• Title/Summary/Keyword: 이온 통로

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EPBS를 이용한 이온채널 단백질의 전하분포와 유전율이 이온 선택성에 미치는 영향 계산

  • Choe, Hyeong-Su;Nam, Min-U
    • Proceeding of EDISON Challenge
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    • 2014.03a
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    • pp.75-88
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    • 2014
  • 본 연구에서는 비선형 Poisson-Boltzmann 식의 해를 구할 수 있는 웹 기반 EPBS를 이용하여 이온채널의 전하 분포와 유전률이 이온채널의 이온선택성에 미치는 영향에 대해 알아본다. 모델로 사용한 이온채널은 이온채널과 유사한 구조를 갖는 합성 단백질인 고리형 펩타이드 나노튜브와 자연계에 존재하는 Gramicidin A 이다. 계산 결과로부터 용매인 물과 단백질의 유전율 차이에 의해 이온이 이온채널을 통과할 때 반응장이 생성되며, 이는 이온과 상호작용을 통해 이온 종류에 관계없이 이온 통과를 방해하는 에너지 장벽을 형성함을 알 수 있다. 한편, 두 이온채널 부분 전하, 특히 골격에 존재하는 카르보닐기의 쌍극자 모멘트에 의해 이온채널 내부에는 0 보다 작은 정전기 퍼텐셜이 형성된다. 이온채널 내부의 총 정전기 퍼텐셜은 이온채널의 부분 전하에 의한 정전기 퍼텐셜과 유전률 차이에 의한 반응장의 합으로 나타나며, 계산 결과 0 보다 작은 값을 갖는다. 이로부터 본 연구에서 사용된 두 종류의 이온채널이 양이온에 선택성이 있음을 알 수 있다.

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Inhibitory Effect of $Zn^{+2}$ on Tolaasin-induced Hemolysis ($Zn^{+2}$에 의한 Tolaasin의 용혈활성 저해효과)

  • Cho, Kwang-Hyun;Kim, Sung-Tae;Kim, Young-Kee
    • Applied Biological Chemistry
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    • v.49 no.4
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    • pp.281-286
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    • 2006
  • Tolaasin, a pore-forming toxin, is a 1,985 Da peptide produced by Pseudomonas tolaasii and causes a brown blotch disease on cultivated mushrooms. Tolaasin forms pores on the plasma membrane of various cells including fungi, bacteria, plant as well as erythrocytes, and destroys cell structure. $Zn^{+2}$ has been known to block the tolaasin activity by an unknown mechanism. Thus, we investigated the inhibitory effects of $Zn^{+2}$ on the tolaasin-induced hemolysis to understand the molecular mechanism of tolaasin-induced pore formation. $Zn^{+2}$ and $Cd^{+2}$ inhibited the tolaasin-induced hemolysis in a dose-dependent manner and their Ki values were 170 ${\mu}M$ and 20 mM, respectively. The effect of $Zn^{+2}$ was reversible since the subsequent addition of EDTA chelates $Zn^{+2}$ and removes the inhibitory effect of $Zn^{+2}$. When an osmotic protectant, PEG 2000, was added, the tolaasin-induced hemolysis was not observed. After the removal of osmotic protectant by centrifugation, resuspended erythrocytes with fresh medium were immediately hemolyzed, while the addition of $Zn^{+2}$ prevented from hemolysis, implying that tolaasin-induced pores on the membrane were already formed in the medium containing osmotic protectant. These results suggest that $Zn^{+2}$ inhibits the activity of tolaasin pores and it has minor effects on the membrane binding of tolaasin and the formation of pore.

Dose-dependent suppression of tolaasin-induced hemolysis by gadolinium ion (가돌리니움 이온에 의한 톨라신 용혈활성의 농도의존적 억제)

  • Huh, Jeong-Hoon;Yun, Yeong-Bae;Kim, Young-Kee
    • Journal of Applied Biological Chemistry
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    • v.64 no.4
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    • pp.369-374
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    • 2021
  • Brown blotch disease of oyster mushrooms is caused by tolaasin and its analog peptide toxins which are produced by Pseudomonas tolaasii. Tolaasin peptides form pores in the plasma membrane and destroy the fruiting body structure of mushroom. Lysis of red blood cells, hemolysis, can be occurred by cytotoxic activity of tolaasin. The hemolytic activity of tolaasin is inhibited by metal ions, such as Zn2+ and Ni2+. When Gadolinium ion was added, a biphasic effect was observed on tolaasin-induced hemolysis, an increase in hemolysis at submillimolar concentrations and an inhibition at millimolar concentrations. The mechanism of gadolinium ion-induced inhibition of tolaasin activity may not be similar to those of the inhibitions by other metal ions. Since gadolinium ion has been reported to change a lateral pressure of lipid membrane by binding to the negative charges of membrane lipids, it may not directly work on the tolaasin channel gating, but rather decrease the stability of tolaasin channel by increasing firmness of membrane.

Activation of polymer electrolyte membrane fuel cells (고분자 전해질 연료전지의 활성화)

  • Ko, Jae-Jun;Ko, Haeng-Jin;Song, Min-Kyu;Yang, Yu-Chang;Lee, Jong-Hyun
    • 한국신재생에너지학회:학술대회논문집
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    • 2005.06a
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    • pp.330-334
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    • 2005
  • 고분자 전해질막 연료전지는 운전시 정상적인 성능을 발현하기 이해서 전지 본체 조립 후 초기 활성화 운전이 필요하다. 이러한 활성화 운전을 통해 전해질 사이의 수소이온이동 통로, 반응가스가 반응할 수 있는 촉매까지의 이동 통로, 촉매층내의 전기적 연속성을 확보함으로 연료전지는 최적의 성능을 나타낼 수 있다. 본 연구를 통해 연료전지 활성화에 영향을 미치는 요인을 찾았고, 이를 통해 효과적이고 빠른 활성화 절차에 관한 연구를 수행하였다.

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Activation of polymer electrolyte membrane fuel cells (고분자 전해질 연료전지의 활성화)

  • Ko, Jae-Jun;Ko, Haeng-Jin;Song, Min-Kyu;Yang, Yu-Chang;Lee, Jong-Hyun
    • New & Renewable Energy
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    • v.1 no.2 s.2
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    • pp.34-40
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    • 2005
  • 고분자 전해질막 연료전지는 운전시 정상적인 성능을 발현하기 위해서 전지 본체 조립 후 초기 활성화 운전이 필요하다. 이러한 활성화 운전을 통해 전해질 사이의 수소이온이동 통로, 반응가스가 반응할 수 있는 촉매까지의 이동 통로, 촉매층내의 전기적 연속성을 확보함으로 연료전지는 최적의 성능을 나타낼 수 있다. 본 연구를 통해 연료전지 활성화에 영향을 미치는 요인을 찾았고, 이를 통해 효과적이고 빠른 활성화 절차에 관한 연구를 수행하였다.

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Phosphorylation as a Signal Transduction Pathway Related with N-channel Inactivation in Rat Sympathetic Neurons (N형 칼슘통로 비활성화와 연계된 세포 신호전달 체계로서의 인산화과정)

  • Lim Wonil;Goo Yong Sook
    • Progress in Medical Physics
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    • v.15 no.4
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    • pp.220-227
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    • 2004
  • In N-type $Ca^{2+}$ channels, the mechanism of inactivation - decline of inward current during a depolarizing voltage step- is still controversial between voltage-dependent inactivation and $Ca^{2+}$ -dependent inactivation. In the previous paper we demonstrated that fast component of inactivation of N-type calcium channels does not involve classic $Ca^{2+}$ -dependent mechanism and the slowly inactivating component could result from a $Ca^{2+}$ -dependent process. However, there should be signal transduction pathway which enhances inactivation no matter what the inactivation mechanism is. We have investigated the effect of phosphorylation on calcium channels of rat sympathetic neurons. Intracellular dialysis with the phosphatase inhibitors okadaic acid markedly enhanced the inactivation. The rapidly inactivating component is N-type calcium current, which is blocked by $\omega$-conotoxin GVIA. Staurosporine, a nonselective protein kinase inhibitor, prevented the action of okadaic acid, suggesting that protein phosphorylation is involved. More specifically lavendustin C, inhibitor of CaM kinase II, prevented the action of okadaic acid, suggesting that calmodulin dependent pathway is involved in inactivation process. It is not certain to this point whether phosphorylation process is inactivation itself. Molecular biological research regarding binding site should be followed to address the question of how the divalent cation binding site is related to phoshorylation process.

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이달의 과학자-서울대 약학대 약학과 오우택 박사

  • Korean Federation of Science and Technology Societies
    • The Science & Technology
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    • v.31 no.3 s.346
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    • pp.66-67
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    • 1998
  • 고추의 매운 성분인 캡사이신이 통각신경을 흥분시켜 통증을 일으킨다는 사실을 밝혀낸 서울대 약학대 오우택 교수. 오 교수는 지난해 세계 최초로 통각신경의 세포막에서 캡사이신이온통로를 발견해 전 세계에서 관심을 모았다. 83년 오클라호마대학 의과대학에 유학한 이후 15년 동안 통증연구를 해온 오 교수는 왜 캡사이신통로가 우리 몸에 있는가 하는 의문을 규명하기 위한연구를 계속하고 있다.

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Transported Metal ton by Crown Ether through Liquid Membrane (Crown Ether에 의한 액체막을 통해서 금속이온의 수송)

  • 남기열;류정욱이기창홍장후
    • KSBB Journal
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    • v.8 no.4
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    • pp.370-374
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    • 1993
  • In transportation the amount of metal ion by crown ethers, dibenzo-18-crown-6 were investigated using ultraviolet spectrometer. Transported the amount of one valence metal ion as $K^+ and Li^+}$ was not so much. On the other hand, two valence metal ion increased by dibenzo-18-crown-6, which means that the ionic charge and hydration of two valence metal ion affected the carrying ability of crown ethers. The carrying ability of dibenzo-18-crown-6 was, therefore, adequate for two valence metal ion as $Ca^{2+}$ and $Ba^{2+}$. It was also suggested that transport metal ion by crown ethers, which is related rather the catching ability than the selectivity of metalion.

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Properties of stretch-activated $K^+$ channels in an G292 osteoblast-like cell (G292 세포에서 세포막 신장으로 활성화되는 $K^+$통로의 특성)

  • Lee, Sang-Gook;Jung, Dong-Keun;Suh, Duk-Joon;Park, Soo-Byung
    • The korean journal of orthodontics
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    • v.30 no.2 s.79
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    • pp.197-204
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    • 2000
  • [$K^+$]-selective ion channels were studied in excised inside-out membrane patches from human osteoblast-like cells (G292). Three classes of $K^+$channels were present and could be distinguished on the basis of conductance. Conductances were $270\pm27\;pS,\;113\pm12\;pS,\;48\pm8\;pS$ according to their approximate conductances in symmetrical 140 mM KCl saline at holding potential of -80 mV It was found that the small conductance (48 pS) $K^+$channel activation was dependent on membrane voltage. In current-voltage relationship, small conductance $K^+$channel showed outward rectification, and it was activated by the positive potential inside the membrane. In recordings, single channel currents were activayed by a negative pressure outside the membrane. The membrane pressure increased $P_{open}$ of the $K^+$ channel in a pressure-dependent manner. In the excised-patch clamp recordings, G292 osteoblast-like cells have been shown to contain three types of $K^+$ channels. Only the small conductance (48 pS) $K^+$channel is sensitive to the membrane stretch. These findings suggest that a hyperpolarizing current, mediated in part by this channel, may be associated with early events during the mechanical loading of the osteoblast. In G292 osteoblast-like cells, $K^+$channel is sensitive to membrane tension, and may represent a unique adaptation of the bone cell membrane to mechanical stress.

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