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Kcnj10  -  potassium inwardly-rectifying channel,...

Mus musculus

Synonyms: ATP-sensitive inward rectifier potassium channel 10, BIR10, BIRK-1, Inward rectifier K(+) channel Kir4.1, Kir1.2, ...
 
 
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Disease relevance of Kcnj10

  • Treatment with soybean-derived Bowman Birk inhibitor increases serum prostate-specific antigen concentration while suppressing growth of human prostate cancer xenografts in nude mice [1].
  • Kir4.1 expression confers the same K+ conductance to glioma membranes and a similar responsiveness to changes in [K+]o that characterizes differentiated astrocytes [2].
 

High impact information on Kcnj10

  • We found that <10% of AQP4 immunogold labeling is retained in the perivascular astrocyte end-feet membranes of the alpha-Syn-/- mice, whereas labeling of the inwardly rectifying K+ channel, Kir4.1, is largely unchanged [3].
  • Overall, these results indicate that Kir4.1 is the principal K(+) channel subunit expressed in mouse Müller glial cells [4].
  • Of 11 members of the Kir channel family examined with reverse transcription-PCR, we could detect only expression of KAB-2 (Kir4.1) mRNA in stria vascularis [5].
  • In vitro immunoprecipitation and pull-down assays demonstrated that Kir4.1 can bind directly to alpha-syntrophin, requiring the presence of the last three amino acids of the channel (SNV), a consensus PDZ domain-binding motif [6].
  • Differential assembly of inwardly rectifying K+ channel subunits, Kir4.1 and Kir5.1, in brain astrocytes [7].
 

Biological context of Kcnj10

 

Anatomical context of Kcnj10

 

Associations of Kcnj10 with chemical compounds

 

Other interactions of Kcnj10

  • Of these, the most compelling seizure susceptibility candidate is Kcnj10 [8].
  • Transcripts encoding Kir2.1, Kir2.2, or Kir2.3, were encountered in a majority of cells, while Kir4.1 was less frequent [14].
  • Differential effect of alpha-syntrophin knockout on aquaporin-4 and Kir4.1 expression in retinal macroglial cells in mice [10].
  • 1. Immunolabeling using specific antibodies showed that channels comprising Kir4.1 and Kir5.1 subunits were assembled in a region-specific fashion [7].
  • The amplitude of slow PIII, revealed by the nob genetic background, was reduced in Kir4.1+/- mice [15].
 

Analytical, diagnostic and therapeutic context of Kcnj10

References

  1. Treatment with soybean-derived Bowman Birk inhibitor increases serum prostate-specific antigen concentration while suppressing growth of human prostate cancer xenografts in nude mice. Wan, X.S., Ware, J.H., Zhang, L., Newberne, P.M., Evans, S.M., Clark, L.C., Kennedy, A.R. Prostate (1999) [Pubmed]
  2. Role of Kir4.1 channels in growth control of glia. Higashimori, H., Sontheimer, H. Glia (2007) [Pubmed]
  3. Delayed K+ clearance associated with aquaporin-4 mislocalization: phenotypic defects in brains of alpha-syntrophin-null mice. Amiry-Moghaddam, M., Williamson, A., Palomba, M., Eid, T., de Lanerolle, N.C., Nagelhus, E.A., Adams, M.E., Froehner, S.C., Agre, P., Ottersen, O.P. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  4. Genetic inactivation of an inwardly rectifying potassium channel (Kir4.1 subunit) in mice: phenotypic impact in retina. Kofuji, P., Ceelen, P., Zahs, K.R., Surbeck, L.W., Lester, H.A., Newman, E.A. J. Neurosci. (2000) [Pubmed]
  5. An ATP-dependent inwardly rectifying potassium channel, KAB-2 (Kir4. 1), in cochlear stria vascularis of inner ear: its specific subcellular localization and correlation with the formation of endocochlear potential. Hibino, H., Horio, Y., Inanobe, A., Doi, K., Ito, M., Yamada, M., Gotow, T., Uchiyama, Y., Kawamura, M., Kubo, T., Kurachi, Y. J. Neurosci. (1997) [Pubmed]
  6. The potassium channel Kir4.1 associates with the dystrophin-glycoprotein complex via alpha-syntrophin in glia. Connors, N.C., Adams, M.E., Froehner, S.C., Kofuji, P. J. Biol. Chem. (2004) [Pubmed]
  7. Differential assembly of inwardly rectifying K+ channel subunits, Kir4.1 and Kir5.1, in brain astrocytes. Hibino, H., Fujita, A., Iwai, K., Yamada, M., Kurachi, Y. J. Biol. Chem. (2004) [Pubmed]
  8. Fine mapping of a seizure susceptibility locus on mouse Chromosome 1: nomination of Kcnj10 as a causative gene. Ferraro, T.N., Golden, G.T., Smith, G.G., Martin, J.F., Lohoff, F.W., Gieringer, T.A., Zamboni, D., Schwebel, C.L., Press, D.M., Kratzer, S.O., Zhao, H., Berrettini, W.H., Buono, R.J. Mamm. Genome (2004) [Pubmed]
  9. Association between variation in the human KCNJ10 potassium ion channel gene and seizure susceptibility. Buono, R.J., Lohoff, F.W., Sander, T., Sperling, M.R., O'Connor, M.J., Dlugos, D.J., Ryan, S.G., Golden, G.T., Zhao, H., Scattergood, T.M., Berrettini, W.H., Ferraro, T.N. Epilepsy Res. (2004) [Pubmed]
  10. Differential effect of alpha-syntrophin knockout on aquaporin-4 and Kir4.1 expression in retinal macroglial cells in mice. Puwarawuttipanit, W., Bragg, A.D., Frydenlund, D.S., Mylonakou, M.N., Nagelhus, E.A., Peters, M.F., Kotchabhakdi, N., Adams, M.E., Froehner, S.C., Haug, F.M., Ottersen, O.P., Amiry-Moghaddam, M. Neuroscience (2006) [Pubmed]
  11. Kir potassium channel subunit expression in retinal glial cells: implications for spatial potassium buffering. Kofuji, P., Biedermann, B., Siddharthan, V., Raap, M., Iandiev, I., Milenkovic, I., Thomzig, A., Veh, R.W., Bringmann, A., Reichenbach, A. Glia (2002) [Pubmed]
  12. Functional consequences of polyamine synthesis inhibition by L-alpha-difluoromethylornithine (DFMO): cellular mechanisms for DFMO-mediated ototoxicity. Nie, L., Feng, W., Diaz, R., Gratton, M.A., Doyle, K.J., Yamoah, E.N. J. Biol. Chem. (2005) [Pubmed]
  13. Identification of an inward rectifier potassium channel gene expressed in mouse cortical astrocytes. Li, L., Head, V., Timpe, L.C. Glia (2001) [Pubmed]
  14. AMPA receptor-mediated modulation of inward rectifier K+ channels in astrocytes of mouse hippocampus. Schröder, W., Seifert, G., Hüttmann, K., Hinterkeuser, S., Steinhäuser, C. Mol. Cell. Neurosci. (2002) [Pubmed]
  15. Contribution of Kir4.1 to the mouse electroretinogram. Wu, J., Marmorstein, A.D., Kofuji, P., Peachey, N.S. Mol. Vis. (2004) [Pubmed]
  16. CIPP, a novel multivalent PDZ domain protein, selectively interacts with Kir4.0 family members, NMDA receptor subunits, neurexins, and neuroligins. Kurschner, C., Mermelstein, P.G., Holden, W.T., Surmeier, D.J. Mol. Cell. Neurosci. (1998) [Pubmed]
 
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