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Anchoring foreign substances on live cell surfaces using Sortase A specific binding peptide
Park, Kyoungsook,Jung, Juyeon,Son, Jieun,Kim, So Hyun,Chung, Bong Hyun The Royal Society of Chemistry 2013 Chemical communications Vol.49 No.83
<P>A simple, rapid, and efficient live cell surface labeling method has been developed that uses a direct conjugation between Sortase A expressed transiently at the cell surface and Sortase A specific binding peptide.</P> <P>Graphic Abstract</P><P>A simple, rapid, and efficient live cell surface labeling method has been developed that uses a direct conjugation between Sortase A expressed transiently at the cell surface and Sortase A specific binding peptide. <IMG SRC='http://pubs.rsc.org/services/images/RSCpubs.ePlatform.Service.FreeContent.ImageService.svc/ImageService/image/GA?id=c3cc44753g'> </P>
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>
An ISFET biosensor for the monitoring of maltose-induced conformational changes in MBP
Park, Hye-Jung,Kim, Sang Kyu,Park, Kyoungsook,Lyu, Hong-Kun,Lee, Chang-Soo,Chung, Sang J.,Yun, Wan Soo,Kim, Moonil,Chung, Bong Hyun Elsevier 2009 FEBS letters Vol.583 No.1
<P><B>Abstract</B></P><P>Here we describe an ion sensitive field effect transistor (ISFET) biosensor, which was designed to monitor directly the surface charge of structurally altered maltose binding protein (MBP) upon stimulation with maltose. This study is the first report of the application of a FET biosensor to the monitoring of conformationally changed proteins. Consequently, a significant drop in current on the basis of the charge-dependent capacitance measurement has been clearly observed in response to maltose, but not for the glucose control, thereby indicating that the substrate-specific conformational properties of the target protein could be successfully monitored using the ISFET. Collectively, our results clearly suggest that ISFET provide a high fidelity system for the detection of maltose-induced structural alterations in MBP.</P>
Park, Joo-Young,Jeon, Ho-Jin,Kim, Tae Yun,Lee, Kyeong-Yeoll,Park, Kyoungsook,Lee, Eui Seok,Choi, Je-Min,Park, Chung-Gyu,Jeon, Soung-Hoo Future Medicine 2013 Regenerative medicine Vol.8 No.4
<P>Human dental mesenchymal stem cells (hDMSCs) have been isolated from extracted human teeth and proven to have different proliferation and differentiation abilities among the subtypes. Despite increasing interest in the clinical use of hDMSCs, a well-defined specific marker has been absent for these stem cells. In this study, a comparative analysis with known mesenchymal stem cell surface markers such as STRO-1, CD90, CD146, CD34 and TfR (CD71) was performed.</P>
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>
Live imaging of cellular dynamics using a multi-imaging vector in single cells
Park, Kyoungsook,Jeong, Jinyoung,Chung, Bong Hyun The Royal Society of Chemistry 2014 Chemical communications Vol.50 No.73
<P>Real-time monitoring of cellular dynamics in living organisms is highly challenging. We developed a multi-imaging vector based on 2A peptides. Live imaging of subcellular compartments can be performed following the transfection of cells with another vector, the multi-labeling vector, which contains localization signals and various fluorescent protein variants.</P> <P>Graphic Abstract</P><P>A multi-imaging vector system based on 2A peptides is developed for real-time monitoring of cellular dynamics. <IMG SRC='http://pubs.rsc.org/services/images/RSCpubs.ePlatform.Service.FreeContent.ImageService.svc/ImageService/image/GA?id=c4cc04980b'> </P>