• Title, Summary, Keyword: Inwardly rectifying $K^+$ channels

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Inwardly Rectifying $K^+$ Currents in Gastric Myocytes of Guinea-pig

  • Jun, Jae-Yeoul;Yeum, Cheol-Ho;Yoon, Pyung-Jin;Jang, In-Youb;Cho, Nam-Soo;Cho, Soo-Hyeong;Kong, In-Deok;Kim, Tae-Wan;So, In-Suk;Kim, Ki-Whan
    • The Korean Journal of Physiology and Pharmacology
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    • v.6 no.1
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    • pp.47-55
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    • 2002
  • To identify the presence of inwardly rectifying $K^+$ channels and its characteristics, membrane currents were measured using a whole-cell patch clamp from isolated gastric myocytes of guinea-pig. Change of external $K^+$ concentration from 5 to 90 mM induced an inward current at a holding potential of -80 mV. The high $K^+-induced$ inward current was blocked by $Ba^{2+}$ and $Cs^+,$ but not by glibenclamide. With 90 mM $K^+$ in bath, the $Ba^{2+}-$ and $Cs^+-sensitive$ currents showed strong inward rectification. Ten mM TEA weakly blocked the inward current only at potentials more negative than -50 mV. With 90 mM $K^+$ in bath, hyperpolarizing step pulses from -10 mV induced inward currents, which were inactivated at potentials more negative than -70 mV. Reduction of external $K^+$ to 60 mM decreased the amplitudes of the currents and shifted the reversal potential to more negative potential. The inactivation of inward $K^+$ current at negative clamp voltage was not affected by removing external $Na^+.$ These results suggest that the inwardly rectifying $K^+$ channels may exist in gastric smooth muscle.

Regulation of G-protein Coupled Inwardly Rectifying $K^+$ Channel Expressed in HEK 293 Cell by Phosphorylation

  • Kim, Jae-Hoon;Park, Choon-Ok;Kim, Yeon-Woong;Hong, Seong-Geun
    • Proceedings of the Korean Biophysical Society Conference
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    • pp.40-41
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    • 1998
  • Acetylcholine-activated $K^{+}$ ($K_{ACh}$) channels has been introduced as a typical G protein ( $G_{K}$)-coupled inwardly rectifying $K^{+}$ (GIRK) channel, which constructs with four subunit composed of two types of GIRK isoforms, GIRK1 and GIRK4 (or CIR) for the atrial $K_{ACh}$ channel.(omitted)d)d)d)

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DAMGO modulates two-pore domain K+ channels in the substantia gelatinosa neurons of rat spinal cord

  • Cho, Pyung Sun;Lee, Han Kyu;Lee, Sang Hoon;Im, Jay Zoon;Jung, Sung Jun
    • The Korean Journal of Physiology and Pharmacology
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    • v.20 no.5
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    • pp.525-531
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    • 2016
  • The analgesic mechanism of opioids is known to decrease the excitability of substantia gelatinosa (SG) neurons receiving the synaptic inputs from primary nociceptive afferent fiber by increasing inwardly rectifying $K^+$ current. In this study, we examined whether a ${\mu}$-opioid agonist, [D-Ala2,N-Me-Phe4, Gly5-ol]-enkephalin (DAMGO), affects the two-pore domain $K^+$ channel (K2P) current in rat SG neurons using a slice whole-cell patch clamp technique. Also we confirmed which subtypes of K2P channels were associated with DAMGO-induced currents, measuring the expression of K2P channel in whole spinal cord and SG region. DAMGO caused a robust hyperpolarization and outward current in the SG neurons, which developed almost instantaneously and did not show any time-dependent inactivation. Half of the SG neurons exhibited a linear I~V relationship of the DAMGO-induced current, whereas rest of the neurons displayed inward rectification. In SG neurons with a linear I~V relationship of DAMGO-induced current, the reversal potential was close to the $K^+$ equilibrium potentials. The mRNA expression of TWIK (tandem of pore domains in a weak inwardly rectifying $K^+$ channel) related acid-sensitive $K^+$ channel (TASK) 1 and 3 was found in the SG region and a low pH (6.4) significantly blocked the DAMGO-induced $K^+$ current. Taken together, the DAMGO-induced hyperpolarization at resting membrane potential and subsequent decrease in excitability of SG neurons can be carried by the two-pore domain $K^+$ channel (TASK1 and 3) in addition to inwardly rectifying $K^+$ channel.

Localization of Divalent Cation-Binding Site in the Pore of a Small Conductance $Ca^{2+}$-activated $K^+$ Channel and Its Role in Determining Current-Voltage Relationship

  • Heun Soh;Shin, Na-Rae;Park, Chul-Seung
    • Proceedings of the Korean Biophysical Society Conference
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    • pp.33-33
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    • 2002
  • In our previous study (Soh and Park, 2001), we proposed that the inwardly rectifying current-voltage (I-V) relationship of small-conductance $Ca^{2+}$-activated $K^{+}$ channels (S $K_{Ca}$ channels) is the result of voltage-dependent blockade of $K^{+}$ currents by intracellular divalent cations. We expressed a cloned S $K_{Ca}$ channel, rSK2, in Xenopus oocytes and further characterized the nature of the divalent cation-binding site by electrophysiological means.(omitted)

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Block of ATP-Sensitive $K^+$ Channels Expressed in Xenopus Oocytes by Dimethyl Sulfoxide

  • Park, Jin-Bong;Chae, Soo-Wan
    • The Korean Journal of Physiology and Pharmacology
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    • v.5 no.2
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    • pp.157-163
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    • 2001
  • The effects of dimethyl sulfoxide (DMSO) were studied in two groups of Xenopus oocytes, one expressing ATP sensitive $K^+\;(K_{ATP})$ channel comprised of sulfonylurea receptor SUR1 and inwardly rectifying $K^+$ channel subunit Kir6.2, and the other expressing renal $K_{ATP}$ channel ROMK2. At concentrations of $0.3{\sim}10%$ (vol/vol) DMSO inhibited whole cell Kir6.2/SUR1 currents elicited by bath application of sodium azide (3 mM) in a concentration-dependent manner. The inhibition constant and Hill coefficient were 2.93% and 1.62, respectively. ROMK2 currents, however, was not affected significantly by DMSO. The results support the idea that DMSO inhibits $K_{ATP}$ channel expressed in Xenopus oocyte through a protein-specific mechanism(s) that remains to be further elucidated.

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Expression and Characterization of G Protein-activated Inward Rectifier $K^+$ Channels in Xenopus Oocytes

  • Kim, Han-Seop;Lee, Chang-Ho;Min, Churl K.
    • Animal cells and systems
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    • v.2 no.4
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    • pp.471-476
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    • 1998
  • The G protein-activated inwardly rectifying $K^+$ channel (GIRK1) was coex-pressed in Xenopus oocytes along with the $5-HT_{1A}$ receptor, a 7-helix receptor known to be coupled to $K^+$ channels in many neural tissues. Thus, the activation of the $5-HT_{1A}$ receptor by its agonist leads to the opening of GIRK1. The GIRK1 current was measured using the two electrode voltage clamp technique with bath application of 5-HT in the presence of various external potassium concentrations $[K^+]_0$. GIRK1 showed a strong inward rectification since only hyperpolarizing voltages evoked inward currents. $K^{+}$ was the major ion carrier as evidenced by about 44㎷ voltage shift corresponding to a 10-fold external 〔$K^+$〕 change. 5-HT induced a concentration-dependent inward $K^+$ current ($EC_{50}{\equation omitted}10.7nM$) which was blocked by $Ba^{2+}$. Pertussis toxin (PTX) pre-treatment reduced the $K^+$ current by as much as about 70%, suggesting that PTX-sensitive G protein ($G_i or G_o$ type) are involved in the $5-HT_{1A}$ receptor-GIRK1 coupling in Xenopus oocytes.

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Regulation of Adenosine-activated GIRK Channels by Gq-coupled Receptors in Mouse Atrial Myocytes

  • Cho, Ha-Na
    • The Korean Journal of Physiology and Pharmacology
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    • v.14 no.3
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    • pp.145-150
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    • 2010
  • Adenosine (Ado) is an important mediator of the endogenous defense against ischemia-induced injury in the heart. The action of Ado is mediated by activation of G protein-gated inwardly rectifying $K^+$ (GIRK) channels. In turn, GIRK channels are inhibited by reducing phosphatidylinositol 4,5-bisphosphate ($PIP_2$) through Gq protein-coupled receptors (GqPCRs). We previously found that GIRK channels activated by acetylcholine, a muscarinic M2 acetylcholine receptor agonist, are inhibited by GqPCRs in a receptor-specific manner. However, it is not known whether GIRK channels activated by Ado signaling are also regulated by GqPCRs. Presently, this was investigated in mouse atrial myocytes using the patch clamp technique. GIRK channels were activated by $100\;{\mu}M$ Ado. When Ado was repetitively applied at intervals of 5~6 min, the amplitude of second Ado-activated GIRK currents ($I_{K(Ado)}$) was $88.3{\pm}3.7%$ of the first $I_{K(Ado)}$ in the control. Pretreatment of atrial myocytes with phenylephrine, endothelin-1, or bradykinin prior to a second application of Ado reduced the amplitude of the second $I_{K(Ado)}$ to $25.5{\pm}11.6%$, $30.5{\pm}5.6%$, and $96.0{\pm}2.7%$, respectively. The potency of $I_{K(Ado)}$ inhibition by GqPCRs was different with that observed in acetylcholine-activated GIRK currents ($I_{K(ACh)}$) (endothelin-1>phenylephrine>bradykinin). $I_{K(Ado)}$ was almost completely inhibited by $500\;{\mu}M$ of the $PIP_2$ scavenger neomycin, suggesting low $PIP_2$ affinity of $I_{K(Ado)}$. Taken together, these results suggest that the crosstalk between GqPCRs and the Ado-induced signaling pathway is receptor-specific. The differential change in $PIP_2$ affinity of GIRK channels activated by Ado and ACh may underlie, at least in part, their differential responses to GqPCR agonists.

[$Ca^{2+}$ Signalling in Endothelial Cells: Role of Ion Channels

  • Nilius, Bernd;Viana, Felix;Kamouchi, Masahiro;Fasolato, Cristina;Eggermont, Jan;Droogmans, Guy
    • The Korean Journal of Physiology and Pharmacology
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    • v.2 no.2
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    • pp.133-145
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    • 1998
  • $Ca^{2+}-signals$ in endothelial cells are determined by release from intracellular stores and entry through the plasma membrane. In this review, the nature of $Ca^{2+}$ entry and mechanisms of its control are reviewed. The following ion channels play a pivotal role in regulation of the driving force for $Ca^{2+}$ entry: an inwardly rectifying $K^+$ channel, identified as Kir2.1, a big-conductance, $Ca^{2+}-activated$ $K^+$ channel (hslo) and at least two $Cl^-$ channels (a volume regulated $Cl^-$ channel, VRAC, and a $Ca^{2+}$ activated $Cl^-$ channel, CaCC). At least two different types of $Ca^{2+}$-entry channels exist: 1. A typical CRAC-like, highly selective $Ca^{2+}$ channel is described. Current density for this $Ca^{2+}$ entry is approximately 0.1pA/pF at 0 mV and thus 10 times smaller than in Jurkat or mast cells. 2. Another entry pathway for $Ca^{2+}$ entry is a more non-selective channel, which might be regulated by intracellular $Ca^{2+}$. Although detected in endothelial cells, the functional role of trp1,3,4 as possible channel proteins is unclear. Expression of trp3 in macrovascular endothelial cells from bovine pulmonary artery induced non-selective cation channels which are probably not store operated or failed to induce any current. Several features as well as a characterisation of $Ca^{2+}$-oscillations in endothelial cells is also presented.

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