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RAW264.7 세포에서 interferon-r 및 LPS에 의해 유도되는 NO생성에 미치는 TALT-35의 영향
박종일,박경석,김종석,박지훈,윤은진,송경섭,서강식,김훈,윤완희,박승길,임규,황병두 충남대학교 생물공학연구소 2006 생물공학연구지 Vol.12 No.-
TALP-35 purified from human term placenta is known to increase microtubule polymerization and stabilize the polymerized microtubule. To examine the effect of TALP-35 on immune system this study was performed. MTT assay was performed to investigate the effect of TALP-35 on the proliferation of RAW264.7 cells. TALP-35 dose dependently suppress the proliferation of RAW264.7 cells at high concentration (above 1 μM) in unstimulated cells, in case of 10 μM TALP-35 treated cells the suppression was 25% but in stimulated cells it was only 15%. Cosedimentation assay was carried out to investigate whether TALP-35 can bind to tubulin of RAW264.7, monocyte/macrophage lineage of mouse, and polymerize it. TALP-35 polymerize the tubulin of RAW264.7 cells and sedimented in dose-dependent manner. To investigate the effect of TALP-35 on the expression of iNOS protein western blotting was performed. The expression level of iNOS was decreased dose dependently in high concentration of TALP-35 treatment. To examine the activity of iNOS, secreted NO was determined by method based on Griess reaction. Interferon-γ and LPS-stimulated production of NO from RAW264.7 cells was decreased dose dependently above 0.1 μM concentration of TALP-35 and 50% is decreased at 10μM of it. This study shows TALP-35 can control cytokine induced-iNOS expression therefore it might control inflammatory diseases.
방사선 조사에 의한 phospholipase D 활성화 연구
김영래,김기환,조문준,임규,황병두,박승길 충남대학교 의과대학 의학연구소 2002 충남의대잡지 Vol.29 No.1
Activation of oleate-dependent phospholipase D (PLD) isozyme by irradiation was reported previously. However, the effects of irradiation on other PLD isotypes (PLD1 and PLD2) have not been studied. There are several kinds of PLD isozymes in a cell. Therefore, it is difficult to study PLD isotype-specific activation in a cell by irradiation. We tested which isotype of PLD responds to irradiation. We used the fibroblasts cell lines overexpressing PLDl or PLD2 by introducing recombinant PLD1 or PLD2 cDNA. Phospholipids in cells were labelled with [(3)^H] myristic acid. Before irradiation, l-butanol was added. After irradiation with doses of 1, 2, and 10 Gray, we measured the formed phosphatidylbutanol containing [(3)^H] myristic acid. The overexpressed PLD isotypes were functional in those cell lines. PLD2 activity was enhanced by irradiation when we compared the PLD activations between control and PLD1 or PLD2 overexpressing cells. However PLD1 was not activated by irradiation. PLD2 isozyme, but not PLD1, was activated by irradiation. One Gray irradiation showed the maximal effect on PLD2 activation. The activation mechanism and physiological significance of PLD2 activation by irradiation remain to be uncovered.
Enhancement of ATP-induced Currents by Phospholipase D1 Overexpressed in PC12 Cells
Park, Jin-Bong,Kim, Young-Rae,Jeon, Byeong-Hwa,Park, Seung-Kiel,Oh, Sae-Ock,Kim, Young-Geun,Lee, Sang-Do,Kim, Kwang-Jin The Korean Society of Pharmacology 2003 The Korean Journal of Physiology & Pharmacology Vol.7 No.4
Using phospholipase D1 (PLD1)-overexpressing PC12 (PLD1-PC12) cells, the regulatory roles of PLD1 on ATP-induced currents were investigated. In control and PLD1-PC12 cells, ATP increased PLD activity in an external $Ca^{2+}$ dependent manner. PLD activity stimulated by ATP was substantially larger in PLD1-PC12 cells than in control cells. In whole-cell voltage-clamp mode, ATP induced transient inward and outward currents. The outward currents inhibited by TEA or charybdotoxin were significantly larger in PLD1-PC12 cells than in control cells. The inward currents known as $Ca^{2+}$ permeable nonselective cation currents were also larger in PLD1-PC12 cells than in control cells. However, the difference between the two groups of cells disappeared in $Ca^{2+}$-free external solution, where ATP did not activate PLD. Finally, ATP-induced $^{45}Ca$ uptakes were also larger in PLD1-PC12 cells than in control cells. These results suggest that PLD enhances ATP-induced $Ca^{2+}$ influx via $Ca^{2+}$ permeable nonselective cation channels and increases subsequent $Ca^{2+}$-activated $K^+$ currents in PC12 cells.
Adenine Inhibits B16-F10 Melanoma Cell Proliferation
Prashanta Silwal,Seung-Kiel Park 대한의생명과학회 2020 Biomedical Science Letters Vol.26 No.3
Adenine, a purine base, is a structural component of essential biomolecules such as nucleic acids and adenine nucleotides. Its physiological roles have been uncovered. Adenine suppresses IgE-mediated allergy and LPS-induced inflammation. Although adenine is known to inhibit lymphocyte proliferation, the effect of adenine to melamoma cells is not reported. Here, we investigated the growth inhibitory effects of adenine on B16-F10 mouse melanoma cells. Adenine suppressed the proliferation of B16-F10 cells in dose-dependent manner with the maximal inhibitory dose of 2 mM. Adenine treatment induced cell death molecular markers such as PARP and caspase 3 cleavages. Pan-caspase inhibitor z-VAD dramatically rescued the cell death molecular markers, cell proliferation recovered marginally. These results provide the possibility of adenine to be used as an anti-tumor agent.
Zheng, Meizi,Son, Mee-Young,Park, Chung,Park, Jong-Il,Jo, Eun-Kyeong,Yoon, Wan-Hee,Park, Seung-Kiel,Hwang, Byung-Doo,Lim, Kyu 충남대학교 암공동연구소 2006 암공동연구소 업적집 Vol.5 No.
Vimentin is a member of the intermediate filament family, and the NF-kB binding site is located in the human vimentin promoter. To gain insight into the role of NF-kB in the regulation of the vimentin gene during 12-O-tetra-decanoylphorbol-13-acetate (TPA)-dependent differentiation of HL-60 cells, the effect of pyrrolidine dithiocarbametc (PDTC) has been investigated using Northern blot hybridization and DNA mobility shift assay. PDTC inhibited macrophage-like morphologic change of HL-60 cells by TPA. TPA-dependent increase of vimentin mRNA level was decreased in a time- and dose-dependent manner by pretreatmcnt with PDTC. One DNA-protcin complex was formed by DNA mobility shift assay when the NF-kB or AP-1 binding sites were incubated with nuclear extract prepared from TPA-treated HI-60 cells, hut no protein bound in control HL-60 cells without TPA. After PDTC pretreatmcnt. NF-kB binding activity vanished but AP-I binding activity was unchanged. Taken together, these results suggest that NF-kB may be an essential transacting factor for transcriptional repression of the vimentin gene by PDTC during TPA-dependent differentiation of HL-60 cells.
Adenine attenuates lipopolysaccharide-induced inflammatory reactions
Silwal, Prashanta,Lim, Kyu,Heo, Jun-Young,Park, Jong IL,Namgung, Uk,Park, Seung-Kiel The Korean Society of Pharmacology 2018 The Korean Journal of Physiology & Pharmacology Vol.22 No.4
A nucleobase adenine is a fundamental component of nucleic acids and adenine nucleotides. Various biological roles of adenine have been discovered. It is not produced from degradation of adenine nucleotides in mammals but produced mainly during polyamine synthesis by dividing cells. Anti-inflammatory roles of adenine have been supported in IgE-mediated allergic reactions, immunological functions of lymphocytes and dextran sodium sulfate-induced colitis. However adenine effects on Toll-like receptor 4 (TLR4)-mediated inflammation by lipopolysaccharide (LPS), a cell wall component of Gram negative bacteria, is not examined. Here we investigated anti-inflammatory roles of adenine in LPS-stimulated immune cells, including a macrophage cell line RAW264.7 and bone marrow derived mast cells (BMMCs) and peritoneal cells in mice. In RAW264.7 cells stimulated with LPS, adenine inhibited production of pro-inflammatory cytokines $TNF-{\alpha}$ and IL-6 and inflammatory lipid mediators, prostaglandin $E_2$ and leukotriene $B_4$. Adenine impeded signaling pathways eliciting production of these inflammatory mediators. It suppressed $I{\kappa}B$ phosphorylation, nuclear translocation of nuclear factor ${\kappa}B$ ($NF-{\kappa}B$), phosphorylation of Akt and mitogen activated protein kinases (MAPKs) JNK and ERK. Although adenine raised cellular AMP which could activate AMP-dependent protein kinase (AMPK), the enzyme activity was not enhanced. In BMMCs, adenine inhibited the LPS-induced production of $TNF-{\alpha}$, IL-6 and IL-13 and also hindered phosphorylation of $NF-{\kappa}B$ and Akt. In peritoneal cavity, adenine suppressed the LPS-induced production of $TNF-{\alpha}$ and IL-6 by peritoneal cells in mice. These results show that adenine attenuates the LPS-induced inflammatory reactions.
Zheng, Meizi,Son, Mee-Young,Park, Chung,Park, Jong-Il,Jo, Eun-Kyeong,Yoon, Wan-Hee,Park, Seung-Kiel,Hwang, Byung-Doo,Lim, Kyu 충남대학교 암연구소 2006 암연구소 업적집 Vol.5 No.-
Vimentin is a member of the intermediate filament family, and the NF-kB binding site is located in the human vimentin promoter. To gain insight into the role of NF-kB in the regulation of the vimentin gene during 12-O-tetra-decanoylphorbol-13-acetate (TPA)-dependent differentiation of HL-60 cells, the effect of pyrrolidine dithiocarbametc (PDTC) has been investigated using Northern blot hybridization and DNA mobility shift assay. PDTC inhibited macrophage-like morphologic change of HL-60 cells by TPA. TPA-dependent increase of vimentin mRNA level was decreased in a time- and dose-dependent manner by pretreatmcnt with PDTC. One DNA-protcin complex was formed by DNA mobility shift assay when the NF-kB or AP-1 binding sites were incubated with nuclear extract prepared from TPA-treated HI-60 cells, hut no protein bound in control HL-60 cells without TPA. After PDTC pretreatmcnt. NF-kB binding activity vanished but AP-I binding activity was unchanged. Taken together, these results suggest that NF-kB may be an essential transacting factor for transcriptional repression of the vimentin gene by PDTC during TPA-dependent differentiation of HL-60 cells.