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Species Specific Antiviral Activity of Porcine Interferon-α8 (IFNα8)
김은혜,전현정,김주희,박은주,조승현,곽아름,김시내,Tam T.Nguyen,강용선,최인수,이중복,김희준,김영현,이시영,김수현 대한면역학회 2017 Immune Network Vol.17 No.6
Interferons (IFNs) have been known as antiviral genes and they are classified by type 1, type 2, and type 3 IFN. The type 1 IFN consists of IFNα, IFNβ, IFNτ, and IFNω whereas the type 2 IFN consists of only IFNγ, which is a key cytokine driving T helper cell type 1 immunity. IFNλ belongs to the type 3 IFN, which is also known as IL-28 and IL-29 possessing antiviral activities. Type 1 IFN is produced by viral infection whereas type 2 IFN is induced by mitogenic or antigenic T-cell stimuli. The IFNτ of bovine was first discovered in an ungulate ruminant recognition hormone. IFNτ belongs to the type 1 IFN with the common feature of type 1 IFN such as antiviral activity. IFNs have been mostly studied for basic research and clinical usages therefore there was no effort to investigate IFNs in industrial animals. Here we cloned porcine IFNα8 from peripheral blood mononuclear cells of Korean domestic pig (Sus scrofa domestica). The newly cloned IFNα8 amino acid sequence from Korean domestic pig shares 98.4% identity with the known porcine IFNα8 in databank. The recombinant porcine IFNα8 showed potent antiviral activity and protected bovine Madin-Darby bovine kidney epithelial (MDBK) cells from the cytopathic effect of vesicular stomatitis virus, but it failed to protect human Wistar Institute Susan Hayflick (WISH) cells and canine Madin-Darby canine kidney epithelial-like (MDCK) cells. The present study demonstrates species specific antiviral activity of porcine IFNα8.
Species Specific Antiviral Activity of Porcine Interferon-α8 (IFNα8)
Kim, Eunhye,Jhun, Hyunjhung,Kim, Joohee,Park, Unjoo,Jo, Seunghyun,Kwak, Areum,Kim, Sinae,Nguyen, Tam T.,Kang, Yongsun,Choi, Insoo,Lee, Joongbok,Kim, Heijun,Kim, Younghyun,Lee, Siyoung,Kim, Soohyun 한국조명·전기설비학회 2017 한국조명·전기설비학회 학술대회논문집 Vol. No.
<P>Interferons (IFNs) have been known as antiviral genes and they are classified by type 1, type 2, and type 3 IFN. The type 1 IFN consists of IFNα, IFNβ, IFNτ, and IFNω whereas the type 2 IFN consists of only IFNγ, which is a key cytokine driving T helper cell type 1 immunity. IFNλ belongs to the type 3 IFN, which is also known as IL-28 and IL-29 possessing antiviral activities. Type 1 IFN is produced by viral infection whereas type 2 IFN is induced by mitogenic or antigenic T-cell stimuli. The IFNτ of bovine was first discovered in an ungulate ruminant recognition hormone. IFNτ belongs to the type 1 IFN with the common feature of type 1 IFN such as antiviral activity. IFNs have been mostly studied for basic research and clinical usages therefore there was no effort to investigate IFNs in industrial animals. Here we cloned porcine IFNα8 from peripheral blood mononuclear cells of Korean domestic pig (<I>Sus scrofa domestica</I>). The newly cloned IFNα8 amino acid sequence from Korean domestic pig shares 98.4% identity with the known porcine IFNα8 in databank. The recombinant porcine IFNα8 showed potent antiviral activity and protected bovine Madin-Darby bovine kidney epithelial (MDBK) cells from the cytopathic effect of vesicular stomatitis virus, but it failed to protect human Wistar Institute Susan Hayflick (WISH) cells and canine Madin-Darby canine kidney epithelial-like (MDCK) cells. The present study demonstrates species specific antiviral activity of porcine IFNα8.</P>
Nguyen, Quang-Tam,Nguyen, Thu-Ha T.,Ju, Seong-A.,Lee, Yea-Sol,Han, Seung Hyun,Lee, Sang-Chul,Kwon, Byoung S.,Yu, Rina,Kim, Gyu Yeol,Lee, Byung Ju,Kim, Byung-Sam American Society for Microbiology 2013 Infection and immunity Vol.81 No.6
<P>Severe sepsis and septic shock caused mainly by bacterial infections are life-threatening conditions that urge the development of novel therapies. However, host responses to and pathophysiology of sepsis have not been clearly understood, which remains a major obstacle for the development of effective therapeutics. Recently, we have shown that stimulation of a costimulatory molecule, CD137, enhanced survival of mice infected with the Gram-positive (G<SUP>+</SUP>) intracellular bacterium <I>Listeria monocytogenes</I> but decreased survival in a polymicrobial sepsis model. Herein, we report that CD137 deficiency or blocking of CD137 signaling decreased antibacterial responses of mice infected with G<SUP>+</SUP> bacteria (<I>Staphylococcus aureus</I>, <I>Streptococcus pneumoniae</I>, and <I>Enterococcus faecalis</I>) but increased these responses in mice infected with Gram-negative (G<SUP>−</SUP>) bacteria (<I>Escherichia coli</I>, <I>Pseudomonas aeruginosa</I>, and <I>Salmonella enterica</I> serovar Typhimurium). Consistent with these findings, stimulation of CD137 by administration of agonistic antibody enhanced responses against G<SUP>+</SUP> bacteria, whereas it decreased these responses against G<SUP>−</SUP> bacteria. Neutrophils were responsible for CD137-mediated opposite roles in control of G<SUP>+</SUP> and G<SUP>−</SUP> bacterial infections. Stimulation of CD137 enhanced activities of neutrophils against <I>S. aureus</I> but decreased these activities against <I>E. coli</I>, while CD137 blocking produced opposite results with the stimulation of CD137 <I>in vivo</I> and <I>in vitro</I>. Furthermore, we found that combined signaling of CD137 and Toll-like receptor 2 (TLR2) induced synergistic production of tumor necrosis factor alpha (TNF-α) and interleukin-6 (IL-6) by neutrophils, but combined signaling of CD137 and TLR4 did not. Our data strongly suggest that CD137 may play a dual role in sepsis in association with TLRs.</P>
Hoan Minh Tran,Tam Huu Nguyen,Viet Quoc Nguyen,Phuc Huynh Tran,Linh Duy Thai,Thuy Thu Truong,Le-Thu T. Nguyen,Ha Tran Nguyen 한국고분자학회 2019 Macromolecular Research Vol.27 No.1
The photoswitching poly(pyrene-1-ylmethyl-methacrylate-random-methyl methacrylate-random-methacrylate spirooxazine) was synthesized via atom transfer radical polymerization and characterized by proton nuclear magnetic resonance (1H NMR), gel permeation chromatography (GPC), Fourier transform infrared (FTIR) spectroscopy, UV-visible spectroscopy, and differential scanning calorimetry (DSC). The obtained copolymer exhibited the capability of erasable and rewritable photoimaging, making it a potential candidate for optical data storage materials. Moreover, the copolymer also showed the sensing ability for cyanide anions effect in aqueous solutions.
Nhung Thanh Thi Truong,Tam Huu Nguyen,Bao Kim Doan,Le-Thu T. Nguyen,Tam Hoang Luu,Chau Duc Tran,Thiet Quoc Nguyen,Ha Tran Nguyen 한국고분자학회 2021 Macromolecular Research Vol.29 No.11
In this research, three organic photocatalysts, 4-(4H-dithieno[3,2-b:2',3'- d]pyrrol-4-yl)-N,N-diphenylaniline, 4-(pyren-1-yl)-4H-dithieno[3,2-b:2',3'-d]pyrrole and 4-(6b,10-dihydroperylen-3-yl)-4H-dithieno[3,2-b:2',3'-d]pyrrole have been successfully synthesized through C-N coupling reactions. The chemical structures and the optical properties of the obtained organic photocatalysts have been characterized via 1H NMR,13C NMR, elemental analysis, and UV-Vis spectroscopy. Next, these dithieno[3,2-b:2′,3′-d]pyrrole-based photocatalysts have been used for the polymerization of methyl methacrylate, 2-(dimethylamino)ethyl methacrylate and tert-butyl methacrylate monomers under 365 nm UV irradiation, resulting in (meth)acrylate polymers with controlled molecular weights and low polydispersity indexes.
Structural Characteristics of Seven IL-32 Variants
손동현,Tam T.Nguyen,김시내,심새록,이시영,이영민,전현정,Tania Azam,김주희,김수현 대한면역학회 2019 Immune Network Vol.19 No.2
IL-32 exists as seven mRNA transcripts that can translate into distinct individual IL-32 variants with specific protein domains. These translated protein domains of IL-32 variants code for specific functions that allow for interaction with different molecules intracellularly or extracellularly. The longest variant is IL-32γ possessing 234 amino acid residues with all 11 protein domains, while the shortest variant is IL-32α possessing 131 amino acid residues with three of the protein domains. The first domain exists in 6 variants except IL-32δ variant, which has a distinct translation initiation codon due to mRNA splicing. The last eleventh domain is common domain for all seven IL-32 variants. Numerous studies in different fields, such as inflammation, autoimmunity, pathogen infection, and cancer biology, have claimed the specific biological activity of individual IL-32 variant despite the absence of sufficient data. There are 4 additional IL-32 variants without proper transcripts. In this review, the structural characteristics of seven IL-32 transcripts are described based on the specific protein domains.
Kim Sinae,Nguyen Tam T.,Taitt Afeisha S.,전현정,Park Ho-Young,Kim Sung-Han,Kim Yong-Gil,Song Eun Young,Lee Youngmin,Yum Hokee,Shin Kyeong-Cheol,Choi Yang Kyu,송창선,Yeom Su Cheong,Kim Byoungguk,Netea Mihai 대한면역학회 2021 Immune Network Vol.21 No.6
Recently, a new severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) (B.1.1.529) Omicron variant originated from South Africa in the middle of November 2021. SARS-CoV-2 is also called coronavirus disease 2019 (COVID-19) since SARS-CoV-2 is the causative agent of COVID-19. Several studies already suggested that the SARS-CoV-2 Omicron variant would be the fastest transmissible variant compared to the previous 10 SARS-CoV-2 variants of concern, interest, and alert. Few clinical studies reported the high transmissibility of the Omicron variant but there is insufficient time to perform actual experiments to prove it, since the spread is so fast. We analyzed the SARS-CoV-2 Omicron variant, which revealed a very high rate of mutation at amino acid residues that interact with angiostatin-converting enzyme 2. The mutation rate of COVID-19 is faster than what we prepared vaccine program, antibody therapy, lockdown, and quarantine against COVID-19 so far. Thus, it is necessary to find better strategies to overcome the current crisis of COVID-19 pandemic.
Kim, Miyong T.,Kim, Kim Byeng,Nguyen, Tam H.,Ko, Jisook,Zabora, Jim,Jacobs, Elizabeth,Levine, David Elsevier 2019 Patient education and counseling Vol.102 No.4
<P><B>Abstract</B></P> <P><B>Objective</B></P> <P>To test the efficacy of a hybrid model of the self-help intervention program (hSHIP), which combines a mobile version of SHIP (mSHIP) and personal coaching, to address unique cultural and motivational factors for optimal self-management of type 2 diabetes and prediabetes among Korean Americans (KAs).</P> <P><B>Methods</B></P> <P>A single-group feasibility study design was used. The hSHIP utilizes texts and motivational counseling based on well-tested intervention content for KAs. To facilitate the dissemination of hSHIP, we developed a web application adopting the principles of persuasive technology to motivate behavior changes.</P> <P><B>Results</B></P> <P>Feasibility assessment found that hSHIP was well accepted by both participants and community health workers who delivered the intervention. An average of 1.3% A1C reduction (from 7.8% to 6.5%) was achieved by KAs with diabetes (n = 165), 51.5% of whom lowered their A1C below 6.5% in 6-months. No one with prediabetes (n = 50) progressed to diabetes. Other clinical outcomes (e.g., weight, depression, and blood pressure) also improved significantly; 41.2% were able to reduce or discontinue antidiabetic drugs.</P> <P><B>Conclusion</B></P> <P>The feasibility and initial efficacy of hSHIP were demonstrated.</P> <P><B>Practice implication</B></P> <P>This hybrid diabetes self-management model is a viable tool for traditionally underserved groups with diabetes or prediabetes.</P> <P><B>Highlights</B></P> <P> <UL> <LI> We tested feasibility of a hybrid diabetes care model in an ethnic minority group. </LI> <LI> Our model combined a digital touch of mHealth and a human touch of CHWs. </LI> <LI> About a half (51.5%) lowered their hemoglobin A1C below 6.5% in 6 months. </LI> <LI> Many (41.2%) stopped/reduced antidiabetic drugs but still managed their diabetes. </LI> <LI> Weight, depression and blood pressure were also significantly improved. </LI> </UL> </P>
김현우,길가애,이시영,곽아름,조승현,김은솜,Tam T.Nguyen,김시내,전현정,김소미,김미연,이영민,김수현 대한면역학회 2016 Immune Network Vol.16 No.5
It has been reported that fatty acid binding proteins (FABPs) do not act only as intracellular mediators of lipid responses but also have extracellular functions. This study aimed to investigate whether extracellular liver type (L)- FABP has a biological activity and to determined serum L-FABP levels in patients with end-stage renal disease (ESRD). We isolated L-FABP complementary deoxyribonucleic acid (cDNA) from the Huh7 human hepatocarcinoma cell line and expressed the recombinant L-FABP protein in Escherichia coli. A549 lung carcinoma and THP-1 monocytic cells were stimulated with the human recombinant L-FABP. Human whole blood cells were also treated with the human recombinant L-FABP or interleukin (IL)-1a. IL-6 levels were measured in cell culture supernatants using IL-6 enzyme-linked immunosorbent assay (ELISA). Human recombinant L-FABP induced IL-6 in a dose-dependent manner in A549, THP-1 cells, and whole blood cells. The blood samples of healthy volunteers and patients with ESRD were taken after an overnight fast. The serum levels of L-FABP in healthy volunteers and ESRD patients were quantified with L-FABP ELISA. The values of L-FABP in patients with ESRD were significantly lower than those in the control group. Our results demonstrated the biological activity of L-FABP in human cells suggesting L-FABP can be a mediator of inflammation.