• The Korean Journal of Physiology and Pharmacology
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• 제6권1호
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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.

• 한국동물학회:뉴스레터
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• 제12권2호
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• pp.108.2-108
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• 1995

No Abstract, See Full Text

• 한국동물학회:학술대회논문집
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• 한국동물학회 1995년도 한국생물과학협회 학술발표대회
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• pp.244.2-244
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• 1995

No Abstract, See Full Text

• The Korean Journal of Physiology and Pharmacology
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• 제20권5호
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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.

• 한국생물물리학회:학술대회논문집
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• 한국생물물리학회 1998년도 학술발표회
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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)

• 한국생물물리학회:학술대회논문집
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• 한국생물물리학회 2002년도 제9회 학술 발표회 프로그램과 논문초록
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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)

• Restorative Dentistry and Endodontics
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• 제27권3호
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• pp.215-231
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• 2002

삼차신경절의 뉴론이 구강악안면영역에서의 촉각, 압각, 온도각 및 통각 등 다양한 감각을 중추신경계로 전달하는 역할을 하는 것은 주지의 사실이다. 이러한 신경전달에 있어서 이온통로는 감각정보를 전달하는데 핵심적인 역할을 수행한다. 이 중 소디움 통로는 활동전위의 발생에 중요하며, 칼슘 통로는 시냅스 전도에 있어서 필수적인 역할을 수행하고, 포타슘 통로는 안정막전압의 유지 및 재분극에 관여한다. 최근에 여러 가지의 이온통로들의 뇌조직내의 분포에 관한 연구가 시작되고 있는데 삼차신경의 일차구심뉴론이 종지하는 삼차신경핵 즉 삼차신경 척수감각핵, 삼차신경 주감각핵, 삼차신경 중뇌핵 및 삼차신경 운동핵에 존재하는 이온통로에 관한 연구는 매우 희소하여 본 연구에서는 횐쥐의 삼차신경 핵에 존재하는 소디움, 칼슘 및 포타슘 이온통로들을 면역조직화학적 방법으로 조사하여 다음과 같은 결과를 얻었다. (1) 소디움 통로는 삼차신경 척수감각핵, 삼차신경 주감각핵 및 삼차신경 운동핵 모두에서 강하게 염색되었다. (2) 칼슘 통로는 삼차신경 척수감각핵에서는 N-type 통로가 중등도로 염색되었으며 , P/Q-type 통로는 약하게 염색되었으나 R-type 통로는 거의 염색되지 않았다. 삼차신경 주감각핵에서는 P/Q-type 통로가 매우 약하게 염색되었다. (3) 포타슘 통로는 삼차신경 척수감각핵과 삼차신경 주감각핵에서 inwardly rectifying 포타슘 통로(Kir 2.1)가 중등도로 염색되었고, voltage-gated 포타슘 통로(Kv 4.2)가 약하게 염색되었으며, BKCa는 그 염색 정도가 매우 약하게 나타났다. 이상의 결과를 종합해 볼 때 삼차신경 감각핵에는 소디움 통로의 분포가 가장 많았으며, 칼슘통로에서는 N-type이, 포타슘 통로 중에는 inwardly rectifying 통로(Kir 2.1)가 가장 많이 분포함을 관찰할 수 있었다.

• ALGAE
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• 제36권4호
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• pp.315-326
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• 2021

Ion channels are membrane protein complexes mediating passive ion flux across the cell membranes. Every organism has a certain set of ion channels that define its physiology. Dinoflagellates are ecologically important microorganisms characterized by effective physiological adaptability, which backs up their massive proliferations that often result in harmful blooms (red tides). In this study, we used a bioinformatics approach to identify homologs of known ion channels that belong to 36 ion channel families. We demonstrated that the versatility of the dinoflagellate physiology is underpinned by a high diversity of ion channels including homologs of animal and plant proteins, as well as channels unique to protists. The analysis of 27 transcriptomes allowed reconstructing a consensus ion channel repertoire (channelome) of dinoflagellates including the members of 31 ion channel families: inwardly-rectifying potassium channels, two-pore domain potassium channels, voltage-gated potassium channels (K_v), tandem K_v, cyclic nucleotide-binding domain-containing channels (CNBD), tandem CNBD, eukaryotic ionotropic glutamate receptors, large-conductance calcium-activated potassium channels, intermediate/small-conductance calcium-activated potassium channels, eukaryotic single-domain voltage-gated cation channels, transient receptor potential channels, two-pore domain calcium channels, four-domain voltage-gated cation channels, cation and anion Cys-loop receptors, small-conductivity mechanosensitive channels, large-conductivity mechanosensitive channels, voltage-gated proton channels, inositole-1,4,5-trisphosphate receptors, slow anion channels, aluminum-activated malate transporters and quick anion channels, mitochondrial calcium uniporters, voltage-dependent anion channels, vesicular chloride channels, ionotropic purinergic receptors, animal volage-insensitive cation channels, channelrhodopsins, bestrophins, voltage-gated chloride channels H⁺/Cl^- exchangers, plant calcium-permeable mechanosensitive channels, and trimeric intracellular cation channels. Overall, dinoflagellates represent cells able to respond to physical and chemical stimuli utilizing a wide range of G-protein coupled receptors- and Ca²⁺-dependent signaling pathways. The applied approach not only shed light on the ion channel set in dinoflagellates, but also provided the information on possible molecular mechanisms underlying vital cellular processes dependent on the ion transport.

• The Korean Journal of Physiology and Pharmacology
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• 제5권2호
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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.

• Animal cells and systems
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• 제2권4호
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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.