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Potassium voltage-gated channel, KQT-like subfamily, member 2
KCNQ2, Kv7.2
The M channel is a slowly activating and deactivating potassium channel that plays a critical role in the regulation of neuronal excitability. The M channel is formed by the association of the protein encoded by this gene and a related protein encoded by the KCNQ3 gene, both integral membrane proteins. M channel currents are inhibited by M1 muscarinic acetylcholine receptors and activated by retigabine, a novel anti-convulsant drug. Defects in this gene are a cause of benign familial neonatal convulsions type 1 (BFNC), also known as epilepsy, benign neonatal type 1 (EBN1). At least five transcript variants encoding five different isoforms have been found for this gene. [provided by RefSeq, Jul 2008] (from
NCBI)
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Papers using
KCNQ2
antibodies
Direct interaction of myosin regulatory light chain with the NMDA receptor.
Supplier
In PLoS ONE, 2004
... The primary antibodies used were KCNQ2-C terminus, KCNQ3-C terminus (Alomone Labs, Jerusalem, Israel) and monoclonal ...
Papers on
KCNQ2
Amyloid β peptides modify the expression of antioxidant repair enzymes and a potassium channel in the septohippocampal system.
New
Brownsville, United States. In Neurobiol Aging, 07 Apr 2013
The expression levels of the K+ voltage-gated channel, KQT-like subfamily, member 2 (KCNQ2) and the OS-related genes superoxide dismutase 1, 8-oxoguanine DNA glycosylase, and monamine oxidase A, were analyzed in the hippocampus, medial, and lateral septum.
Genetic testing in benign familial epilepsies of the first year of life: Clinical and diagnostic significance.
New
Genova, Italy. In Epilepsia, 31 Mar 2013
SCN2A, KCNQ2, KCNQ3, PPRT2 point mutations were analyzed by direct sequencing of amplified genomic DNA.
Genotype-phenotype correlations in neonatal epilepsies caused by mutations in the voltage sensor of Kv7.2 potassium channel subunits.
New
Napoli, Italy. In Proc Natl Acad Sci U S A, 25 Mar 2013
Mutations in the K(V)7.2
The Neuronal Serum- and Glucocorticoid-Regulated Kinase 1.1 Reduces Neuronal Excitability and Protects against Seizures through Upregulation of the M-Current.
New
Leioa, Spain. In J Neurosci, 06 Mar 2013
The M-current formed by tetramerization of Kv7.2 and Kv7.3 subunits is a neuronal voltage-gated K(+) conductance that controls resting membrane potential and cell excitability.
The role of potassium channel activation in celecoxib-induced analgesic action.
New
Shijiazhuang, China. In Plos One, Dec 2012
We found that CXB, UMC and DMC concentration-dependently activated Kv7.2/7.3 channels expressed in HEK293 cells and the M-type current in dorsal root ganglia neurons, negatively shifted I-V curve of Kv7.2/7.3 channels, with a potency and efficiency inverse to their COX-2 inhibitory potential.
The urinary safety profile and secondary renal effects of retigabine (ezogabine): a first-in-class antiepileptic drug that targets KCNQ (K(v)7) potassium channels.
Review
New
United Kingdom. In Epilepsia, Apr 2012
Retigabine (RTG; international nonproprietary name)/ezogabine (EZG; North American adopted name), a first-in-class antiepileptic drug (AED) that reduces neuronal excitability primarily by enhancing the activity of KCNQ2/3 (K(v)7.2/7.3)
The mechanism of action of retigabine (ezogabine), a first-in-class K+ channel opener for the treatment of epilepsy.
Review
New
Harlow, United Kingdom. In Epilepsia, Mar 2012
Its primary mechanism of action (MoA) as a positive allosteric modulator of KCNQ2-5 (K(v) 7.2-7.5)
Regulation of neuronal M-channel gating in an isoform-specific manner: functional interplay between calmodulin and syntaxin 1A.
GeneRIF
Tel Aviv-Yafo, Israel. In J Neurosci, 2011
The existence of constitutive interactions between the N and C termini in homomeric KCNQ2 and KCNQ3 channels has been determined in living cells by means of optical, biochemical, electrophysiological, and molecular biology analyses.
Distribution of M-channel subunits KCNQ2 and KCNQ3 in rat hippocampus.
GeneRIF
San Antonio, United States. In Neuroimage, 2011
we show the distribution and co-localization of KCNQ2 and KCNQ3 subunits throughout the hippocampal formation
Temperature and pharmacological rescue of a folding-defective, dominant-negative KV 7.2 mutation associated with neonatal seizures.
GeneRIF
Ulm, Germany. In Hum Mutat, 2011
The results represent a first example of temperature and pharmacological rescue of K(V) 7 mutation and suggest a folding and trafficking deficiency as the cause of reduced current amplitudes.
[New antiepileptic drugs, and therapeutic considerations].
Review
Kantharalak, Thailand. In Ideggyogy Sz, 2011
Retigabine is a carbamic derivate, and its anticonvulsive properties are largely due to its ability to prolong the opening of neuronal voltage-gated potassium Kv7.2 and Kv7.3 channels.
Pharmacogenetics of new analgesics.
Review
Frankfurt am Main, Germany. In Br J Pharmacol, 2011
This addresses voltage-gated sodium, calcium and potassium channels, for which SCN9A, CACNA1B, KCNQ2 and KCNQ3, respectively, are primary gene candidates because they code for the subunits of the respective channels targeted by analgesics currently in clinical development.
Epilepsy and the new cytogenetics.
Review
Adelaide, Australia. In Epilepsia, 2011
Multiplex ligase-dependent probe amplification (MLPA) targeted to predetermined regions such as SCN1A and KCNQ2 has been effectively applied over the last half a decade, and oligonucleotide array comparative genome hybridization (array CGH) is now well established for genome-wide exploration of microchromosomal variation.
Accumulation of Kv7.2 channels in putative ectopic transduction zones of mice nerve-end neuromas.
GeneRIF
Madrid, Spain. In Mol Pain, 2010
Accumulation of Kv7 channels in afferent fibers may increase M-type currents which then acquired a more important role at regulating fiber excitability.
Kv7 channels can function without constitutive calmodulin tethering.
GeneRIF
Leioa, Spain. In Plos One, 2010
constitutive tethering of calmodulin is not required for Kv7 channel function
Moderate loss of function of cyclic-AMP-modulated KCNQ2/KCNQ3 K+ channels causes epilepsy.
Impact
Hamburg, Germany. In Nature, 1999
Potassium channels are important regulators of electrical signalling, and benign familial neonatal convulsions (BFNC), an autosomal dominant epilepsy of infancy, is caused by mutations in the KCNQ2 or the KCNQ3 potassium channel genes.
KCNQ2 and KCNQ3 potassium channel subunits: molecular correlates of the M-channel.
Impact
Stony Brook, United States. In Science, 1999
The biophysical properties, sensitivity to pharmacological blockade, and expression pattern of the KCNQ2 and KCNQ3 potassium channels were determined.
A potassium channel mutation in neonatal human epilepsy.
Impact
Bonn, Germany. In Science, 1998
In a large pedigree with BFNC, a five-base pair insertion would delete more than 300 amino acids from the KCNQ2 carboxyl terminus.
A novel potassium channel gene, KCNQ2, is mutated in an inherited epilepsy of newborns.
Impact
Salt Lake City, United States. In Nat Genet, 1998
Five other BFNC probands were shown to have KCNQ2 mutations, including two transmembrane missense mutations, two frameshifts and one splice-site mutation.
A pore mutation in a novel KQT-like potassium channel gene in an idiopathic epilepsy family.
Impact
Salt Lake City, United States. In Nat Genet, 1998
By positional cloning, we recently identified the gene for EBN1 as KCNQ2 (ref.
