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RISS 인기검색어
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- 저자 : ( Joo-ho Song ) (검색결과 1,551 건)
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Bae,,Gi-Sang,Kim,,Dong-Goo,Jo,,Il-Joo,Choi,,Sun-Bok,Kim,,Myoung-Jin,Shin,,Joon,Yeon,Kim,,Dong-Uk,Song,,Ho-Joon,Joo,,Myungsoo,Park,,Sung-Joo ELSEVIER 2019 INTERNATIONAL IMMUNOPHARMACOLOGY Vol.69 No.-
<P><B>Abstract</B></P> <P>Heme oxygenase-1 (HO-1) has an anti-inflammatory action in acute pancreatitis (AP). However, its mechanism of action and natural compounds/drugs to induce HO-1 in pancreas are not well understood. In this study, we investigated the regulatory mechanisms of HO-1 during AP using desoxo-narchinol-A (DN), the natural compound inducing HO-1 in the pancreas. Female C57/BL6 Mice were intraperitoneally injected with supramaximal concentrations of cerulein (50 μg/kg) hourly for 6 h to induce AP. DMSO or DN was administered intraperitoneally, then mice were sacrificed 6 h after the final cerulein injection. Administration of DN increased pancreatic HO-1 expression through activation of activating protein-1, mediated by mitogen-activated protein kinases. Furthermore, DN treatment reduced the pancreatic weight-to-body weight ratio as well as production of digestive enzymes and pro-inflammatory cytokines. Inhibition of HO-1 by tin protoporphyrin IX abolished the protective effects of DN on pancreatic damage. Additionally, DN treatment inhibited neutrophil infiltration into the pancreas via regulation of chemokine (C-X-C motif) ligand 2 (CXCL2) by HO-1. Our results suggest that DN is an effective inducer of HO-1 in the pancreas, and that HO-1 regulates neutrophil infiltration in AP via CXCL2 inhibition.</P> <P><B>Highlights</B></P> <P> <UL> <LI> Desoxo-narchinol-A (DN) is a natural compound of HO-1 inducer in pancreas. </LI> <LI> Mechanism of DN-induced HO-1 is mediated by MAPK/Activator Protein-1/HO-1 signaling. </LI> <LI> DN-induced HO-1 blocks neutrophil infiltration into pancreas via inhibition of CXCL2. </LI> <LI> DN inhibits cerulein-induced acute pancreatitis (AP) and AP-associated lung injury. </LI> </UL> </P> <P><B>Graphical abstract</B></P> <P>[DISPLAY OMISSION]</P>
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Shim,,Byoung-Shik,Choi,,Jung-ah,Song,,Ho-Hyun,Park,,Sung-Moo,Cheon,,In,Su,Jang,,Ji-Eun,Woo,,Sun,Je,Cho,,Chung,Hwan,Song,,Min-Suk,Kim,,Hyemi,Song,,Kyung,Joo,Lee,,Jae,Myun,Kim,,Suhng,Wook,Song,,Dae,Sub Springer-Verlag 2013 The journal of microbiology Vol.51 No.1
<P>Influenza viruses are respiratory pathogens that continue to pose a significantly high risk of morbidity and mortality of humans worldwide. Vaccination is one of the most effective strategies for minimizing damages by influenza outbreaks. In addition, rapid development and production of efficient vaccine with convenient administration is required in case of influenza pandemic. In this study, we generated recombinant influenza virus hemagglutinin protein 1 (sHA1) of 2009 pandemic influenza virus as a vaccine candidate using a well-established bacterial expression system and administered it into mice via sublingual (s.l.) route. We found that s.l. immunization with the recombinant sHA1 plus cholera toxin (CT) induced mucosal antibodies as well as systemic antibodies including neutralizing Abs and provided complete protection against infection with pandemic influenza virus A/CA/04/09 (H1N1) in mice. Indeed, the protection efficacy was comparable with that induced by intramuscular (i.m.) immunization route utilized as general administration route of influenza vaccine. These results suggest that s.l. vaccination with the recombinant non-glycosylated HA1 protein offers an alternative strategy to control influenza outbreaks including pandemics.</P>
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Song,,Woong-Kyu,Kang,,Joo-Hyun,Cha,,Jae-Kook,Lee,,Jung-Seok,Paik,,Jeong-Won,Jung,,Ui-Won,Kim,,Byung-Hoon,Choi,,Seong-Ho Korean Academy of Periodontology 2018 Journal of Periodontal & Implant Science Vol.48 No.5
Purpose: The aim of the present study was to evaluate the biocompatibility and barrier function of mussel adhesive protein (MAP)-loaded collagen membranes in guided bone regeneration (GBR). Methods: Eight male New Zealand white rabbits were used. Four circular defects (diameter: 8 mm) were created in the calvarium of each animal. The defects were randomly assigned to 1) a negative control group, 2) a cyanoacrylate (CA)-loaded collagen membrane group (the CA group), 3) a MAP-loaded collagen membrane group (the MAP group), and 4) a group that received a polycaprolactone block with MAP-loaded collagen membrane (the MAP-PCL group). Specimens were harvested at 2 weeks (n=4) and 8 weeks (n=4) postoperatively for observational histology and histometric analysis. Results: In the histologic analysis, MAP was completely absorbed without any byproducts. In contrast, some of the CA adhesive remained, showing an inflammatory reaction, at 8 weeks. In the MAP-PCL group, the MAP-loaded collagen membranes served as a barrier membrane despite their fast degradation in GBR. No significant difference was found in the amount of new bone between the MAP-PCL and MAP groups ($1.82{\pm}0.86mm^2$ and $2.60{\pm}0.65mm^2$, respectively). Conclusions: The MAP-loaded collagen membrane functioned efficiently in this rabbit calvarial GBR model, with excellent biocompatibility. Further research is needed to assess clinical applications in defect types that are more challenging for GBR than those used in the current model.
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Structure and interaction of ubiquitin-associated domain of human Fas-associated factor 1.
Song,,Jinsue,Park,,Joon,Kyu,Lee,,Jae-Jin,Choi,,Yun-Seok,Ryu,,Kyoung-Seok,Kim,,Jae-Hong,Kim,,Eunhee,Lee,,Kong-Joo,Jeon,,Young-Ho,Kim,,Eunice,Eunkyeong Cambridge University Press 2009 Protein science Vol.18 No.11
<P>Fas-associated factor (FAF)-1 is a multidomain protein that was first identified as a member of the Fas death-inducing signaling complex, but later found to be involved in various biological processes. Although the exact mechanisms are not clear, FAF1 seems to play an important role in cancer, asbestos-induced mesotheliomas, and Parkinson's disease. It interacts with polyubiquitinated proteins, Hsp70, and p97/VCP (valosin-containing protein), in addition to the proteins of the Fas-signaling pathway. We have determined the crystal structure of the ubiquitin-associated domain of human FAF1 (hFAF1-UBA) and examined its interaction with ubiquitin and ubiquitin-like proteins using nuclear magnetic resonance. hFAF1-UBA revealed a canonical three-helical bundle that selectively binds to mono- and di-ubiquitin (Lys48-linked), but not to SUMO-1 (small ubiquitin-related modifier 1) or NEDD8 (neural precursor cell expressed, developmentally down-regulated 8). The interaction between hFAF1-UBA and di-ubiquitin involves hydrophobic interaction accompanied by a transition in the di-ubiquitin conformation. These results provide structural insight into the mechanism of polyubiquitin recognition by hFAF1-UBA.</P>
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Joo,,Joungsu,Choi,,Hae,Jong,Lee,,Youn,Hab,Lee,,Sarah,Lee,,Choong,Hwan,Kim,,Chung,Ho,Cheong,,Jong-Joo,Choi,,Yang,Do,Song,,Sang,Ik Korean Society for Biochemistry and Molecular Biol 2014 BMB Reports Vol.47 No.1
Plant abiotic stress tolerance has been modulated by engineering the trehalose synthesis pathway. However, many stress-tolerant plants that have been genetically engineered for the trehalose synthesis pathway also show abnormal development. The metabolic intermediate trehalose 6-phosphate has the potential to cause aberrations in growth. To avoid growth inhibition by trehalose 6-phosphate, we used a gene that encodes a bifunctional in-frame fusion (BvMTSH) of maltooligosyltrehalose synthase (BvMTS) and maltooligosyltrehalose trehalohydrolase (BvMTH) from the nonpathogenic bacterium Brevibacterium helvolum. BvMTS converts maltooligosaccharides into maltooligosyltrehalose and BvMTH releases trehalose. Transgenic rice plants that over-express BvMTSH under the control of the constitutive rice cytochrome c promoter (101MTSH) or the ABA-inducible Ai promoter (105MTSH) show enhanced drought tolerance without growth inhibition. Moreover, 101MTSH and 105MTSH showed an ABA-hyposensitive phenotype in the roots. Our results suggest that over-expression of BvMTSH enhances drought-stress tolerance without any abnormal growth and showes ABA hyposensitive phenotype in the roots.
