, potassium channel subunit Kir3.1 type 3 delta
, inward rectifying potassium channel, Kir3.1