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- 저자 : Guanhao Li (검색결과 3 건)
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Effects of G-Rh2 on mast cell-mediated anaphylaxis via AKT-Nrf2/NF-κB and MAPK-Nrf2/NF-κB pathways
Chang Xu,Liangchang Li,Chongyang Wang,Jingzhi Jiang,Li Li,Lianhua Zhu,Shan Jin,Zhehu Jin,Jung Joon Lee,Guanhao Li,Guanghai Yan 고려인삼학회 2022 Journal of Ginseng Research Vol.46 No.4
Background: The effect of ginsenoside Rh2 (G-Rh2) on mast cell-mediated anaphylaxis remains unclear. Herein, we investigated the effects of G-Rh2 on OVA-induced asthmatic mice and on mast cell-mediatedanaphylaxis. Methods: Asthma model was established for evaluating airway changes and ear allergy. RPMCs and RBL-2H3 were used for in vitro experiments. Calcium uptake, histamine release and degranulation weredetected. ELISA and Western blot measured cytokine and protein levels, respectively. Results: G-Rh2 inhibited OVA-induced airway remodeling, the production of TNF-a, IL-4, IL-8, IL-1b andthe degranulation of mast cells of asthmatic mice. G-Rh2 inhibited the activation of Syk and Lyn in lungtissue of OVA-induced asthmatic mice. G-Rh2 inhibited serum IgE production in OVA induced asthmaticmice. Furthermore, G-Rh2 reduced the ear allergy in IgE-sensitized mice. G-Rh2 decreased the earthickness. In vitro experiments G-Rh2 significantly reduced calcium uptake and inhibited histaminerelease and degranulation in RPMCs. In addition, G-Rh2 reduced the production of IL-1b, TNF-a, IL-8, andIL-4 in IgE-sensitized RBL-2H3 cells. Interestingly, G-Rh2 was involved in the FcεRI pathway activation ofmast cells and the transduction of the Lyn/Syk signaling pathway. G-Rh2 inhibited PI3K activity in adose-dependent manner. By blocking the antigen-induced phosphorylation of Lyn, Syk, LAT, PLCg2, PI3KERK1/2 and Raf-1 expression, G-Rh2 inhibited the NF-kB, AKT-Nrf2, and p38MAPK-Nrf2 pathways. However, G-Rh2 up-regulated Keap-1 expression. Meanwhile, G-Rh2 reduced the levels of p-AKT,p38MAPK and Nrf2 in RBL-2H3 sensitized IgE cells and inhibited NF-kB signaling pathway activation byactivating the AKT-Nrf2 and p38MAPK-Nrf2 pathways. Conclusion: G-Rh2 inhibits mast cell-induced allergic inflammation, which might be mediated by theAKT-Nrf2/NF-kB and p38MAPK-Nrf2/NF-kB signaling pathways
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Juan Wang,Haoming Liu,Haili Wang,Mingxun Cui,Qing Jin,Tie Jin,Fushun Cui,Taihua Cui,Cheng Yun Liang,김범식,Guanhao Li 한국식품과학회 2016 Food Science and Biotechnology Vol.25 No.4
An protease from Actinidia arguta for improving meat tenderness was purified, characterizedfrom wild A. arguta fruit by ammonium sulfate precipitation, Sephdex G-25 gel filtration chromatography,and DEAE Sepharose Fast Flow ion exchange chromatography, and its activity was investigated. Thepurified protease was subjected to sodium dodecyl sulfate polyacrylamide gel electrophoresis toobtain a single band of protease. The protease was purified successfully, and found to have a molecularweight of 23.8 kDa (mass spectrometry). The specific activity of the purified protease reached 53,428U/mg with a 25.5-fold purification factor and 9% activity recovery. Based on N-terminal sequencingresults, the A. arguta protease was derived from the class of actinidia proteases that have an Nterminalsequence of VLPDY VDWRS AGAVV. The protease was effective for tenderizing beef anddecomposing actomyosin, suggesting the potential application for improving meat tenderness.
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Wang, Juan,Liu, Haoming,Wang, Haili,Cui, Mingxun,Jin, Qing,Jin, Tie,Cui, Fushun,Cui, Taihua,Liang, Chengyun,Kim, Bumsik,Li, Guanhao 한국식품과학회 2016 Food Science and Biotechnology Vol.25 No.4
An protease from Actinidia arguta for improving meat tenderness was purified, characterized from wild A. arguta fruit by ammonium sulfate precipitation, Sephdex G-25 gel filtration chromatography, and DEAE Sepharose Fast Flow ion exchange chromatography, and its activity was investigated. The purified protease was subjected to sodium dodecyl sulfate polyacrylamide gel electrophoresis to obtain a single band of protease. The protease was purified successfully, and found to have a molecular weight of 23.8 kDa (mass spectrometry). The specific activity of the purified protease reached 53,428 U/mg with a 25.5-fold purification factor and 9% activity recovery. Based on N-terminal sequencing results, the A. arguta protease was derived from the class of actinidia proteases that have an N-terminal sequence of VLPDY VDWRS AGAVV. The protease was effective for tenderizing beef and decomposing actomyosin, suggesting the potential application for improving meat tenderness.
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