• Title/Summary/Keyword: Membrane binding

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Mutant and Its Functional Revertant Signal Peptides of Escherichia coli Ribose Binding Protein Show the Differences in the Interaction with Lipid Bilayer

  • Oh, Doo-Byoung;Taeho Ahn;Kim, Hyoung-Man
    • Proceedings of the Korean Biophysical Society Conference
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    • 1999.06a
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    • pp.43-43
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    • 1999
  • Signal peptides of secretary proteins interact with various membranes and non-membrane components during the translocation. We investigated the interaction of signal peptides of ribose binding protein (RBP) with Escherichia coli (E.coli) signal recognition particle (SRP), SecA and lipid bilayer. Previous studies showed that the functional signal peptides inhibit the GTPase activity of E.coli SRP which consisted of F로 and 4.5S RNA.(omitted)

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Effect of Juglans sinensis Dode aquacupuncture(JS) on t-butylhydroperoxide-induced alterations in membrane transport function in renal epithelial cells (신장상피세포(腎臟上皮細胞)에서 호도약침액(胡桃藥鍼液)이 t-Butylhydroperoxide에 의한 세포막물질이동계(細胞膜物質移動系)의 장애(障碍)에 미치는 영향(影響))

  • Narm, Sang-pil;Cho, Tai-sung;Kim, Cheol-hong;Youn, Hyoun-min;Jang, Kyung-jeon;Song, Choon-ho;Ahn, Chang-beohm
    • Journal of Acupuncture Research
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    • v.20 no.6
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    • pp.128-139
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    • 2003
  • Juglans sinensis Dode has been reported to have antioxidant activity. However, the effect of Juglans sinensis Dode aquacupuncture(JS) on reactive oxygen species(ROS)-induced alterations in membrane transport function in renal tubular cells. This study was performed to evaluate the effect of JS on the organic hydroperoxide t-butylhydroperoxide(tBHP)-induced inhibition of $Na^+$-dependent phosphate($Na^+$-Pi) uptake in opossum kidney (OK) cells, an established renal proximal epithelial cell line. tBHP inhibited $Na^+$-Pi uptake in a time-dependent manner. The inhibitory effect of tBHP was prevented by JS over concentration range of 0.05-1mg/100ml in a dose-dependent manner. Kinetic studies showed that tBHP caused an decrease in Vmax for $Na^+$-Pi uptake without any a significant change in Km. $Na^+$-dependent phosphonoformic acid binding, a irreversible inhibitor of renal $Na^+$-Pi uptake, was decreased by tBHP treatment. The reduction in Vmax and phosphonoformic acid binding by tBHP was prevented by JS. tBHP induced lipid peroxidation and its effect was completely inhibited by JS and antioxidant N,N'-diphenyl-p-phenylenediamine. These data suggest that the oxidant inhibits phosphate uptake by a reduction in the number of active carrier across the membrane. JS may prevent oxidant-induced inhibition of membrane transport function by a mechanism similar to antioxidants in renal epithelial cells. Although the precise constituents remain to be explored, JS may be employed as a useful candidate herb for drug development to prevent and treat oxidant-mediated renal failure.

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Proteomic Analysis of Fructophilic Properties of Osmotolerant Candida magnoliae

  • Yu, Ji-Hee;Lee, Dae-Hee;Park, Yong-Cheol;Lee, Mi-Gi;Kim, Dae-Ok;Ryu, Yeon-Woo;Seo, Jin-Ho
    • Journal of Microbiology and Biotechnology
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    • v.18 no.2
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    • pp.248-254
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    • 2008
  • Candida magnoliae, an osmotolerant and erythritol producing yeast, prefers D-fructose to D-glucose as carbon sources. For the investigation of the fructophilic characteristics with respect to sugar transportation, a sequential extraction method using various detergents and ultracentrifugation was developed to isolate cellular membrane proteins in C. magnoliae. Immunoblot analysis with the Pma1 antibody and two-dimensional electrophoresis analysis coupled with MS showed that the fraction II was enriched with membrane proteins. Eighteen proteins out of 36 spots were identified as membrane or membrane-associated proteins involved in sugar uptake, stress response, carbon metabolism, and so on. Among them, three proteins were significantly upregulated under the fructose supplying conditions. The hexose transporter was highly homologous to Ght6p in Schizosaccharomyces pombe, which was known as a predominant transporter for the fructose uptake of S. pombe because it exhibited higher affinity to D-fructose than D-glucose. The physicochemical properties of the ATP-binding cassette transporter and inorganic transporter explained their direct or indirect associations with the fructophilic behavior of C. magnoliae. The identification and characterization of membrane proteins involved in sugar uptake might contribute to the elucidation of the selective utilization of fructose to glucose by C. magnoliae at a molecular level.

The Novel Biological Action of Antimicrobial Peptides via Apoptosis Induction

  • Cho, Jaeyong;Hwang, In-Sok;Choi, Hyemin;Hwang, Ji Hong;Hwang, Jae-Sam;Lee, Dong Gun
    • Journal of Microbiology and Biotechnology
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    • v.22 no.11
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    • pp.1457-1466
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    • 2012
  • Antimicrobial peptides (AMPs) exert antimicrobial activity against Gram-positive and Gram-negative bacteria, fungi, and viruses by various mechanisms. AMPs commonly possess particular characteristics by harboring cationic and amphipathic structures and binding to cell membranes, resulting in the leakage of essential cell contents by forming pores or disturbing lipid organization. These membrane disruptive mechanisms of AMPs are possible to explain according to the various structure forming pores in the membrane. Some AMPs inhibit DNA and/or RNA synthesis as well as apoptosis induction by reactive oxygen species (ROS) accumulation and mitochondrial dysfunction. Specifically, mitochondria play a major role in the apoptotic pathway. During apoptosis induced by AMPs, cells undergo cytochrome c release, caspase activation, phosphatidylserine externalization, plasma or mitochondrial membrane depolarization, DNA and nuclei damage, cell shrinkage, apoptotic body formation, and membrane blebbing. Even AMPs, which have been reported to exert membrane-active mechanisms, induce apoptosis in yeast. These phenomena were also discovered in tumor cells treated with AMPs. The apoptosis mechanism of AMPs is available for various therapeutics such as antibiotics for antibiotic-resistant pathogens that resist to the membrane active mechanism, and antitumor agents with selectivity to tumor cells.

Development and Application of Cation-exchange Membranes Including Chelating Resin for Efficient Heavy-metal Ion Removal (효율적인 중금속 이온 제거를 위한 킬레이팅 수지를 포함한 양이온 교환막의 개발 및 응용)

  • Kim, Do-Hyeong;Choi, Young-Eun;Park, Jin-Soo;Kang, Moon-Sung
    • Membrane Journal
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    • v.27 no.2
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    • pp.129-137
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    • 2017
  • In this study, we have developed cation-exchange membranes (CEMs) which can efficiently separate heavy-metal ions among the cations contained in a water system. Sulfonated polyetheretherketone (SPEEK) was used as a base polymer and a powdered chelating resin with strong binding ability to heavy-metal ions was added into it. In order to optimize the performance of the CEM, the content of chelating resin powder and the ion exchange capacity of SPEEK have been controlled. As a result, it was confirmed that the removal efficiency of heavy metal ion was improved by more than 20% by applying the CEM to membrane capacitive deionization (MCDI).

Deletion Analysis of the Major NF-${\kappa}B$ Activation Domain in Latent Membrane Protein 1 of Epstein-Barr Virus

  • Cho, Shin;Lee, Won-Keun
    • Journal of Microbiology
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    • v.37 no.4
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    • pp.256-262
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    • 1999
  • Latent membrane protein 1 (LMP1) of the Epstein-Barr virus (EBV) is an integral membrane protein with six transmembrane domains, which is essential for EBV-induced B cell transformation. LMP1 functions as a constitutively active tumor necrosis factor receptor (TNFR) like membrane receptor, whose signaling requires recruitment of TNFR-associated factors (TRAFs) and leads to NF-${\kappa}B$ activation. NF-${\kappa}B$ activation by LMP1 is critical for B cell transformation and has been linked to many phenotypic changes associated with EBV-induced B cell transformation. Deletion analysis has identified two NF-${\kappa}B$ activation regions in the carboxy terminal cytoplasmic domains of LMP1, termed CTAR1 (residues 194-232) and CTAR2 (351-386). The membrane proximal C-terminal domain was precisely mapped to a PXQXT motif (residues 204-208) involved in TRAF binding as well as NF-${\kappa}B$ activation. In this study, we dissected the CTAR2 region, which is the major NF-${\kappa}B$ signaling effector of LMP1, to determine a minimal functional sequence. A series of LMP1 mutant constructs systematically deleted for the CTAR2 region were prepared, and NF-${\kappa}B$ activation activity of these mutants were assessed by transiently expressing them in 293 cells and Jurkat T cells. The NF-${\kappa}B$ activation domain of CTAR2 appears to reside in a stretch of 6 amino acids (residues 379-384) at the end of the carboxy terminus.

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Blue light signaling in stomatal guard cells

  • Shimazaki, Ken-ichiro;Michio Doi;Toshinori Kinoshita
    • Journal of Photoscience
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    • v.9 no.2
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    • pp.86-89
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    • 2002
  • Blue light activates proton pump, and creates electrical gradient across the plasma membrane and drives $K^{+}$ uptake in stomatal guard cells. In this presentation, we provide evidence for regulatory mechanisms of the pump and the identification of blue light receptor. The pump is shown to be the plasma membrane H$^{+}$- ATPase and is activated through phosphorylation of the C-terminus. Phosphorylation occurred and 14-3-3 protein bound to the phosphorylation site. The binding of 14-3-3 protein was required for the H$^{+}$-ATPase activation. We also found that phot1 phot2 double mutant does not respond to blue light but other mutants respond to blue light by stomatal opening. However, all these mutants are capable of stomatal opening in the presence of fusicoccin, an activator of the H$^{+}$-ATPase. These results suggest that both photl and phot2 act as blue light receptors in guard cells.d cells.

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System-Wide Expression and Function of Olfactory Receptors in Mammals

  • Oh, S. June
    • Genomics & Informatics
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    • v.16 no.1
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    • pp.2-9
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    • 2018
  • Olfactory receptors (ORs) in mammals are generally considered to function as chemosensors in the olfactory organs of animals. They are membrane proteins that traverse the cytoplasmic membrane seven times and work generally by coupling to heterotrimeric G protein. The OR is a G protein-coupled receptor that binds the guanine nucleotide-binding $G{\alpha}_{olf}$ subunit and the $G{\beta}{\gamma}$ dimer to recognize a wide spectrum of organic compounds in accordance with its cognate ligand. Mammalian ORs were originally identified from the olfactory epithelium of rat. However, it has been recently reported that the expression of ORs is not limited to the olfactory organ. In recent decades, they have been found to be expressed in diverse organs or tissues and even tumors in mammals. In this review, the expression and expected function of olfactory receptors that exist throughout an organism's system are discussed.

Potentiometric Sensor for the Determination of Dibucaine in Pharmaceutical Preparations and Electrochemical Study of the Drug with BSA

  • Ensafi, Ali A.;Allafchian, A.R.
    • Bulletin of the Korean Chemical Society
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    • v.32 no.8
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    • pp.2722-2726
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    • 2011
  • Plasticized poly(vinyl chloride), PVCs, with different membrane compositions tested for use in the construction of an ion-selective sensor for the determination dibucaine. A prepared membrane with dioctyl phthalate-PVC and ion-pair of N-(1-naphthyl)ethylenediamine dihydrochloride-tetraphenyl borate had a good potential to acts as a potentiometric sensor for the analysis of dibucaine. A linear relationship was obtained between potential and logC varying between $1.0{\times}10^{-6}$ and $1.0{\times}10^{-2}$ M dibucaine with a good repeatability and reproducibility. The sensor was applied for the determination of the drug in pharmaceuticals and biological fluids such as plasma and urine samples with satisfactory results. The drug electrode has also been used to study the interaction of bovine serum albumin (BSA) with dibucaine. The saturated quantities of dibucaine binding were 13.04, 5.30 and 9.70 mol/mol in 0.01, 0.02 and 0.1% of protein, respectively.

Identification of Inhibitors Against BAK Pore Formation using an Improved in vitro Assay System

  • Song, Seong-Soo;Lee, Won-Kyu;Aluvila, Sreevidya;Oh, Kyoung Joon;Yu, Yeon Gyu
    • Bulletin of the Korean Chemical Society
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    • v.35 no.2
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    • pp.419-424
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    • 2014
  • The pro-apoptotic BCL-2 family protein BID activates BAK and/or BAX, which form oligomeric pores in the mitochondrial outer membrane. This results in the release of cytochrome c into the cytoplasm, initiating the apoptotic cascade. Here, we utilized liposomes encapsulating sulfo-rhodamine at a controlled temperature to improve upon a previously reported assay system with enhanced sensitivity and specificity for measuring membrane permeabilization by BID-dependent BAK activation. BAK activation was inhibited by BCL-$X_L$ protein but not by a mutant protein with impaired anti-apoptotic activity. With the assay system, we screened a chemical library and identified several compounds including trifluoperazine, a mitochondrial apoptosis-induced channel blocker. It inhibited BAK activation by direct binding to BAK and blocking the oligomerization of BAK.