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Discrete-Time Sliding Mode Controller for Linear Time-Varying Systems with Disturbances
Park, Kang-Bak Institute of Control 2000 Transaction on control, automation and systems eng Vol.2 No.4
In this paper, a discrete-time sliding mode controller for linear time-varying systems with disturbances is proposed. The proposed method guarantees the systems state is globally uniformly ultimately bounded(G.U.U.B) under the existence of time-varying disturbances.
BAK, Geon-Yong,KANG, Mun-Il,SON, Kyu-Yeol,PARK, Jun-Gyu,KIM, Deok-Song,SEO, Ja-Young,KIM, Ji-Yun,ALFAJARO, Mia Madel,SOLIMAN, Mahmoud,BAEK, Yeong-Bin,CHO, Eun-Hyo,KWON, Joseph,CHOI, Jong-Soon,PARK, Sa The Japanese Society of Veterinary Science 2016 The Journal of veterinary medical science Vol.78 No.12
<P>To determine the occurrence and genetic diversity of <I>Sapelovirus A</I> (SV-A) in diarrhea and non-diarrhea feces of Korean pigs, 110 specimens from different age groups of pigs in the same farm were analyzed by RT-nested PCR. SV-As were detected in 60% of both diarrhea and non-diarrhea specimens regardless of age groups with primer pairs for 2C region, in which all diarrhea samples were co-infected by other enteric pathogens. Phylogenetical analysis of partial VP1 region showed that our strains and several other Korean strains belonged to cluster I, distinct from some strains reported in Korea and other countries. These data indicate that genetically distinct SV-As are frequently detected in Korean pigs irrespective of diarrhea and age.</P>
Interleukin-32δ interacts with IL-32β and inhibits IL-32β-mediated IL-10 production
Kang, J.W.,Park, Y.S.,Lee, D.H.,Kim, M.S.,Bak, Y.,Park, S.H.,Ham, S.Y.,Yang, Y.,Hong, J.T.,Yoon, D.Y. North-Holland Pub ; Elsevier Science Ltd 2013 FEBS letters Vol.587 No.23
There is growing evidence for multifunctional properties of IL-32. We previously demonstrated that IL-32β upregulates IL-10 production through the association with PKCδ. In this study, we examined the effects of other IL-32 isoforms on IL-10 production. We found that IL-32δ decreased IL-10 production and investigated the inhibitory mechanism of IL-32δ. We showed that IL-32δ suppressed IL-32β binding to PKCδ by interacting with IL-32β. The inhibitory effect of IL-32δ on IL-32β association with PKCδ was further verified by immuno-fluorescence staining. The co-localization of IL-32β and PKCδ around the nuclear membrane was disrupted by IL-32δ. Our data therefore indicate that IL-32δ plays an inhibitory role against IL-32β function, which also suggests that IL-32 may be regulated by its own isoform.
Kang, Jeong-Woo,Park, Yun Sun,Lee, Dong Hun,Kim, Jung-hee,Kim, Man Sub,Bak, Yesol,Hong, Jintae,Yoon, Do-Young American Society for Biochemistry and Molecular Bi 2012 The Journal of biological chemistry Vol.287 No.42
<P>IL-32α is known as a proinflammatory cytokine. However, several evidences implying its action in cells have been recently reported. In this study, we present for the first time that IL-32α plays an intracellular mediatory role in IL-6 production using constitutive expression systems for IL-32α in THP-1 cells. We show that phorbol 12-myristate 13-acetate (PMA)-induced increase in IL-6 production by IL-32α-expressing cells was higher than that by empty vector-expressing cells and that this increase occurred in a time- and dose-dependent manner. Treatment with MAPK inhibitors did not diminish this effect of IL-32α, and NF-κB signaling activity was similar in the two cell lines. Because the augmenting effect of IL-32α was dependent on the PKC activator PMA, we tested various PKC inhibitors. The pan-PKC inhibitor Gö6850 and the PKCϵ inhibitor Ro-31-8220 abrogated the augmenting effect of IL-32α on IL-6 production, whereas the classical PKC inhibitor Gö6976 and the PKCδ inhibitor rottlerin did not. In addition, IL-32α was co-immunoprecipitated with PMA-activated PKCϵ, and this interaction was totally inhibited by the PKCϵ inhibitor Ro-31-8220. PMA-induced enhancement of STAT3 phosphorylation was observed only in IL-32α-expressing cells, and this enhancement was inhibited by Ro-31-8220, but not by Gö6976. We demonstrate that IL-32α mediated STAT3 phosphorylation by forming a trimeric complex with PKCϵ and enhanced STAT3 localization onto the IL-6 promoter and thereby increased IL-6 expression. Thus, our data indicate that the intracellular interaction of IL-32α with PKCϵ and STAT3 promotes STAT3 binding to the IL-6 promoter by enforcing STAT3 phosphorylation, which results in increased production of IL-6.</P>