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        Hypoxia inhibition of camptothecin-induced apoptosis by Bax loss

        Park, Kyoungsook,Woubit, Abdela,Fermin, Cesar,Reddy, Gopal,Habtemariam, Tsegaye,Chung, Jin,Park, Minseo,Seol, Dai-Wu,Kim, Moonil De Gruyter Open Sp. z o.o. 2012 BIOLOGIA -BRATISLAVA- Vol.67 No.3

        <B>Abstract</B><P>Tumor cell hypoxia is linked to the resistance of human solid tumors to the various anti-cancer therapies: thus, its exploitation has been considered to be a potential target for cancer treatment. Previously, we demonstrated for the first time that hypoxia inhibits apoptosis induced by tumor necrosis factor (TNF)-related apoptosis-inducing ligand (TRAIL) through blocking translocation of Bax, a pro-apoptotic protein, from the cytosol to the mitochondria. Nevertheless, the molecular mechanism coupling hypoxia to resistance for drugs, especially for anti-cancer chemotherapeutics, still remains to be elucidated. Here, we demonstrate that hypoxia attenuates camptothecin (CPT)-induced apoptosis by decreasing the protein levels of Bax, thereby leading to resistance to the drug. DNA damage after exposure to CPT resulted in an increase of p53, and a concomitant up-regulation of p21, regardless of oxygen content. Under normoxic condition, CPT induced expression of p53 and its down-stream target molecule Bax as well, in the presence of increased p21. In contrast, when preexposed to hypoxia, Bax-inducing activity of CPT was completely lost and the Bax level was even decreased, although CPT increased both p53 and p21 as observed under normoxic condition. Our data indicate that hypoxia attenuates apoptosis via Bax. Our data also suggest that hypoxia regulates tumor cell apoptosis differentially, through regulating Bax translocation or through down-regulating Bax levels, depending on death-inducing signals as shown by TRAIL- or CPT-induced apoptosis.</P>

      • KCI등재

        A Portable Surface Plasmon Resonance Biosensor for Rapid Detection of Salmonella typhimurium

        Hoang Hiep Nguyen,이소연,Abdela Woubit,김문일 한국진공학회 2016 Applied Science and Convergence Technology Vol.25 No.3

        Here, the rapid detection of Salmonella typhimurium by a portable surface plasmon resonance (SPR) biosensor in which the beam from a diode laser is modulated by a rotating mirror is reported. Using this system, immunoassay based on lipopolysaccharides (LPS)-specific monoclonal anti-Salmonella antibody was performed. For the purpose of orientation-controlled immobilization of antibodies on the SPR chip surface, the cysteine-mediated immobilization method, which is based on interaction between a gold surface and a thiol group (-SH) of cysteine, was adopted. As a result, using the portable SPR-based immunoassay, we detected S. typhimurium in the range from 10^7 CFU/mL to 10^9 CFU/mL within 1 hour. The results indicate that the portable SPR system could be potentially applied for general laboratory detection as well as on-site monitoring of foodborne, clinical, and environmental agents of interest.

      • KCI우수등재

        Applications of Field-Effect Transistor (FET)-Type Biosensors

        Park, Jeho,Nguyen, Hoang Hiep,Woubit, Abdela,Kim, Moonil The Korean Vacuum Society 2014 Applied Science and Convergence Technology Vol.23 No.2

        A field-effect transistor (FET) is one of the most commonly used semiconductor devices. Recently, increasing interest has been given to FET-based biosensors owing totheir outstanding benefits, which are likely to include a greater signal-to-noise ratio (SNR), fast measurement capabilities, and compact or portable instrumentation. Thus far, a number of FET-based biosensors have been developed to study biomolecular interactions, which are the key drivers of biological responses in in vitro or in vivo systems. In this review, the detection principles and characteristics of FET devices are described. In addition, biological applications of FET-type biosensors and the Debye length limitation are discussed.

      • KCI등재

        Applications of Field-Effect Transistor (FET)-Type Biosensors

        박제호,김문일,Hoang Hiep Nguyen,Abdela Woubit 한국진공학회 2014 Applied Science and Convergence Technology Vol.23 No.2

        A field-effect transistor (FET) is one of the most commonly used semiconductor devices. Recently, increasing interest has been given to FET-based biosensors owing totheir outstanding benefits, which are likely to include a greater signal-to-noise ratio (SNR), fast measurement capabilities, and compact or portable instrumentation. Thus far, a number of FET-based biosensors have been developed to study biomolecular interactions, which are the key drivers of biological responses in in vitro or in vivo systems. In this review, the detection principles and characteristics of FET devices are described. In addition, biological applications of FET-type biosensors and the Debye length limitation are discussed.

      • KCI우수등재

        A Portable Surface Plasmon Resonance Biosensor for Rapid Detection of Salmonella typhimurium

        Nguyen, Hoang Hiep,Yi, So Yeon,Woubit, Abdela,Kim, Moonil The Korean Vacuum Society 2016 Applied Science and Convergence Technology Vol.25 No.3

        Here, the rapid detection of Salmonella typhimurium by a portable surface plasmon resonance (SPR) biosensor in which the beam from a diode laser is modulated by a rotating mirror is reported. Using this system, immunoassay based on lipopolysaccharides (LPS)-specific monoclonal anti-Salmonella antibody was performed. For the purpose of orientation-controlled immobilization of antibodies on the SPR chip surface, the cysteine-mediated immobilization method, which is based on interaction between a gold surface and a thiol group (-SH) of cysteine, was adopted. As a result, using the portable SPR-based immunoassay, we detected S. typhimurium in the range from 10^7 CFU/mL to 10^9 CFU/mL within 1 hour. The results indicate that the portable SPR system could be potentially applied for general laboratory detection as well as on-site monitoring of foodborne, clinical, and environmental agents of interest.

      • Combination of cysteine- and oligomerization domain-mediated protein immobilization on a surface plasmon resonance (SPR) gold chip surface

        Park, Kyoungsook,Lee, Jeong Min,Jung, Yongwon,Habtemariam, Tsegaye,Salah, Abdela Woubit,Fermin, Cesar D.,Kim, Moonil Royal Society of Chemistry 2011 The Analyst Vol.136 No.12

        <P>Here we report an effective method for protein immobilization on a surface plasmon resonance (SPR) gold chip, describing the combination of cysteine- and oligomerization domain-mediated immobilization of enhanced green fluorescent protein (EGFP) as a model protein for the purpose of orientation-controlled surface density packing. In order to facilitate the oligomerization of EGFP, the dimeric and trimeric constructs derived from GCN4- leucine zipper domain were chosen for multimeric EGFP assembly. For orientation-controlled immobilization of the protein, EGFP modified with cysteine residues showing excellent orientation on a gold chip was used as a starting protein, as previously reported in our earlier study (<I>Anal. Chem.</I>, 2007, <B>79</B>, 2680–2687). Constructs of EGFP with oligomerization domains were genetically engineered, and corresponding fusion proteins were purified, applied to a gold chip, and then analyzed under SPR. The immobilized EGFP density on a gold chip increased according to the states of protein oligomerization, as dimeric and trimeric EGFPs displayed better adsorption capability than monomeric and dimeric forms, respectively. Fluorescence measurement corroborated the SPR results. Taken together, our findings indicated that the combination of cysteine- and oligomerization domain-mediated immobilization of protein could be used in SPR biosensor applications, allowing for an excellent orientation and high surface density simultaneously.</P> <P>Graphic Abstract</P><P>Here we report an effective method for protein immobilization on a SPR gold chip, describing the combination of cysteine- and oligomerization domain-mediated immobilization of EGFP as a model protein for the purpose of orientation-controlled surface density packing. <IMG SRC='http://pubs.rsc.org/services/images/RSCpubs.ePlatform.Service.FreeContent.ImageService.svc/ImageService/image/GA?id=c0an00966k'> </P>

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