gopubmed logo
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Potassium inwardly-rectifying channel, subfamily J, member 15

Kir4.2, KCNJ15, Kir1.3
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 has a greater tendency to allow potassium to flow into a cell rather than out of a cell. Three transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: KIR, Kir4.1, Kir5.1, ROMK, ACID
Papers on Kir4.2
Involvement of Potassium and Cation Channels in Hippocampal Abnormalities of Embryonic Ts65Dn and Tc1 Trisomic Mice.
Moses et al., Portugal. In Ebiomedicine, Sep 2015
Quantitative real-time PCR analysis indicates overexpression of 40% of KCNJ15, an inward rectifying potassium channel, contributing to the increased inhibition.
Potassium channel KCNJ15 is required for histamine-stimulated gastric acid secretion.
Zhu et al., Shanghai, China. In Am J Physiol Cell Physiol, Sep 2015
Our previous studies have shown the translocation of KCNJ15 from cytoplasmic vesicles to the apical membrane on stimulation, indicating its involvement in gastric acid secretion.
Diagnostic value of blood gene expression signatures in active tuberculosis in Thais: a pilot study.
Mahasirimongkol et al., Thailand. In Genes Immun, Jun 2015
FCGR1A, FCGR1B variant 1, FCGR1B variant 2, APOL1, GBP5, PSTPIP2, STAT1, KCNJ15, MAFB and KAZN had significantly higher expression level in active TB individuals as compared with healthy controls and previous TB cases (P<0.01).
Molecular insights into the possible role of Kir4.1 and Kir5.1 in thyroid hormone biosynthesis.
Polak et al., Paris, France. In Horm Res Paediatr, 2014
OBJECTIVES: To investigate the thyroid developmental expression of three members, Kir4.1, Kir4.2 and Kir5.1, in mice.
KCNJ15/Kir4.2 couples with polyamines to sense weak extracellular electric fields in galvanotaxis.
Zhao et al., Sacramento, United States. In Nat Commun, 2014
Knockdown of the KCNJ15 gene (encoding inwardly rectifying K(+) channel Kir4.2) specifically abolishes galvanotaxis, without affecting basal motility and directional migration in a monolayer scratch assay.
Focus on Kir7.1: physiology and channelopathy.
Pattnaik et al., India. In Channels (austin), 2013
Kir4.2, and Kir6.1, albeit at levels at least 50-fold lower than Kir7.1.
Replication study for the association of a single-nucleotide polymorphism, rs3746876, within KCNJ15, with susceptibility to type 2 diabetes in a Japanese population.
Maeda et al., Yokohama, Japan. In J Hum Genet, 2013
By an association mapping for the candidate locus in chromosome 21q, rs3746876 within KCNJ15 was shown to be associated with type 2 diabetes in Japanese populations.
Inhibition of glucose-stimulated insulin secretion by KCNJ15, a newly identified susceptibility gene for type 2 diabetes.
Tokunaga et al., Tokyo, Japan. In Diabetes, 2012
It was shown that downregulation of Kcnj15 leads to increased insulin secretion in vitro and in vivo. The mechanism for regulating insulin secretion inolved a calcium-sensiong receptor.
Integrin α9β1-mediated cell migration in glioblastoma via SSAT and Kir4.2 potassium channel pathway.
Rao et al., Peoria, United States. In Cell Signal, 2012
The migratory potential of MMP-9/uPAR/cathepsin B-overexpressed 4910 and 5310 cells was not affected by either glybenclamide (Kir 6.x inhibitor) or tertiapin-Q (Kir 1.1 and 3.x inhibitor) but instead was significantly inhibited by either barium or Kir4.2 siRNA treatments.
Potassium-dependent activation of Kir4.2 K⁺ channels.
Palmer et al., New York City, United States. In J Physiol, 2012
The inwardly rectifying potassium channel Kir4.2 is sensitive to changes in the extracellular potassium concentration ([K(+)](o)).
Acid secretion-associated translocation of KCNJ15 in gastric parietal cells.
Zhu et al., Buffalo, United States. In Am J Physiol Gastrointest Liver Physiol, 2011
in nonsecreting parietal cells, KCNJ15 is stored in vesicles distinct from the H(+)-K(+)-ATPase-enriched tubulovesicles. Furthermore, upon stimulation, KCNJ15 and H(+)-K(+)-ATPase both translocate to the apical membrane for active acid secretion.
Random mutagenesis screening indicates the absence of a separate H(+)-sensor in the pH-sensitive Kir channels.
Tucker et al., Oxford, United Kingdom. In Channels (austin), 2010
Kir4.1 and Kir4.2) are characterised by their sensitivity to inhibition by intracellular H(+) within the physiological range.
Mutations at KCNQ1 and an unknown locus cause long QT syndrome in a large Australian family: implications for genetic testing.
Radford et al., Edinburgh, United Kingdom. In Am J Med Genet A, 2010
One region on chromosome 21 contained the KCNE1, KCNE2, KCNJ6, and KCNJ15 genes.
Identification of KCNJ15 as a susceptibility gene in Asian patients with type 2 diabetes mellitus.
Tokunaga et al., Tokyo, Japan. In Am J Hum Genet, 2010
KCNJ15 is a previously unreported susceptibility gene for T2DM among Asians
Discovery of a small molecule inhibitor of ROMK with unprecedented selectivity
Lindsley et al., Bethesda, United States. In Unknown Journal, 2009
Kir4.1, Kir4.2, Kir5.1, Kir7.1) of the Kir channel family are expressed in the nephron, but their physiological functions are not well understood.
Discovery of a small molecule inhibitor of ROMK and Kir7.1
Lindsley et al., Bethesda, United States. In Unknown Journal, 2009
Kir4.1, Kir4.2, Kir5.1, Kir7.1) of the Kir channel family are expressed in the nephron, but their physiological functions are not well understood.
MUPP1 complexes renal K+ channels to alter cell surface expression and whole cell currents.
Miller et al., Cleveland, United States. In Am J Physiol Renal Physiol, 2009
MUPP1 and Kir4.2 may participate in a protein complex in the nephron that could regulate transport of K(+) as well as other ions.
Interaction of the Ca2+-sensing receptor with the inwardly rectifying potassium channels Kir4.1 and Kir4.2 results in inhibition of channel function.
Miller et al., Cleveland, United States. In Am J Physiol Renal Physiol, 2007
Calcium-sensing receptor interacts directly with Kir4.1 and Kir4.2 and can decrease their currents.
share on facebooktweetadd +1mail to friends