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Su, Xiang Dong,Ali, Irshad,Arooj, Madeeha,Koh, Young Sang,Yang, Seo Young,Kim, Young Ho The Pharmaceutical Society of Korea 2018 Archives of Pharmacal Research Vol.41 No.5
Sanguisorba officinalis L. (Rosaceae) is a perennial herbaceous plant and its roots have been used as an important astringent medicine in Eastern Asian countries over many thousand years. In this phytochemical research, 23 compounds (1-23) were isolated from the roots of S. officinalis. Their chemical structures were identified by extensive spectroscopic methods, including 1D and 2D NMR experiments. The anti-inflammatory effects of extracts and isolated compounds were investigated by measuring the production of pro-inflammatory cytokine IL-12 p40, IL-6 and <TEX>$TNF-{\alpha}$</TEX> in LPS-stimulated bone marrow-derived dendritic cell. Compounds 1, 3, 7-8, 11-14 revealed promising anti-inflammatory effects. These results suggested that some phenolic compounds and monoterpenoids from S. officinalis could be potential candidates for anti-inflammatory treatments.
Xiang-Dong Su,Seo Y Yang,Saroj K Shrestha,Yunjo Soh 대한수의학회 2022 Journal of Veterinary Science Vol.23 No.4
Background: In lipopolysaccharide-induced RAW264.7 cells, Aster tataricus (AT) inhibits the nuclear factor kappa-light-chain-enhancer of activated B cells and MAPKs pathways and critical pathways of osteoclast development and bone resorption. Objectives: This study examined how aster saponin A2 (AS-A2) isolated from AT affects the processes and function of osteoclastogenesis induced by receptor activator of nuclear factor kappa-B ligand (RANKL) in RAW264.7 cells and bone marrow macrophages (BMMs). Methods: The cell viability, tartrate-resistant acid phosphatase staining, pit formation assay, polymerase chain reaction, and western blot were carried out to determine the effects of AS-A2 on osteoclastogenesis. Results: In RAW264.7 and BMMs, AS-A2 decreased RANKL-initiated osteoclast differentiation in a concentration-dependent manner. In AS-A2-treated cells, the phosphorylation of ERK1/2, JNK, and p38 protein expression were reduced considerably compared to the control cells. In RAW264.7 cells, AS-A2 suppressed the RANKL-induced activation of osteoclast-related genes. During osteoclast differentiation, AS-A2 suppressed the transcriptional and translational expression of NFATc1 and c-Fos. AS-A2 inhibited osteoclast development, reducing the size of the bone resorption pit area. Conclusion: AS-A2 isolated from AT appears to be a viable therapeutic therapy for osteolytic illnesses, such as osteoporosis, Paget’s disease, and osteogenesis imperfecta.
A New Time Stepping Method for Solving One Dimensional Burgers' Equations
Piao, Xiang Fan,Kim, Sang-Dong,Kim, Phil-Su,Kim, Do-Hyung Department of Mathematics 2012 Kyungpook mathematical journal Vol.52 No.3
In this paper, we present a simple explicit type numerical method for discretizations in time for solving one dimensional Burgers' equations. The proposed method does not need an iteration process that may be required in most implicit methods and have good convergence and efficiency in computational sense compared to other known numerical methods. For evidences, several numerical demonstrations are also provided.
Quinolone Alkaloids from Evodiae Fructus and Their Inhibitory Effects on Monoamine Oxidase
Han, Xiang-Hua,Hong, Seong-Su,Lee, Dong-Ho,Lee, Jung-Joon,Lee, Moon-Soon,Moon, Dong-Cheul,Han, Kun,Oh, Ki-Wan,Lee, Myung-Koo,Ro, Jai-Seup,Hwang, Bang-Yeon 대한약학회 2007 Archives of Pharmacal Research Vol.30 No.4
1-Methyl-2-undecyl-4(1H)-quinolone (1) was previously isolated as a selective MAO-B inhibitor from the Evodiae Fructus. Further bioassay-guided purification led to the identification of five known quinolone alkaloids, 1 -methyl-2-nonyl-4(1H)-quinolone (2), 1-methyl-2-[(Z)-6-unde-cenyl]-4(1 H)-quinolone (3), evocarpine (4), 1-methyl-2-[(6Z,9Z)-6,9-pentadecadienyl]-4(1H)-quinolone (5), and dihydroevocarpine (6). All the isolates showed more potent inhibitory effects against MAO-B compared to MAO-A. The most MAO-B selective compound 5 among the isolates inhibited MAO-B in a competitive manner, according to kinetic analyses by Lineweaver-Burk reciprocal plots.
Lee, Dong-Sung,Cui, Xiang,Ko, Wonmin,Kim, Kyoung-Su,Kim, Il Chan,Yim, Joung Han,An, Ren-Bo,Kim, Youn-Chul,Oh, Hyuncheol 대한약학회 2014 Archives of Pharmacal Research Vol.37 No.8
In this study, we isolated a new sulfonic acid derivative, (Z)-4-methylundeca-1,9-diene-6-sulfonic acid (1), from the sea urchin collected from the Sea of Okhotsk. We established the structure of this new compound by analysis of NMR and HRMS data, along with comparison of the data with those of the related compounds reported in the literature. In addition, we investigated its anti-inflammatory effects in LPS-stimulated RAW264.7 macrophages. Compound 1 inhibited the production of NO, iNOS, $PGE_2$, and COX-2, and it also suppressed the production of proinflammatory cytokines, such as $TNF-{\alpha}$ and $IL-1{\beta}$. It inhibited the translocation of the $NF-{\kappa}B$ subunit p65 into the nucleus by interrupting the phosphorylation and degradation of $I{\kappa}B-{\alpha}$. In addition, compound 1 significantly decreased the phosphorylation of JNK and p38 in LPS-stimulated RAW264.7 macrophages, suggesting that suppression of the inflammation process by compound 1 was mediated through the MAPK pathway. Taken together, this study showed that the anti-inflammatory effects of a new sulfonic acid derivative, (Z)-4-methylundeca-1,9-diene-6-sulfonic acid were mediated through the inhibition of $NF-{\kappa}B$ and JNK/p38 MAPK signaling pathways.
N-terminal arginylation generates a bimodal degron that modulates autophagic proteolysis
Yoo, Young Dong,Mun, Su Ran,Ji, Chang Hoon,Sung, Ki Woon,Kang, Keum Young,Heo, Ah Jung,Lee, Su Hyun,An, Jee Young,Hwang, Joonsung,Xie, Xiang-Qun,Ciechanover, Aaron,Kim, Bo Yeon,Kwon, Yong Tae National Academy of Sciences 2018 PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF Vol.115 No.12
<P>The conjugation of amino acids to the protein N termini is universally observed in eukaryotes and prokaryotes, yet its functions remain poorly understood. In eukaryotes, the amino acid L-arginine (L-Arg) is conjugated to N-terminal Asp (Nt-Asp), Glu, Gln, Asn, and Cys, directly or associated with posttranslational modifications. Following Ntarginylation, the Nt-Arg is recognized by UBR boxes of N-recognins such as UBR1, UBR2, UBR4/p600, and UBR5/EDD, leading to substrate ubiquitination and proteasomal degradation via the N-end rule pathway. It has been a mystery, however, why studies for the past five decades identified only a handful of Nt-arginylated substrates in mammals, although five of 20 principal amino acids are eligible for arginylation. Here, we show that the Nt-Arg functions as a bimodal degron that directs substrates to either the ubiquitin (Ub)proteasome system (UPS) or macroautophagy depending on physiological states. In normal conditions, the arginylated forms of proteolytic cleavage products, D101-CDC6 and D1156-BRCA1, are targeted to UBR box-containing N-recognins and degraded by the proteasome. However, when proteostasis by the UPS is perturbed, their Nt-Arg redirects these otherwise cellularwastes tomacroautophagy through its binding to the ZZ domain of the autophagic adaptor p62/STQSM/Sequestosome-1. Upon binding to the Nt-Arg, p62 acts as an autophagic N-recognin that undergoes self-polymerization, facilitating cargo collection and lysosomal degradation of p62-cargo complexes. A chemical mimic of Nt-Arg redirects Ub-conjugated substrates from the UPS to macroautophagy and promotes their lysosomal degradation. Our results suggest that the Nt-Arg proteome of arginylated proteins contributes to reprogramming global proteolytic flux under stresses.</P>
A facile macroporous resin-based method for separation of yellow and orange Monascus pigments
Suo Chen,Dong-Xiao Su,Meng-Xiang Gao,Jia-Lan Zhang,Ying-Bao Liu,Qing-Hua Wu,Hua-Lin Yang,Li Li 한국식품과학회 2021 Food Science and Biotechnology Vol.30 No.4
The yellow Monascus pigments (YMPs) namedmonascin and ankaflavin and the orange Monascus pigments(OMPs) named rubropunctatin and monascorubrinare two groups of bioactive components in a mixture statein the Monascus fermented products. In order to separatethese two groups of bioactive pigments, a facile macroporousresin-based method was developed. The weak-polarresin CAD-40 was selected from the seven tested macroporousresins as it revealed better properties for theadsorption and desorption of the YMPs and OMPs. Then,CAD-40 resin was used for column-chromatographicseparation. After eluted by 4 bed volumes of ethanol, theyellow group (monascin and ankaflavin) and the orangegroup (rubropunctatin and monascorubrin) were successfullyseparated and purified, with an increased content from49.3% and 44.2% in the crude pigment extract to 85.2%and 83.0% in the final products, respectively. This methodwould be helpful for the large-scale separation and purificationof Monascus pigment products with specificbioactivity.
Park, Gyeong-Su,Kwon, Hyuksang,Kwak, Dong Wook,Park, Seong Yong,Kim, Minseok,Lee, Jun-Ho,Han, Hyouksoo,Heo, Sung,Li, Xiang Shu,Lee, Jae Hak,Kim, Young Hwan,Lee, Jeong-Gun,Yang, Woochul,Cho, Hoon Young American ChemicalSociety 2012 Nano letters Vol.12 No.3
<P>We report on rapid thermal chemical vapor depositiongrowth of silicon nanowires (Si NWs) that contain a high density ofgold nanoclusters (Au NCs) with a uniform coverage over the entirelength of the nanowire sidewalls. The Au NC-coated Si NWs with anantibody-coated surface obtain the unique capability to capture breastcancer cells at twice the highest efficiency currently achievable(∼88% at 40 min cell incubation time) from a nanostructuredsubstrate. We also found that irradiation of breast cancer cells capturedon Au NC-coated Si NWs with a near-infrared light resulted in a highmortality rate of these cancer cells, raising a fine prospect forsimultaneous capture and plasmonic photothermal therapy for circulatingtumor cells.</P><P><B>Graphic Abstract</B> <IMG SRC='http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/nalefd/2012/nalefd.2012.12.issue-3/nl2045759/production/images/medium/nl-2011-045759_0006.gif'></P><P><A href='http://pubs.acs.org/doi/suppl/10.1021/nl2045759'>ACS Electronic Supporting Info</A></P>