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Potassium voltage-gated channel, shaker-related subfamily, member 7

KCNA7, Kv1.7, voltage-gated potassium channel Kv1.7
Potassium channels represent the most complex class of voltage-gated ion channels from both functional and structural standpoints. Their diverse functions include regulating neurotransmitter release, heart rate, insulin secretion, neuronal excitability, epithelial electrolyte transport, smooth muscle contraction, and cell volume. Four sequence-related potassium channel genes - shaker, shaw, shab, and shal - have been identified in Drosophila, and each has been shown to have human homolog(s). This gene encodes a member of the potassium channel, voltage-gated, shaker-related subfamily. This member contains six membrane-spanning domains with a shaker-type repeat in the fourth segment. The gene is expressed preferentially in skeletal muscle, heart and kidney. It is a candidate gene for inherited cardiac disorders. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Potassium Channel, Kv1.1, SF-1, Kv1.4, Kv1.6
Papers on KCNA7
Differential expression of the Kv1 voltage-gated potassium channel family in the rat nephron.
Escobar et al., Mexico. In J Mol Histol, 2014
Immunofluorescence labeling detected Kv1.5 in Bowman´s capsule and endothelial cells and Kv1.7 in podocytes, endothelial cells and macula densa in glomeruli; Kv1.4,
Block of Kv1.7 potassium currents increases glucose-stimulated insulin secretion.
GeneRIF
Terlau et al., Calgary, Canada. In Embo Mol Med, 2012
The authors conclude that K(v) 1.7 contributes to the membrane-repolarizing current of beta cells during glucose-stimulated insulin.
Functional ion channels in human pulmonary artery smooth muscle cells: Voltage-dependent cation channels.
Yuan et al., Los Angeles, United States. In Pulm Circ, 2011
Transcripts of (a) two Na(+) channel α-subunit genes (SCN5A and SCN6A), (b) six Ca(2+) channel α-subunit genes (α(1A), α(1B), α(1x), α(1D), α(1E) and α(1G)) and many regulatory subunits (α(2)δ(1), β(1-4), and γ(6)), (c) 22 Kv channel α-subunit genes (Kv1.1 - Kv1.7, Kv1.10, Kv2.1, Kv3.1, Kv3.3, Kv3.4,
Biochemical characterization of kappaM-RIIIJ, a Kv1.2 channel blocker: evaluation of cardioprotective effects of kappaM-conotoxins.
Olivera et al., Salt Lake City, United States. In J Biol Chem, 2010
kappaM-RIIIJ shows more potency for Kv1.2-Kv1.5 and Kv1.2-Kv1.6 heterodimers than kappaM-RIIIK, whereas the affinity of kappaM-RIIIK to Kv1.2-Kv1.7 heterodimeric channels is higher (IC(50) = 680 nm) than that of kappaM-RIIIJ (IC(50) = 3.15 mum).
Potassium channel modulation by a toxin domain in matrix metalloprotease 23.
Chandy et al., Irvine, United States. In J Biol Chem, 2010
Kv1.5, Kv1.7, and KCa3.1).
The Kv1.2 potassium channel: the position of an N-glycan on the extracellular linkers affects its protein expression and function.
Thornhill et al., United States. In Brain Res, 2009
The S1-S2 is the only linker that has an N-glycan and it is at a conserved position on this linker on Kv1.1-Kv1.5 and Kv1.7 channels.
Effects of various K+ channel blockers on spontaneous glycine release at rat spinal neurons.
Akaike et al., Kumamoto, Japan. In Brain Res, 2007
The results suggest the existence of the following K+ channel subtypes on glycinergic nerve endings that are involved in regulating 'spontaneous' glycine release (mIPSCs): the Shaker-related K+ channels Kv1.1, Kv1.2, Kv1.3, Kv1.6 and Kv1.7 and the intracellular Ca2+ -sensitive K+ channels BKCa, IKCa and SKCa.
Phylogenomic analyses of KCNA gene clusters in vertebrates: why do gene clusters stay intact?
Meyer et al., Konstanz, Germany. In Bmc Evol Biol, 2006
Phylogenetic analyses of the genes suggest a basal position of the only intron containing KCNA gene in vertebrates (KCNA7).
Potassium channels lost during harvesting of epithelial cells are restored with a kinetics that depends on channel species.
Cereijido et al., Mexico. In Cell Physiol Biochem, 2006
(iii) Replacement is not an all-or-none response, since mRNA for MaxiK channels increases by 8-fold after re-seeding, but those for Kv1.6 and Kv1.7 are not affected by harvesting/re-seeding.
Bone morphogenetic protein-2 upregulates expression and function of voltage-gated K+ channels in human pulmonary artery smooth muscle cells.
Yuan et al., San Diego, United States. In Am J Physiol Lung Cell Mol Physiol, 2006
BMP-2 (100 nM for 18-24 h) significantly (>2-fold) upregulated mRNA expression of KCNA5, KCNA7, KCNA10, KCNC3, KCNC4, KCNF1, KCNG3, KCNS1, and KCNS3 but downregulated (at least 2-fold) KCNAB1, KCNA2, KCNG2, and KCNV2.
Gene expression profiling of human cardiac potassium and sodium channels.
Boldogkoi et al., Szeged, Hungary. In Int J Cardiol, 2006
Further, we found that the expression levels of Kv1.5 and Kv2.1 transcripts in the ventricle were very high, and that mRNAs for Kv1.7 and Kv3.4 are highly abundant in both the atrium and ventricle, which might indicate a functional role of these ion channel subunits in the formation of action potential in the human ventricle and both in the atrium and ventricle, respectively.
Molecular and Functional Differences between Heart mKv1.7 Channel Isoforms.
GeneRIF
Terlau et al., Göttingen, Germany. In J Gen Physiol, 2006
Kv1.7 channels from mouse heart muscle have two putative translation initiation start sites that generate two channel isoforms with different functional characteristics, mKv1.7L (489 aa) and a shorter mKv1.7S (457 aa).
Characterization of potassium channels involved in volume regulation of human spermatozoa.
Cooper et al., Münster, Germany. In Mol Hum Reprod, 2005
Kv1.5 and Kv1.7, acid-sensitive channel TASK2 and the beta-subunit minK (IsK) in regulatory volume decrease (RVD).
Kv1.3-blocking 5-phenylalkoxypsoralens: a new class of immunomodulators.
Chandy et al., Kiel, Germany. In Mol Pharmacol, 2004
Kv1.2, Kv1.4, and Kv1.7) with the exception of Kv1.5 (EC50, 7.7 nM) and showed no effect on human ether-a-go-go-related channel, Kv3.1, the calcium-activated K+ channels (IKCa1, SK1-SK3, and BKCa), or the neuronal NaV1.2 channel.
[Distribution and significance of cSNP in KCNA7 gene as a novel NIDDM candidate gene in the population of northeast China].
Guo et al., Shenyang, China. In Yi Chuan, 2003
To investigate the distribution and significance of a coding single nucleotide polymorphism (cSNP) of the novel NIDDM candidate gene,KCNA7 in the population of Northeast China, 97 patients with NIDDM and 141 controls were tested.
Characterisation of the human voltage-gated potassium channel gene, KCNA7, a candidate gene for inherited cardiac disorders, and its exclusion as cause of progressive familial heart block I (PFHBI).
GeneRIF
Corfield et al., Stellenbosch, South Africa. In Eur J Hum Genet, 2002
Expressed in heart, but not the cause of progressive familial heart block I.
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