scholarly journals Peroxisome proliferator-activated receptor gamma coactivator-1 alpha (PGC-1α) upregulated E-cadherin expression in HepG2 cells

FEBS Letters ◽  
2008 ◽  
Vol 582 (5) ◽  
pp. 627-634 ◽  
Author(s):  
Hui-Ju Lee ◽  
Yeu Su ◽  
Wing-Yiu Lui ◽  
Gar-Yang Chau ◽  
Pen-Hui Yin ◽  
...  
Keyword(s):  
Hepg2 Cells ◽  
Peroxisome Proliferator ◽  
Peroxisome Proliferator Activated Receptor ◽  
E Cadherin

scholarly journals Bioinformatics analysis of different candidate genes involved in hepatocellular carcinoma induced by HepG2 cells or tumor cells of patients

2020 ◽  
Vol 48 (6) ◽  
pp. 030006052093211
Author(s):  
Xiang Zhang ◽  
Songna Yin ◽  
Ke Ma
Keyword(s):  
Hepatocellular Carcinoma ◽  
Hepg2 Cells ◽  
Liver Parenchyma ◽  
Preclinical Study ◽  
Gene Expression Omnibus ◽  
Receptor Interaction ◽  
Peroxisome Proliferator ◽  
Ppi Network ◽  
Peroxisome Proliferator Activated Receptor ◽  
Protein Protein Interaction

Objective Hepatocellular carcinoma (HCC) is a common cancer with a high mortality rate; the molecular mechanism involved in HCC remain unclear. We aimed to provide insight into HCC induced with HepG2 cells and identify genes and pathways associated with HCC, as well as potential therapeutic targets. Methods Dataset GSE72581 was downloaded from the Gene Expression Omnibus, including samples from mice injected in liver parenchyma with HepG2 cells, and from mice injected with cells from patient tumor explants. Differentially expressed genes (DEGs) between the two groups of mice were analyzed. Then, gene ontology and Kyoto Encyclopedia of Gene and Genomes pathway enrichment analyses were performed. The MCODE plug-in in Cytoscape was applied to create a protein–protein interaction (PPI) network of DEGs. Results We identified 1,405 DEGs (479 upregulated and 926 downregulated genes), which were enriched in complement and coagulation cascades, peroxisome proliferator-activated receptor signaling pathway, and extracellular matrix–receptor interaction. The top 4 modules and top 20 hub genes were identified from the PPI network, and associations with overall survival were determined using Kaplan–Meier analysis. Conclusion This preclinical study provided data on molecular targets in HCC that could be useful in the clinical treatment of HCC.

Peroxisome proliferator-activated receptor transactivational effects in HepG2 cells of cembranoids from the soft coral Lobophytum crassum Von Marenzeller

2014 ◽  
Vol 38 (5) ◽  
pp. 769-775 ◽  
Author(s):  
Nguyen Phuong Thao ◽  
Bui Thi Thuy Luyen ◽  
Nguyen Thi Thanh Ngan ◽  
Le Duc Dat ◽  
Nguyen Xuan Cuong ◽  
...  
Keyword(s):  
Hepg2 Cells ◽  
Soft Coral ◽  
Peroxisome Proliferator ◽  
Peroxisome Proliferator Activated Receptor

scholarly journals Curcumin Suppresses Intestinal Fibrosis by Inhibition of PPARγ-Mediated Epithelial-Mesenchymal Transition

2017 ◽  
Vol 2017 ◽  
pp. 1-12 ◽  
Author(s):  
Su Xu ◽  
Bin Jiang ◽  
Hui Wang ◽  
Cunsi Shen ◽  
Hao Chen ◽  
...  
Keyword(s):  
Nuclear Translocation ◽  
Epithelial Mesenchymal Transition ◽  
Smooth Muscle Actin ◽  
Peroxisome Proliferator ◽  
Colon Tissue ◽  
Peroxisome Proliferator Activated Receptor ◽  
Smad Pathway ◽  
Mesenchymal Transition ◽  
Intestinal Fibrosis ◽  
E Cadherin

Intestinal fibrotic stricture is a major complication of Crohn’s disease (CD) and epithelial-to-mesenchymal transition (EMT) is considered as an important contributor to the formation of intestinal fibrosis by increasing extracellular matrix (ECM) proteins. Curcumin, a compound derived from rhizomes ofCurcuma, has been demonstrated with a potent antifibrotic effect. However, its effect on intestinal fibrosis and the potential mechanism is not completely understood. Here we found that curcumin pretreatment significantly represses TGF-β1-induced Smad pathway and decreases its downstreamα-smooth muscle actin (α-SMA) gene expression in intestinal epithelial cells (IEC-6); in contrast, curcumin increases expression of E-cadherin and peroxisome proliferator-activated receptorγ(PPARγ) in IEC-6. Moreover, curcumin promotes nuclear translocation of PPARγand the inhibitory effect of curcumin on EMT could be reversed by PPARγantagonist GW9662. Consistently, in the rat model of intestinal fibrosis induced by 2,4,5-trinitrobenzene sulphonic acid (TNBS), oral curcumin attenuates intestinal fibrosis by increasing the expression of PPARγand E-cadherin and decreasing the expression ofα-SMA, FN, and CTGF in colon tissue. Collectively, these results indicated that curcumin is able to prevent EMT progress in intestinal fibrosis by PPARγ-mediated repression of TGF-β1/Smad pathway.

scholarly journals LRRK2 Regulates CPT1A to Promote β-Oxidation in HepG2 Cells

Molecules ◽  
2020 ◽  
Vol 25 (18) ◽  
pp. 4122 ◽  
Author(s):  
Chiao-Wei Lin ◽  
Yu-Ju Peng ◽  
Yuan-Yu Lin ◽  
Harry John Mersmann ◽  
Shih-Torng Ding
Keyword(s):  
Lipid Metabolism ◽  
Hepg2 Cells ◽  
Peroxisome Proliferator ◽  
Peroxisome Proliferator Activated Receptor ◽  
Alcoholic Fatty Liver ◽  
Cytokine Tumor Necrosis Factor ◽  
Factor Α ◽  
Amp Activated Protein Kinase ◽  
Necrosis Factor

Leucine-rich repeat kinase 2 (LRRK2) is involved in lipid metabolism; however, the role of LRRK2 in lipid metabolism to affect non-alcoholic fatty liver disease (NAFLD) is still unclear. In the mouse model of NAFLD induced by a high-fat diet, we observed that LRRK2 was decreased in livers. In HepG2 cells, exposure to palmitic acid (PA) down-regulated LRRK2. Overexpression and knockdown of LRRK2 in HepG2 cells were performed to further investigate the roles of LRRK2 in lipid metabolism. Our results showed that β-oxidation in HepG2 cells was promoted by LRRK2 overexpression, whereas LRRK2 knockdown inhibited β-oxidation. The critical enzyme of β-oxidation, carnitine palmitoyltransferase 1A (CPT1A), was positively regulated by LRRK2. Our data suggested that the regulation of CPT1A by LRRK2 may be via the activation of AMP-activated protein kinase (AMPK) and peroxisome proliferator-activated receptor α (PPARα). The overexpression of LRRK2 reduced the concentration of a pro-inflammatory cytokine, tumor necrosis factor α (TNFα), induced by PA. The increase in β-oxidation may promote lipid catabolism to suppress inflammation induced by PA. These results indicated that LRRK2 participated in the regulation of β-oxidation and suggested that the decreased LRRK2 may promote inflammation by suppressing β-oxidation in the liver.

Sign in / Sign up

Export Citation Format

Share Document