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Potassium channel, subfamily K, member 13

This gene encodes one of the members of the superfamily of potassium channel proteins containing two pore-forming domains. The product of this gene is an open channel that can be stimulated by arachidonic acid. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: ACID, TREK-1, THIK-2, TWIK-2, K2P
Papers on THIK-1
Breaking the silence: functional expression of the two-pore-domain potassium channel THIK-2.
Daut et al., Marburg an der Lahn, Germany. In Pflugers Arch, 2014
THIK-2 has a highly conserved 19-amino-acid region in its N terminus (residues 6-24 in the rat orthologue) that is missing in the closely related channel THIK-1.
THIK-1 (K2P13.1) is a small-conductance background K(+) channel in rat trigeminal ganglion neurons.
Kim et al., North Chicago, United States. In Pflugers Arch, 2014
We tested the hypothesis that the 5-pS channel is a K2P channel by comparing the pharmacological and single-channel properties of THIK-1 expressed in HEK293 cells.
Leak K⁺ channel mRNAs in dorsal root ganglia: relation to inflammation and spontaneous pain behaviour.
Lawson et al., Bristol, United Kingdom. In Mol Cell Neurosci, 2012
This study is the first to demonstrate expression of THIK1, THIK2 and TWIK2 mRNA in DRGs.
TREK-1 isoforms generated by alternative translation initiation display different susceptibility to the antidepressant fluoxetine.
Wischmeyer et al., Würzburg, Germany. In Neuropharmacology, 2011
In this study we investigated the potency of the antidepressant fluoxetine to inhibit brain and cardiac K(2)P channels, TREK-1, TASK-1 and THIK-1.
Identification and characterization of Cs(+) -permeable K(+) channel current in mouse cerebellar Purkinje cells in lobules 9 and 10 evoked by molecular layer stimulation.
Kubo et al., Okazaki, Japan. In Eur J Neurosci, 2010
KCNK13 is a Cs(+)-permeable K(+) channel that shows intense expression of mRNA in Purkinje cells.
Anesthetic activation of central respiratory chemoreceptor neurons involves inhibition of a THIK-1-like background K(+) current.
Bayliss et al., Charlottesville, United States. In J Neurosci, 2010
Single-cell reverse transcription-PCR analysis of dissociated green fluorescent protein-labeled RTN neurons revealed expression of THIK-1 (TWIK-related halothane-inhibited K(+) channel, K(2P)13.1), a channel that shares key properties with the native RTN current (i.e., suppression by inhalational anesthetics, weak rectification, inhibition by extracellular Na(+), and pH-insensitivity).
Regulation of two-pore-domain (K2P) potassium leak channels by the tyrosine kinase inhibitor genistein.
Thomas et al., Heidelberg, Germany. In Br J Pharmacol, 2008
Among functional hK2P family members, genistein also reduced K2P6.1 (TWIK-2), K2P9.1 (TASK-3) and K2P13.1 (THIK-1) currents, respectively.
Cellular localization of THIK-1 (K(2P)13.1) and THIK-2 (K(2P)12.1) K channels in the mammalian kidney.
Derst et al., Berlin, Germany. In Cell Physiol Biochem, 2007
THIK-1 and THIK-2 are abundantly expressed in the proximal and distal nephron of the mammalian kidney.
Deafness associated changes in two-pore domain potassium channels in the rat inferior colliculus.
Altschuler et al., Ann Arbor, United States. In Neuroscience, 2007
TASK-3, TWIK-2, THIK-1, TRAAK and TREK-1 did not show any significant changes in gene expression.
A Ba2+-resistant, acid-sensitive K+ conductance in Na+-absorbing H441 human airway epithelial cells.
Wilson et al., Dundee, United Kingdom. In Am J Physiol Lung Cell Mol Physiol, 2007
Analyses using RT-PCR showed that mRNA encoding several two-pore domain K(+) (K2P) channels was detected in cells grown under standard conditions (TWIK-1, TREK-1, TASK-2, TWIK-2, KCNK-7, TASK-3, TREK-2, THIK-1, and TALK-2).
Evidence for two-pore domain potassium channels in rat cerebral arteries.
Marrelli et al., Houston, United States. In Am J Physiol Heart Circ Physiol, 2006
RT-PCR revealed message for the following AA-sensitive K(2P) channels in rat MCA: tandem of P domains in weak inward rectifier K+ (TWIK-2), TWIK-related K+ (TREK-1 and TREK-2), TWIK-related AA-stimulated K+ (TRAAK), and TWIK-related halothane-inhibited K+ (THIK-1) channels.
Zinc and mercuric ions distinguish TRESK from the other two-pore-domain K+ channels.
Enyedi et al., Budapest, Hungary. In Mol Pharmacol, 2006
The specificity of the identified agents was determined by measuring their effects on mouse TALK-1, TASK-1, TASK-2, TASK-3, THIK-1, TRAAK, TREK-1, and TREK-2.
Acute hypoxic regulation of recombinant THIK-1 stably expressed in HEK293 cells.
Nurse et al., Hamilton, Canada. In Adv Exp Med Biol, 2005
expression in cell hypoxia
O2 sensing by recombinant TWIK-related halothane-inhibitable K+ channel-1 background K+ channels heterologously expressed in human embryonic kidney cells.
Fearon et al., Hamilton, Canada. In Neuroscience, 2004
Hypoxic inhibition of K+ channels provides a link between low O2 and cell function, and in glossopharyngeal neurons hypoxic inhibition of a TWIK-related halothane-inhibitable K+ channel-1 (THIK-1)-like background K+ channel regulates neuronal function.
Identification and distribution of a two-pore domain potassium channel in the CNS of Aplysia californica.
Moroz et al., United States. In Brain Res Mol Brain Res, 2004
The deduced amino acid sequence is homologous to channels of the mammalian two-pore domain halothane inhibited (THIK) subfamily, bearing 46% identity to THIK-1 (KCNK 13) and 48% to THIK-2 (KCNK12).
Functional evidence of a role for two-pore domain potassium channels in rat mesenteric and pulmonary arteries.
Weston et al., Manchester, United Kingdom. In Br J Pharmacol, 2004
5. RT-PCR demonstrated the expression of TASK-1, TASK-2, THIK-1, TRAAK, TREK-1, TWIK-1 and TWIK-2 in mesenteric arteries and TASK-1, TASK-2, THIK-1, TREK-2 and TWIK-2 in pulmonary arteries.
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