http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
- 中文 을 입력하시려면 zhongwen을 입력하시고 space를누르시면됩니다.
- 北京 을 입력하시려면 beijing을 입력하시고 space를 누르시면 됩니다.
RISS 인기검색어
- 검색키워드
- 저자 : Zhou Yaru (검색결과 4 건)
- 무료
- 기관 내 무료
- 유료
-
Yaru Li,Shuchen Zhang,Ziwei Zhu,Ruonan Zhou,Pingyuan Xu,Lingyan Zhou,Yue Kan,Jiao Li,Juan Zhao,Penghua Fang,Xizhong Yu,Wenbin Shang 고려인삼학회 2022 Journal of Ginseng Research Vol.46 No.4
Background: Ginsenoside Rb1 (GRb1) is capable of regulating lipid and glucose metabolism through itsaction on adipocytes. However, the beneficial role of GRb1-induced up-regulation of adiponectin in liversteatosis remains unelucidated. Thus, we tested whether GRb1 ameliorates liver steatosis and insulinresistance by promoting the expression of adiponectin. Methods: 3T3-L1 adipocytes and hepatocytes were used to investigate GRb1's action on adiponectinexpression and triglyceride (TG) accumulation. Wild type (WT) mice and adiponectin knockout (KO)mice fed high fat diet were treated with GRb1 for 2 weeks. Hepatic fat accumulation and function as wellas insulin sensitivity was measured. The activation of AMPK was also detected in the liver andhepatocytes. Results: GRb1 reversed the reduction of adiponectin secretion in adipocytes. The conditioned medium(CM) from adipocytes treated with GRb1 reduced TG accumulation in hepatocytes, which was partlyattenuated by the adiponectin antibody. In the KO mice, the GRb1-induced significant decrease of TGcontent, ALT and AST was blocked by the deletion of adiponectin. The elevations of GRb1-induced insulinsensitivity indicated by OGTT, ITT and HOMA-IR were also weakened in the KO mice. The CM treatmentsignificantly enhanced the phosphorylation of AMPK in hepatocytes, but not GRb1 treatment. Likewise,the phosphorylation of AMPK in liver of the WT mice was increased by GRb1, but not in the KO mice. Conclusions: The up-regulation of adiponectin by GRb1 contributes to the amelioration of liver steatosisand insulin resistance, which further elucidates a new mechanism underlying the beneficial effects ofGRb1 on obesity
-
Incomplete autophagy promotes the replication of Mycoplasma hyopneumoniae
Wang Zhaodi,Wen Yukang,Zhou Bingqian,Tian Yaqin,Ning Yaru,Ding Honglei 한국미생물학회 2021 The journal of microbiology Vol.59 No.8
Autophagy is an important cellular homeostatic mechanism for recycling of degradative proteins and damaged organelles. Autophagy has been shown to play an important role in cellular responses to bacteria and bacterial replication. However, the role of autophagy in Mycoplasma hyopneumoniae infection and the pathogenic mechanism is not well characterized. In this study, we showed that M. hyopneumoniae infection significantly increases the number of autophagic vacuoles in host cells. Further, we found significantly enhanced expressions of autophagy marker proteins (LC3-II, ATG5, and Beclin 1) in M. hyopneumoniae-infected cells. Moreover, immunofluorescence analysis showed colocalization of P97 protein with LC3 during M. hyopneumoniae infection. Interestingly, autophagic flux marker, p62, accumulated with the induction of infection. Conversely, the levels of p62 and LC3-II were decreased after treatment with 3-MA, inhibiting the formation of autophagosomes, during infection. In addition, accumulation of autophagosomes promoted the expression of P97 protein and the survival of M. hyopneumoniae in PK- 15 cells, as the replication of M. hyopneumoniae was downregulated by adding 3-MA. Collectively, these findings provide strong evidence that M. hyopneumoniae induces incomplete autophagy, which in turn enhances its reproduction in host cells. These findings provide novel insights into the interaction of M. hyopneumoniae and host.
-
Xiao Kai,Liu Xiaohui,Zhang Aidong,Zha Dingshi,Zhu WeiMin,Tan Feng,Huang Qianru,Zhou Yaru,Zhang Min,Li Jianyong,Wu Xuexia 한국원예학회 2022 Horticulture, Environment, and Biotechnology Vol.63 No.5
Browning of fresh-cut eggplant (Solanum melongena L.) reduces its sensory and nutritional qualities and further influences consumption. Polyphenolic oxidases (PPOs) are key enzymes involved in browning, but the mechanisms that regulate the expression of PPO genes are still unclear. Here, 12 SmPPO genes were identified and phylogenetic analysis clustered these genes into four branches. Protein and cis-regulatory element analyses showed that the SmPPO gene family has a conserved gene structure and diverse functions. Gene expression analysis in different tissues showed that the expression of SmPPO2, SmPPO3, SmPPO6, SmPPO7, and SmPPO10 was higher in the flesh of the browning-sensitive inbred line ‘36’ than in the flesh of the browning-resistant line ‘Fu’. Furthermore, almost all SmPPO genes in ‘36’ were upregulated at 4 °C and 36 °C compared with those in ‘Fu’, and the expression increased earlier after harvest. In addition, SmPPO1, SmPPO6, SmPPO7, and SmPPO10 expression was significantly elevated in ‘36’ after 2 days at 36 °C. These results suggest that SmPPOs are key modulators of eggplant browning and provide candidate genes for further research on the mechanisms regulating fruit browning.
-
HCBP6 upregulates human SREBP1c expression by binding to C/EBPβ-binding site in the SREBP1c promoter
( Xueliang Yang ),( Ming Han ),( Shunai Liu ),( Xiaoxue Yuan ),( Xiaojing Liu ),( Shenghu Feng ),( Li Zhou ),( Yaru Li ),( Hongping Lu ),( Jun Cheng ),( Shumei Lin ) 생화학분자생물학회(구 한국생화학분자생물학회) 2018 BMB Reports Vol.51 No.1
Sterol regulatory element-binding protein-1c (SREBP1c) plays an important role in triglyceride (TG) homeostasis. Although our previous study showed that hepatitis C virus core-binding protein 6 (HCBP6) regulates SREBP1c expression to maintain intracellular TG homeostasis, the mechanism underlying this regulation is unclear. In the present study, we found that HCBP6 increased intracellular TG levels by upregulating SREBP1c expression. HCBP6 increased SREBP1c transcription by directly binding to the SREBP1c promoter (at the -139- to +359-bp region). Moreover, we observed that HCBP6 interacted with C/EBPβ-binding site in the SREBP1c promoter both in vitro and in vivo. These results indicate that HCBP6 upregulates human SREBP1c expression by binding to the C/EBPβ-binding site in the SREBP1c promoter. [BMB Reports 2018; 51(1): 33-38]
DBpia
ScienceON연관 검색어 추천
이 검색어로 많이 본 자료
활용도 높은 자료
