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Hong-Lin Xu,Guang-Hong Chen,Yu-Ting Wu,Ling-Peng Xie,Zhang-Bin Tan,Bin Liu,Hui-Jie Fan,Hong-Mei Chen,Gui-Qiong Huang,Min Liu,Ying-Chun Zhou 고려인삼학회 2022 Journal of Ginseng Research Vol.46 No.1
Background: Panax ginseng Meyer (P. ginseng), a herb distributed in Korea, China and Japan, exerts benefits on diverse inflammatory conditions. However, the underlying mechanism and active ingredients remains largely unclear. Herein, we aimed to explore the active ingredients of P. ginseng against inflammation and elucidate underlying mechanisms. Methods: Inflammation model was constructed by lipopolysaccharide (LPS) in C57BL/6 mice and RAW264.7 macrophages. Molecular docking, molecular dynamics, surface plasmon resonance imaging (SPRi) and immunofluorescence were utilized to predict active component. Results: P. ginseng significantly inhibited LPS-induced lung injury and the expression of proinflammatory factors, including TNF-a, IL-6 and IL-1b. Additionally, P. ginseng blocked fluorescence-labeled LPS (LPS488) binding to the membranes of RAW264.7 macrophages, the phosphorylation of nuclear factor-kB (NF-kB) and mitogen-activated protein kinases (MAPKs). Furthermore, molecular docking demonstrated that ginsenoside Ro (GRo) docked into the LPS binding site of toll like receptor 4 (TLR4)/myeloid differentiation factor 2 (MD2) complex. Molecular dynamic simulations showed that the MD2-GRo binding conformation was stable. SPRi demonstrated an excellent interaction between TLR4/MD2 complex and GRo (KD value of 1.16 × 10<SUP>-9</SUP> M). GRo significantly inhibited LPS488 binding to cell membranes. Further studies showed that GRo markedly suppressed LPS-triggered lung injury, the transcription and secretion levels of TNF-α, IL-6 and IL-1β. Moreover, the phosphorylation of NF-kB and MAPKs as well as the p65 subunit nuclear translocation were inhibited by GRo dose-dependently. Conclusion: Our results suggest that GRo exerts anti-inflammation actions by direct inhibition of TLR4 signaling pathway.
Patent Ductus Arteriosus and Pulmonary Valve Stenosis in A Patient with 18p Deletion Syndrome
Chun-Hong Xie,Jian-Bin Yang,Fang-Qi Gong,Zheng-Yan Zhao 연세대학교의과대학 2008 Yonsei medical journal Vol.49 No.3
We report on a patient with a partial deletion on the short arm of chromosome 18 (del 18p), who presented with dysmorphic features and delayed developmental milestones as well as with a patent ductus arteriosus (PDA) and pulmonary valve stenosis (PS). Several forms of congenital heart disease (CHD) are found in about 10% of patients with del (18p), but coexisting PDA and PS have not been reported. Del (18p) must be considered in patients with characteristic phenotypic abnormalities and congenital heart disease, including a combination of PDA and PS.
Chun-Ying Liu,Rui-Xin Zhou,Chang-Kai Sun,Ying-Hua Jin,Hong-Shan Yu,Tian-Yang Zhang,Long-Quan Xu,Feng-Xie Jin 고려인삼학회 2015 Journal of Ginseng Research Vol.39 No.3
Background: Minor ginsenosides, those having low content in ginseng, have higher pharmacological activities. To obtain minor ginsenosides, the biotransformation of American ginseng protopanaxadiol (PPD)-ginsenoside was studied using special ginsenosidase type-I from Aspergillus niger g.848. Methods: DEAE (diethylaminoethyl)-cellulose and polyacrylamide gel electrophoresis were used in enzyme purification, thin-layer chromatography and high performance liquid chromatography (HPLC) were used in enzyme hydrolysis and kinetics; crude enzyme was used in minor ginsenoside preparation from PPD-ginsenoside; the products were separated with silica-gel-column, and recognized by HPLC and NMR (Nuclear Magnetic Resonance). Results: The enzyme molecular weight was 75 kDa; the enzyme firstly hydrolyzed the C-20 position 20- O-b-D-Glc of ginsenoside Rb1, then the C-3 position 3-O-b-D-Glc with the pathway Rb1/Rd/F2/C-K. However, the enzyme firstly hydrolyzed C-3 position 3-O-b-D-Glc of ginsenoside Rb2 and Rc, finally hydrolyzed 20-O-L-Ara with the pathway Rb2/C-O/C-Y/C-K, and Rc/C-Mc1/C-Mc/C-K. According to enzyme kinetics, Km and Vmax of MichaeliseMenten equation, the enzyme reaction velocities on ginsenosides were Rb1 > Rb2 > Rc > Rd. However, the pure enzyme yield was only 3.1%, so crude enzyme was used for minor ginsenoside preparation. When the crude enzyme was reacted in 3% American ginseng PPD-ginsenoside (containing Rb1, Rb2, Rc, and Rd) at 45C and pH 5.0 for 18 h, the main products were minor ginsenosides C-Mc, C-Y, F2, and C-K; average molar yields were 43.7% for CMc from Rc, 42.4% for C-Y from Rb2, and 69.5% for F2 and C-K from Rb1 and Rd. Conclusion: Four monomer minor ginsenosides were successfully produced (at low-cost) from the PPDginsenosides using crude enzyme.
Gui Chun Wang,Jun Ping He,Deng Feng Hong,Yan Zhou Xie,Zheng Hua Xu,Ping Wu Liu,Guang Sheng Yang 한국유전학회 2007 Genes & Genomics Vol.29 No.4
9012AB is a recessive genic male sterility (RGMS) line in rapeseed, of which the male sterility is controlled by two pairs of recessive duplicate male sterile genes (Bnms3 and Bnms4) interacting with a recessive epistatic suppressor gene (esp). The recessive homozygosity at the esp locus (espesp) can suppress the expression of the recessive male sterility trait in homozygous plants (Bnms3Bnms3Bnms4Bnms4) and result in fertility restoration. A F2 population of 188 plants, derived from self-pollinated progenies of a 9012 AB fertile plants (BnMs3Bnms3Bnms4Bnms4EspEsp), was conducted to identify molecular markers linked to the recessive male sterility gene (Bnms3). By amplified fragment length polymorphism (AFLP) assay combining with bulked segregant analysis (BSA), 13 markers linked to Bnms3 were identified. Linkage analysis indicated that 13 AFLP markers were tightly linked to the Bnms3 gene with a genetic distance varying from 1.3 cM to 7.1 cM. Among them, one marker was co-dominant marker, 6 markers were in coupling phase with Bnms3, and the others were in repulsion phase with Bnms3 gene, One AFLP marker with a genetic distance of 1.4cM was further converted into a SCAR marker successfully, which have been applied in marker-assisted selection of RGMS lines and their temporary maintainers effectively.
Liu, Chun-Ying,Zhou, Rui-Xin,Sun, Chang-Kai,Jin, Ying-Hua,Yu, Hong-Shan,Zhang, Tian-Yang,Xu, Long-Quan,Jin, Feng-Xie The Korean Society of Ginseng 2015 Journal of Ginseng Research Vol.39 No.3
Background: Minor ginsenosides, those having low content in ginseng, have higher pharmacological activities. To obtain minor ginsenosides, the biotransformation of American ginseng protopanaxadiol (PPD)-ginsenoside was studied using special ginsenosidase type-I from Aspergillus niger g.848. Methods: DEAE (diethylaminoethyl)-cellulose and polyacrylamide gel electrophoresis were used in enzyme purification, thin-layer chromatography and high performance liquid chromatography (HPLC) were used in enzyme hydrolysis and kinetics; crude enzyme was used in minor ginsenoside preparation from PPD-ginsenoside; the products were separated with silica-gel-column, and recognized by HPLC and NMR (Nuclear Magnetic Resonance). Results: The enzyme molecular weight was 75 kDa; the enzyme firstly hydrolyzed the C-20 position 20-O-${\beta}$-D-Glc of ginsenoside Rb1, then the C-3 position 3-O-${\beta}$-D-Glc with the pathway $Rb1{\rightarrow}Rd{\rightarrow}F2{\rightarrow}C-K$. However, the enzyme firstly hydrolyzed C-3 position 3-O-${\beta}$-D-Glc of ginsenoside Rb2 and Rc, finally hydrolyzed 20-O-L-Ara with the pathway $Rb2{\rightarrow}C-O{\rightarrow}C-Y{\rightarrow}C-K$, and $Rc{\rightarrow}C-Mc1{\rightarrow}C-Mc{\rightarrow}C-K$. According to enzyme kinetics, $K_m$ and $V_{max}$ of Michaelis-Menten equation, the enzyme reaction velocities on ginsenosides were Rb1 > Rb2 > Rc > Rd. However, the pure enzyme yield was only 3.1%, so crude enzyme was used for minor ginsenoside preparation. When the crude enzyme was reacted in 3% American ginseng PPD-ginsenoside (containing Rb1, Rb2, Rc, and Rd) at $45^{\circ}C$ and pH 5.0 for 18 h, the main products were minor ginsenosides C-Mc, C-Y, F2, and C-K; average molar yields were 43.7% for C-Mc from Rc, 42.4% for C-Y from Rb2, and 69.5% for F2 and C-K from Rb1 and Rd. Conclusion: Four monomer minor ginsenosides were successfully produced (at low-cost) from the PPD-ginsenosides using crude enzyme.
Dynamic changes of multi-notoginseng stem-leaf ginsenosides in reaction with ginsenosidase type-I
Yongkun Xiao,Chun-Ying Liu,임완택,Shuang Chen,Kangze Zuo,Hong Shan Yu,Jian-Guo Song,Long-Quan Xu,Tea-Hoo Yi,Feng Xie Jin 고려인삼학회 2019 Journal of Ginseng Research Vol.43 No.2
Background: Notoginseng stem-leaf (NGL) ginsenosides have not been well used. To improve their utilization, the biotransformation of NGL ginsenosides was studied using ginsenosidase type-I from Aspergillus niger g.848. Methods: NGL ginsenosides were reacted with a crude enzyme in the RAT-5D bioreactor, and the dynamic changes of multi-ginsenosides of NGL were recognized by HPLC. The reaction products were separated using a silica gel column and identified by HPLC and NMR. Results: All the NGL ginsenosides are protopanaxadiol-type ginsenosides; the main ginsenoside contents are 27.1% Rb3, 15.7% C-Mx1, 13.8% Rc, 11.1% Fc, 7.10% Fa, 6.44% C-Mc, 5.08% Rb2, and 4.31% Rb1. In the reaction of NGL ginsenosides with crude enzyme, the main reaction of Rb3 and C-Mx1 occurred through Rb3/C-Mx1/C-Mx; when reacted for 1 h, Rb3 decreased from 27.1% to 9.82 %, C-Mx1 increased from 15.5% to 32.3%, C-Mx was produced to 6.46%, finally into C-Mx and a small amount of C-K. When reacted for 1.5 h, all the Rb1, Rd, and Gyp17 were completely reacted, and the reaction intermediate F2 was produced to 8.25%, finally into C-K. The main reaction of Rc (13.8%) occurred through Rc/C-Mc1/CMc/ C-K. The enzyme barely hydrolyzed the terminal xyloside on 3-Oe or 20-O-sugar-moiety of the substrate; therefore, 9.43 g C-Mx, 6.85 g C-K, 4.50 g R7, and 4.71 g Fc (hardly separating from the substrate) were obtained from 50 g NGL ginsenosides by the crude enzyme reaction. Conclusion: Four monomer ginsenosides were successfully produced and separated from NGL ginsenosides by the enzyme reaction.
MTHFR C677T Polymorphism and Colorectal Cancer Risk in Asians, a Meta-analysis of 21 Studies
Yang, Zhen,Zhang, Xie-Fu,Liu, Hong-Xiang,Hao, Yong-Shun,Zhao, Chun-Lin Asian Pacific Journal of Cancer Prevention 2012 Asian Pacific journal of cancer prevention Vol.13 No.4
Background: Previous studies concerning the association between methylenetetrahydrofolate reductase (MTHFR) C677T polymorphism and colorectal cancer risk in Asian populations generated conflicting results. A meta-analysis was therefore performed to allow a more reliable estimate of any link. Methods: Relevant studies concerning the association between the MTHFR C677T polymorphism and risk of colorectal cancer were included into this meta-analysis. The quality of the studies was assessed according to a predefined scale. Odds ratios (ORs) and 95% confidence intervals (CIs) were determined for this gene-disease association using fixed or random effect models according to the heterogeneity between included studies. Results: Finally, 21 studies with a total of 6692 cases and 8266 controls were included. Meta-analyses showed that there was an obvious association of the MTHFR 677T allele with decreased risk of colorectal cancer (OR = 0.91, 95%CI=0.85-0.98, P=0.011). Subgroup analyses by country further identified this association, with dietary folate as the main source of heterogeneity. Conclusion: The MTHFR 677T allele is associated with a lower risk of colorectal cancer in Asian populations, and there is effect modification by population plasma folate.
( Xue Feng Jin ),( Hong Shan Yu ),( Dong Ming Wang ),( Ting Qiang Liu ),( Chun Ying Liu ),( Dong Shan An ),( Wan Taek Im ),( Song Gun Kim ),( Feng Xie Jin ) 한국미생물 · 생명공학회 2012 Journal of microbiology and biotechnology Vol.22 No.3
In this paper, the kinetics of a cloned special glucosidase, named ginsenosidase type III hydrolyzing 3-O-glucoside of multi-protopanaxadiol (PPD)-type ginsenosides, were investigated. The gene (bgpA) encoding this enzyme was cloned from a Terrabacter ginsenosidimutans strain and then expressed in E. coli cells. Ginsenosidase type III was able to hydrolyze 3-O-glucoside of multi-PPD-type ginsenosides. For instance, it was able to hydrolyze the 3- O-β-D-(1→2)-glucopyranosyl of Rb1 to gypenoside XVII, and then to further hydrolyze the 3-O-β-D-glucopyranosyl of gypenoside XVII to gypenoside LXXV. Similarly, the enzyme could hydrolyze the glucopyranosyls linked to the 3-O- position of Rb2, Rc, Rd, Rb3, and Rg3. With a larger enzyme reaction Km value, there was a slower enzyme reaction speed; and the larger the enzyme reaction Vmax value, the faster the enzyme reaction speed was. The Km values from small to large were 3.85 mM for Rc, 4.08 mM for Rb1, 8.85 mM for Rb3, 9.09 mM for Rb2, 9.70 mM for Rg3(S), 11.4 mM for Rd and 12.9 mM for F2; and Vmax value from large to small was 23.2 mM/h for Rc, 16.6 mM/h for Rb1, 14.6 mM/h for Rb3, 14.3 mM/h for Rb2, 1.81mM/h for Rg3(S), 1.40 mM/h for Rd, and 0.41 mM/h for F2. According to the Vmax and Km values of the ginsenosidase type III, the hydrolysis speed of these substrates by the enzyme was Rc>Rb1>Rb3>Rb2>Rg3(S)>Rd>F2 in order.