scholarly journals YDFYPSSTKDQQS (P3), a peptide from lupin protein, absorbed by Caco-2 cells, modulates cholesterol metabolism in HepG2 cells via SREBP-1 activation

2019 ◽  
Vol 43 (1) ◽  
pp. e12757
Author(s):  
Carmen Lammi ◽  
Chiara Zanoni ◽  
Anna Arnoldi ◽  
Gilda Aiello
Keyword(s):  
Hepg2 Cells ◽  
Cholesterol Metabolism ◽  
Lupin Protein

Oxysterols suppress constitutive fibrinogen expression

2003 ◽  
Vol 90 (07) ◽  
pp. 43-51 ◽  
Author(s):  
Hui Xia ◽  
Colvin Redman
Keyword(s):  
Apolipoprotein B ◽  
Hepg2 Cells ◽  
Cholesterol Metabolism ◽  
Acute Phase Protein ◽  
Feedback Mechanism ◽  
Cholesterol Homeostasis ◽  
Mrna Levels ◽  
Regulatory Pathway ◽  
Phase Protein ◽  
Artery Disease

SummaryElevated levels of both fibrinogen and cholesterol are risk factors in coronary artery disease. Previously we reported a metabolic link between fibrinogen and lipid metabolism in that HepG2 cells that were programmed by transfection of Bβ-fibrinogen cDNA to overexpress fibrinogen exhibited increased synthesis of cholesterol and increased secretion of apolipoprotein B. In this study we demonstrate that oxysterols, which participate in maintaining cholesterol homeostasis, also down regulate fibrinogen expression. Treatment of HepG2 cells with 25-hydroxycholesterol lowered fibrinogen Aα, Bβ and γ mRNA levels and inhibited fibrinogen synthesis and secretion but had no effect on α1-antitrypsin which, like fibrinogen, is an acute-phase protein. The inhibition of fibrinogen synthesis by oxysterols was maintained in interleukin-6 treated cells. Other oxysterols, that inhibit cholesterol synthesis by a feedback mechanism, also diminished fibrinogen expression in HepG2, rat H-4-II-E hepatoma cells and in primary human hepatocytes. Overexpression of SREBP-1 and SREBP-2 by transfection of HepG2 cells, or treatment with a synthetic LXRα agonist, which affect cholesterol metabolism, did not affect fibrinogen expression. We conclude that fibrinogen and cholesterol may share a novel common regulatory pathway.

scholarly journals Effect of reduced low-density lipoprotein receptor level on HepG2 cell cholesterol metabolism

1998 ◽  
Vol 329 (1) ◽  
pp. 81-89 ◽  
Author(s):  
Lahoucine IZEM ◽  
Eric RASSART ◽  
Lassana KAMATE ◽  
Louise FALSTRAULT ◽  
David RHAINDS ◽  
...  
Keyword(s):  
Hepg2 Cell ◽  
Hepg2 Cells ◽  
Cholesterol Metabolism ◽  
Low Density Lipoprotein ◽  
Ldl Receptor ◽  
Constitutive Expression ◽  
Density Lipoprotein ◽  
Low Density ◽  
Apo B ◽  
Acat Activity

Low-density lipoproteins (LDL) are taken up by both LDL receptor (LDLr)-dependent and -independent pathways. In order to determine the importance of these pathways in the activity of the various enzymes that are important in maintaining the cellular cholesterol level in hepatic cells, we created HepG2 cells expressing lower levels of LDLr. Thus HepG2 cells were transfected with a constitutive expression vector (pRc/CMV) containing a fragment of LDLr cDNA inserted in an antisense manner. Stable transformants were obtained that showed significant reductions of 42, 72 and 85% of LDLr protein levels compared with the control, as demonstrated by immunoblotting and confirmed by the LDL binding assay. The best inactivation was achieved with the construct containing the first 0.7 kb of LDLr cDNA. Incubating the different HepG2 cell subtypes with LDL showed similar association of apolipoprotein B (apo B) or cholesteryl esters from LDL with the cells, indicating that the LDLr deficiency did not significantly affect LDL uptake by the cell. However, apoB degradation was reduced significantly by 71-82% in the most LDLr-deficient HepG2 cells. We also found that 3-hydroxy-3-methylglutaryl-CoA reductase (HMGCoA red) activity is significantly increased by 32-35% in HepG2 cells expressing very low levels of LDLr that also demonstrate a significant decrease of 20% in acyl-CoA:cholesterol acyltransferase (ACAT) activity. However, these effects are moderate compared with those observed when cells were incubated in lipoprotein-depleted medium, where a > 900% increase in HMGCoA red activity and a loss of 60% of ACAT activity was observed. Thus, in HepG2 cells, different levels of LDLr affect LDL-apoB degradation, but have very little effect on LDL association, HMGCoA red and ACAT activities, revealing that LDLr is more important in the clearance of LDL-apoB than in HepG2 cell cholesterol homoeostasis, a role that should be attributable to both LDLr-dependent and -independent pathways.

Effect of simvastatin on cholesterol metabolism in C2C12 myotubes and HepG2 cells, and consequences for statin-induced myopathy

2010 ◽  
Vol 79 (8) ◽  
pp. 1200-1209 ◽  
Author(s):  
Peter James Mullen ◽  
Barbara Lüscher ◽  
Hubert Scharnagl ◽  
Stephan Krähenbühl ◽  
Karin Brecht
Keyword(s):  
Hepg2 Cells ◽  
Cholesterol Metabolism ◽  
C2c12 Myotubes

Effect of FR194738, a potent inhibitor of squalene epoxidase, on cholesterol metabolism in HepG2 cells

2001 ◽  
Vol 431 (1) ◽  
pp. 11-16 ◽  
Author(s):  
Masae Sawada ◽  
Masahiko Matsuo ◽  
Hiroyuki Hagihara ◽  
Noriko Tenda ◽  
Akira Nagayoshi ◽  
...  
Keyword(s):  
Hepg2 Cells ◽  
Potent Inhibitor ◽  
Cholesterol Metabolism ◽  
Squalene Epoxidase

scholarly journals Long Non-coding RNAs Expression Profile in HepG2 Cells Reveals the Potential Role of Long Non-coding RNAs in the Cholesterol Metabolism

2015 ◽  
Vol 128 (1) ◽  
pp. 91-97 ◽  
Author(s):  
Gang Liu ◽  
Xinxin Zheng ◽  
Yanlu Xu ◽  
Jie Lu ◽  
Jingzhou Chen ◽  
...  
Keyword(s):  
Expression Profile ◽  
Hepg2 Cells ◽  
Potential Role ◽  
Cholesterol Metabolism ◽  
Non Coding Rnas
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