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Kim, J.Y.,Kim, K.B.,Son, H.J.,Chae, Y.C.,Oh, S.T.,Kim, D.W.,Pak, J.H.,Seo, S.B. North-Holland Pub ; Elsevier Science Ltd 2012 FEBS letters Vol.586 No.19
Significant progress has been made in understanding the relationship between histone modifications and 'reader' molecules and their effects on transcriptional regulation. A previously identified INHAT complex subunit, SET/TAF-Iβ, binds to histones and inhibits histone acetylation. To investigate the binding specificities of SET/TAF-Iβ to various histone modifications, we employed modified histone tail peptide array analyses. SET/TAF-Iβ strongly recognized PRC2-mediated H3K27me½/3; however, the bindings were completely disrupted by H3S28 phosphorylation. We have demonstrated that SET/TAF-Iβ is sequentially recruited to the target gene promoter ATF3 after the PRC2 complex via H3K27me recognition and may offer additive effects in the repression of the target gene.
Oh, N.S.,Kwon, H.S.,Lee, H.A.,Joung, J.Y.,Lee, J.Y.,Lee, K.B.,Shin, Y.K.,Baick, S.C.,Park, M.R.,Kim, Y.,Lee, K.W.,Kim, S.H. American Dairy Science Association 2014 Journal of dairy science Vol.97 No.6
The aim of this study was to determine the dual effect of Maillard reaction and fermentation on the preventive cardiovascular effects of milk proteins. Maillard reaction products (MRP) were prepared from the reaction between milk proteins, such as whey protein concentrates (WPC) and sodium caseinate (SC), and lactose. The hydrolysates of MRP were obtained from fermentation by lactic acid bacteria (LAB; i.e., Lactobacillus gasseri H10, L. gasseri H11, Lactobacillus fermentum H4, and L. fermentum H9, where human-isolated strains were designated H1 to H15), which had excellent proteolytic and 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical scavenging activities (>20%). The antioxidant activity of MRP was greater than that of intact proteins in assays of the reaction with 2,2'-azino-bis (3-ethylbenzothiazoline-6-sulfonic acid) diammonium salt and trivalent ferric ions; moreover, the effect of MRP was synergistically improved by fermentation. The Maillard reaction dramatically increased the level of antithrombotic activity and 3-hydroxy-3-methylglutaryl-CoA reductase (HMGR) inhibitory effect of milk proteins, but did not change the level of activity for micellar cholesterol solubility. Furthermore, specific biological properties were enhanced by fermentation. Lactobacillus gasseri H11 demonstrated the greatest activity for thrombin and HMGR inhibition in Maillard-reacted WPC, by 42 and 33%, respectively, whereas hydrolysates of Maillard-reacted SC fermented by L. fermentum H9 demonstrated the highest reduction rate for micellar cholesterol solubility, at 52%. In addition, the small compounds that were likely released by fermentation of MRP were identified by size-exclusion chromatography. Therefore, MRP and hydrolysates of fermented MRP could be used to reduce cardiovascular risks.
대장 선종과 암의 동시성 병변에서 K-ras 유전자의 돌연변이 및 k-Ras, p16, Cyclin D1과 p53 단백질의 발현
오용열 ( Y. L. Oh ),전훈재 ( H. J. Chun ),박동규 ( D. K. Park ),박재홍 ( J. H. Park ),박철희 ( C. H. Park ),진윤태 ( Y. T. Jeen ),이홍식 ( H. S. Lee ),이상우 ( S. W. Lee ),엄순호 ( S. H. Um ),최재현 ( J. H. Choi ),김창덕 ( C. D. Kim 대한소화기학회 2002 대한소화기학회 춘계학술대회 Vol.2002 No.-
<Background> The colorectal adenoma-carcinoma sequence represents a well-known paradigm for the sequential development of cancer driven by the accumulation of genomic defects, Although the colorectal adenoma-carcinoma sequence is well established, the stu
Antiviral phenolics from the leaves of Cleistocalyx operculatus
Ha, T.K.Q.,Dao, T.T.,Nguyen, N.H.,Kim, J.,Kim, E.,Cho, T.Oh.,Oh, W.K. Elsevier 2016 Fitoterapia Vol.110 No.-
<P>During the screening program for anti-influenza agents from medicinal plants, the ethanolic extract of Cleistocalyx operculatus leaves was found to exhibit potential neuraminidase (NA) inhibitory activity. Bioassay directed fractionation led to the isolation of two new acetophenones (1 and 2) and one new flavanone (3), along with six known compounds (4-9). The structures of all isolated compounds were elucidated using various spectroscopic methods and through comparison with the previous literature. Compounds 6 and 8 exhibited strong enzymatic inhibition on various neuraminidases from different influenza viruses, including H1N1, H9N2, novel H1N1, and oseltamivir-resistant novel H1N1 (H274Y mutation) expressed in HEM293 cells (IC50 values ranging from 5.07 +/- 0.94 mu M to 9.34 +/- 2.52 mu M, respectively). Kinetic experiments revealed the non-competitive inhibitory mode of both compounds 6 and 8. Furthermore, these flavonoids reduced the cytopathic effect of the H1N1 virus in MDCK cells. The present study suggests the potential of two flavonoids (6 and 8) as new lead compounds for the development of novel NA inhibitors in the future. (C) 2016 Elsevier B.V. All rights reserved.</P>
Pi, S.-H.,Jeong, G.-S.,Oh, H.-W.,Kim, Y.-S.,Pae, H.-O.,Chung, H.-T.,Lee, S.-K.,Kim, E.-C. Blackwell Publishing Ltd 2010 Journal of periodontal research Vol.45 No.2
<P><I>Pi S-H, Jeong G-S, Oh H-W, Kim Y-S, Pae H-O, Chung H-T, Lee S-K, Kim E-C. Heme oxygenase-1 mediates nicotine- and lipopolysaccharide-induced expression of cyclooxygenase-2 and inducible nitric oxide synthase in human periodontal ligament cells. J Periodont Res 2010; 45: 177–183. © 2010 John Wiley & Sons A/S</I></P><P>Background and Objective: </P><P>Although heme oxygenase-1 (HO-1) plays a key role in inflammation, its anti-inflammatory effects and mechanism of action in periodontitis are still unknown. This study aimed to identify the effects of HO-1 on the proinflammatory mediators activated by nicotine and lipopolysaccharide (LPS) stimulation in human periodontal ligament (PDL) cells.</P><P>Material and Methods: </P><P>The production of nitric oxide (NO) and prostaglandin E<SUB>2</SUB> (PGE<SUB>2</SUB>) was evaluated using Griess reagent and an enzyme immunoassay, respectively. The expression of inducible nitric oxide synthase (iNOS), cyclooxygenase-2 (COX-2) and HO-1 proteins was evaluated by Western blot analysis.</P><P>Results: </P><P>Lipopolysaccharide and nicotine synergistically induced the production of NO and PGE<SUB>2</SUB> and increased the protein expression of iNOS, COX-2 and HO-1. Treatment with an HO-1 inhibitor and HO-1 small interfering RNAs blocked the LPS- and nicotine-stimulated NO and PGE<SUB>2</SUB> release as well as the expression of iNOS and COX-2.</P><P>Conclusion: </P><P>Our data suggest that the nicotine- and LPS-induced inflammatory effects on PDL cells may act through a novel mechanism involving the action of HO-1. Thus, HO-1 may provide a potential therapeutic target for the treatment of periodontal disease associated with smoking and dental plaque.</P>
In vivo imaging of tumor apoptosis using histone H1-targeting peptide
Wang, K.,Purushotham, S.,Lee, J.Y.,Na, M.H.,Park, H.,Oh, S.J.,Park, R.W.,Park, J.Y.,Lee, E.,Cho, B.C.,Song, M.N.,Baek, M.C.,Kwak, W.,Yoo, J.,Hoffman, A.S.,Oh, Y.K.,Kim, I.S.,Lee, B.H. Elsevier Science Publishers 2010 Journal of controlled release Vol.148 No.3
In vivo imaging of apoptosis could allow monitoring of tumor response to cancer treatments such as chemotherapy. Using phage display, we identified the CQRPPR peptide, named ApoPep-1(Apoptosis-targeting Peptide-1), that was able to home to apoptotic and necrotic cells in tumor tissue. ApoPep-1 also bound to apoptotic and necrotic cells in culture, while only little binding to live cells was observed. Its binding to apoptotic cells was not dependent on calcium ion and not competed by annexin V. The receptor for ApoPep-1 was identified to be histone H1 that was exposed on the surface of apoptotic cells. In necrotic cells, ApoPep-1 entered the cells and bound to histone H1 in the nucleus. The imaging signals produced during monitoring of tumor apoptosis in response to chemotherapy was enhanced by the homing of a fluorescent dye- or radioisotope-labeled ApoPep-1 to tumor treated with anti-cancer drugs, whereas its uptake of the liver and lung was minimal. These results suggest that ApoPep-1 holds great promise as a probe for in vivo imaging of apoptosis, while histone H1 is a unique molecular signature for this purpose.