International Union of Pharmacology. XLI. Compendium of Voltage-Gated Ion Channels: Potassium Channels

Gutman, George A.; Chandy, K. George; Adelman, John P.; Aiyar, Jayashree; Bayliss, Douglas A.; Clapham, David E.; Covarriubias, Manuel; Desir, Gary V.; Furuichi, Kiyoshi; Ganetzky, Barry; García, María L.; Grissmer, Stephan; Jan, Yuh Nung; Karschin, Andreas; Kim, Dong‐Hee; Kuperschmidt, Sabina; Kurachi, Yoshihisa; Lazdunski, Michel; Lesage, Florian; Lester, Henry A.; McKinnon, David; Nichols, Colin G.; O’Kelly, Ita; Robbins, Jon; Robertson, Gail A.; Rudy, Bernardo; Sanguinetti, Michael C.; Seino, Susumu; Stuehmer, W.; Tamkun, Michael M.; Vandenberg, Carol A.; Wei, Aguan; Wulff, Heike; Wymore, Randy S.

doi:10.1124/pr.55.4.9

Cited by 351 publications

(201 citation statements)

References 4 publications

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“…Immunohistochemical analyses (Sheng et al, 1992;Maletic-Savatic et al, 1995;Tsaur et al, 1997;Varga et al, 2000; for review, see Trimmer and Rhodes, 2004), pharmacological sensitivity (Wu and Barish, 1992;Holmqvist et al, 2001), and electrophysiological characteristics (Serô dio et al, 1994(Serô dio et al, , 1996Serô dio and Rudy, 1998) suggest that a major component of the somatodendritic A-type Kv current is formed by ␣ subunits from the Shal or Kv4 family (Gutman et al, 2003). However, A-type currents from Kv4 ␣ subunits expressed in heterologous cells and neurons differ.…”

Section: Introductionmentioning

confidence: 99%

KChIPs and Kv4 α Subunits as Integral Components of A-Type Potassium Channels in Mammalian Brain

Rhodes¹,

Carroll²,

Sung³

et al. 2004

J. Neurosci.

238

291

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Section: Introductionmentioning

confidence: 99%

KChIPs and Kv4 α Subunits as Integral Components of A-Type Potassium Channels in Mammalian Brain

Rhodes¹,

Carroll²,

Sung³

et al. 2004

J. Neurosci.

238

291

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“…Cette diversité repose sur leur très grande variété génique [6,7]. En effet, chez l'homme, plus de 70 gènes différents codent pour des sous-unités K + .…”

unclassified

Physiologie, pharmacologie et modélisation de canaux potassiques

et al. 2012

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“…However, the effect of PKC activation on KCNQ channels is still controversial [8] . The inhibition of the metabolism of DAG by DAG kinase blockers cannot mimic the effect of muscarinic modulation by muscarinic agonist, and it has been suggested Functional study of the effect of phosphatase inhibitors on KCNQ4 channels expressed in Xenopus oocytes Tzu-rong SU 1 , Cay-huyen CHEN 2 , Shih-jen HUANG 2 , Chun-yi LEE 2 , Mao-chang SU 3 , Gwan-hong CHEN 4 , Shuan-yow LI 4 , Jiannjou YANG 4 , Min-jon LIN 4, * that activated PKC and its targets are not essential players in the acute muscarinic modulation of KCNQ channels in mammalian expression systems [8] . By contrast, the activation of PKC induced a large positive shift in the conductance-voltage curve for KCNQ channels expressed in Xenopus oocytes [9] .…”

Section: Introductionmentioning

confidence: 99%

“…The KCNQ gene subfamily is composed of five K + channels, KCNQ1 to KCNQ5. The KCNQ4 channel was included in the Kv nomenclature as Kv 7.4 (voltage-gated potassium channel subunit Kv7.4) [3] . The heteromers of KCNQ2/KCNQ3 underlie the neuronal M-current, which modulates neuronal excitability.…”

mentioning

confidence: 99%

Functional study of the effect of phosphatase inhibitors on KCNQ4 channels expressed in Xenopus oocytes

Su¹,

Chen²,

Huang³

et al. 2009

Acta Pharmacol Sin

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npg Introduction KCNQ4, a novel potassium channel, plays a part in regulating the membrane potential and function of various cell types in the body [1] . The KCNQ4 current is a low-threshold, slow activating and noninactivating current that is expressed in the outer hair cells of the cochlea, brain, and heart. Mutations in KCNQ4 give rise to an inherited syndrome of deafness [2] . Therefore, the regulatory pathways of KCNQ4 channels play an important role in adjusting the function of outer hair cells. The KCNQ gene subfamily is composed of five K + channels, KCNQ1 to KCNQ5. The KCNQ4 channel was included in the Kv nomenclature as Kv 7.4 (voltage-gated potassium channel subunit Kv7.4) [3] . The heteromers of KCNQ2/KCNQ3 underlie the neuronal M-current, which modulates neuronal excitability. Many intracellular messengers, eg, PIP2, IP3, diacylglycerol (DAG), calmodulin, calcineurin, activators/inhibitors of PKC, tyrosine kinases, and myosin light chain kinase, have been reported to modulate M currents [4][5][6] . Moreover, the A-kinase-anchoring protein AKAP150, which binds PKC, facilitates the inhibition of KCNQ2 current [7] . Analysis of recombinant KCNQ2 channels suggests that targeting of PKC through association with AKAP150 is important for inhibition. However, the effect of PKC activation on KCNQ channels is still controversial [8] . The inhibition of the metabolism of DAG by DAG kinase blockers cannot mimic the effect of muscarinic modulation by muscarinic agonist, and it has been suggested Aim: KCNQ4 channels play an important part in adjusting the function of cochlear outer hair cells. The aim of this study was to investigate the effects of ser/thr phosphatase inhibitors on human KCNQ4 channels expressed in Xenopus laevis oocytes. Methods: Synthetic cRNA encoding human KCNQ4 channels was injected into Xenopus oocytes. We used a two-electrode voltage clamp to measure the ion currents in the oocytes. Results: Wild-type KCNQ4 expressed in Xenopus oocytes showed the typical properties of slow activation kinetics and low threshold activation. The outward K + current was almost completely blocked by a KCNQ4 blocker, linopirdine (0.25 mmol/L). BIMI (a PKC inhibitor) prevented the effects of PMA (a PKC activator) on the KCNQ4 current, indicating that PKC may be involved in the regulation of KCNQ4 expressed in the Xenopus oocyte system. Treatment with the ser/thr phosphatase inhibitors, cyclosporine (2 µmol/L), calyculin A (2 µmol/L) or okadaic acid (1 µmol/L), caused a significant positive shift in V 1/2 and a decrease in the conductance of KCNQ4 channels. The V 1/2 was shifted from -14.6±0.5 to -6.4±0.4 mV by cyclosporine, -18.8±0.5 to -9.2±0.4 mV by calyculin A, and -14.1±0.5 to -0.7±0.6 mV by okadaic acid. Moreover, the effects of these phosphatase inhibitors (okadaic acid or calyculin A) on the induction of a positive shift of V 1/2 were augmented by further addition of PMA. Conclusion: These results indicate that ser/thr phosphatase inhibitors can induce a shift to more positive potentials of the activation ...

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International Union of Pharmacology. XLI. Compendium of Voltage-Gated Ion Channels: Potassium Channels

Cited by 351 publications

References 4 publications

KChIPs and Kv4 α Subunits as Integral Components of A-Type Potassium Channels in Mammalian Brain

KChIPs and Kv4 α Subunits as Integral Components of A-Type Potassium Channels in Mammalian Brain

Physiologie, pharmacologie et modélisation de canaux potassiques

Functional study of the effect of phosphatase inhibitors on KCNQ4 channels expressed in Xenopus oocytes

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