scholarly journals Stevia: limiting cholesterol synthesis in Hep-G2 cells

2020 ◽  
pp. 110-119
Author(s):  
Amirul Nazhan Ilias ◽  
Hazilawati Hamzah ◽  
Intan Safinar Ismail ◽  
Mokrish Ajat
Keyword(s):  
Cholesterol Synthesis ◽  
De Novo ◽  
Stevia Rebaudiana ◽  
Dependent Manner ◽  
Hep G2 ◽  
Hep G2 Cells ◽  
High Concentration ◽  
Immunofluorescent Microscopy ◽  
G2 Cells

As of today, no literature has been reported on the efficacy of stevia on lipid regulations conducted in vitro. Thus, the current study was focusing on the potential of Stevia rebaudiana bertoni as an anti-hypercholesterolemia substitute in limiting the de novo cholesterol synthesis in Hep-G2 cell line. The cytotoxicity and lipid internalization effects of stevia on Hep-G2 cells were assessed quantitatively and qualitatively in this study. As evaluated by MTT assay, commercialized stevia (0.5-20.0 mg/ml) and stevioside (1.0-10 µM) inhibited Hep-G2 cells viability in a dose-dependent manner for 24 hours. IC50 was detected at 8.68 mg/ml (commercialized stevia) and 10.91 µM (stevioside). From the assay, suitable concentrations were chosen to study the effect of stevia on cholesterol internalization in Hep-G2 cells supplemented with exogenous lipids. Cholesterol quantification assay revealed that high concentration commercialized stevia and stevioside promoted significant cholesterol internalized in Hep-G2 cells as compared to simvastatin. Finally, immunofluorescent microscopy assessment was done to qualitatively observe the formation of lipid droplets and low-density lipoprotein receptor in relation to total cholesterol extracted. The microphotographs of immunofluorescent microscopy were in parallel to results obtained from the cholesterol quantification assay which further revealed the effect of stevia as a potential anti-hypercholesterolemia agent.

The Hep G2 Cell Line as a Possible Alternative to Isolated Hepatocytes in Cytotoxicity Studies

1988 ◽  
Vol 16 (1) ◽  
pp. 16-22
Author(s):  
Marina Marinovich ◽  
Jose L. Lorenzo ◽  
Liliana M. Flaminio ◽  
Agnese Granata ◽  
Corrado L. Galli
Keyword(s):  
Cell Line ◽  
Rat Hepatocytes ◽  
Prostaglandin E ◽  
Human Hepatoma ◽  
Hep G2 ◽  
Hep G2 Cells ◽  
Isolated Rat Hepatocytes ◽  
G2 Cells ◽  
Isolated Rat

The hepatotoxicity of carbon tetrachloride (CC14) was evaluated in vitro in freshly isolated rat hepatocytes and in the human hepatoma cell line, Hep G2. Toxicity was assessed by the leakage of cytosolic enzymes (lactate dehydrogenase and aspartate aminotransferase) and cell viability (trypan blue exclusion). The established human cells were less sensitive to CCl4-induced injury; higher doses of the toxic agent and longer incubation times were necessary to elicit cell damage. Micromolar concentrations of prostaglandin E2 significantly decreased enzyme leakage in both Hep G2 cells and rat hepatocytes challenged with CC14; a stable derivative of prostacyclin (ZK 36374) was ineffective. These results suggest that human hepatoma Hep G2 cells may represent a valid alternative to isolated rat hepatocytes for an initial approach to the in vitro evaluation of cell toxicity.

Synthesis and Processing of Human Serum Apolipoprotein AII in vitro and in Hep G2 Cells

1985 ◽  
Vol 366 (1) ◽  
pp. 173-180 ◽  
Author(s):  
Wilhelm STOFFEL ◽  
Rosemarie BLAU ◽  
Martin BURK
Keyword(s):  
Human Serum ◽  
Hep G2 ◽  
Hep G2 Cells ◽  
Synthesis And Processing ◽  
G2 Cells

Modelling ethanol cytotoxicity in vitro, in Hep G2 cells

1994 ◽  
Vol 27 (3) ◽  
pp. 211
Author(s):  
M.G. Neuman ◽  
N.H. Shear ◽  
C. Tiribelli
Keyword(s):  
Hep G2 ◽  
Hep G2 Cells ◽  
Ethanol Cytotoxicity ◽  
G2 Cells

scholarly journals Fukinolic Acid Derivatives and Triterpene Glycosides from Black Cohosh Inhibit CYP Isozymes, but are Not Cytotoxic to Hep-G2 Cells In Vitro

2010 ◽  
Vol 5 (2) ◽  
pp. 118-124 ◽  
Author(s):  
Yue Huang ◽  
Bei Jiang ◽  
Paiboon Nuntanakorn ◽  
Edward Kennelly ◽  
Stacy Shord ◽  
...  
Keyword(s):  
Triterpene Glycosides ◽  
Black Cohosh ◽  
Hep G2 ◽  
Hep G2 Cells ◽  
G2 Cells ◽  
Cyp Isozymes

Role of cytokines in ethanol-induced cytotoxicity in vitro in Hep G2 cells

1998 ◽  
Vol 115 (1) ◽  
pp. 157-166 ◽  
Author(s):  
Manuela G. Neuman ◽  
Neil H. Shear ◽  
Stefano Bellentani ◽  
Claudio Tiribelli
Keyword(s):  
Hep G2 ◽  
Hep G2 Cells ◽  
G2 Cells

In Vitro Apoptosis Enhancement of Hep-G2 Cells by PLA–TPGS and PLA–PEG Block Copolymer Encapsulated Curcumin Nanoparticles

2013 ◽  
Vol 42 (3) ◽  
pp. 255-257 ◽  
Author(s):  
Ha Phuong Thu ◽  
Duong Tuan Quang ◽  
Mai Thi Thu Trang ◽  
Tran Thi Hong Ha ◽  
Nguyen Hoai Nam ◽  
...  
Keyword(s):  
Block Copolymer ◽  
Hep G2 ◽  
Hep G2 Cells ◽  
Curcumin Nanoparticles ◽  
G2 Cells

In vitro toxicity of iron oxide nanoparticle: Oxidative damages on Hep G2 cells

2015 ◽  
Vol 67 (2) ◽  
pp. 197-203 ◽  
Author(s):  
Leila Sadeghi ◽  
Farzeen Tanwir ◽  
Vahid Yousefi Babadi
Keyword(s):  
Iron Oxide ◽  
In Vitro Toxicity ◽  
Iron Oxide Nanoparticle ◽  
Hep G2 ◽  
Hep G2 Cells ◽  
Oxidative Damages ◽  
Oxide Nanoparticle ◽  
G2 Cells

scholarly journals Estrogen Receptor β Activates the Human Retinoic Acid Receptorα -1 Promoter in Response to Tamoxifen and Other Estrogen Receptor Antagonists, but Not in Response to Estrogen

1999 ◽  
Vol 13 (3) ◽  
pp. 418-430 ◽  
Author(s):  
Aihua Zou ◽  
Keith B. Marschke ◽  
Katharine E. Arnold ◽  
Elaine M. Berger ◽  
Patrick Fitzgerald ◽  
...  
Keyword(s):  
Estrogen Receptor ◽  
Retinoic Acid ◽  
Receptor Binding ◽  
Transcriptional Activation ◽  
Retinoic Acid Receptor ◽  
Hep G2 ◽  
Hep G2 Cells ◽  
Amino Terminal ◽  
G2 Cells

Abstract Human estrogen receptor-α (hERα) or -β (hERβ) transfected into Hep G2 or COS1 cells each responded to estrogen to increase transcription from an estrogen-responsive element (ERE)-driven reporter vector with similar fold induction through a classical mechanism involving direct receptor binding to DNA. ER antagonists inhibited this estrogen induction through both hERα and hERβ, although raloxifene was more potent through ERα than ERβ, and tamoxifen was more potent via ERβ than ERα. We have shown previously that estrogen stimulated the human retinoic acid receptor-α-1 (hRARα-1) promoter through nonclassical EREs by a mechanism that was ERα dependent, but that did not involve direct receptor binding to DNA. We show here that in contrast to hERα, hERβ did not induce reporter activity driven by the hRARα-1 promoter in the presence of estrogen. While hERβ did not confer estrogen responsiveness on this promoter, it did elicit transcriptional activation in the presence of 4-hydroxytamoxifen (4-OH-Tam). Additionally, this 4-OH-Tam agonist activity via ERβ was completely blocked by estrogen. Like ERα, transcriptional activation of this promoter by ERβ was not mediated by direct receptor binding to DNA. While hERα was shown to act through two estrogen-responsive sequences within the promoter, hERβ acted only at the 3′-region, through two Sp1 sites, in response to 4-OH-Tam. Other ER antagonists including raloxifene, ICI-164,384 and ICI-182,780 also acted as agonists through ERβ via the hRARα-1 promoter. Through the use of mutant and chimeric receptors, it was shown that the 4-OH-Tam activity via ERβ from the hRARα-1 promoter in Hep G2 cells required the amino-terminal region of ERβ, a region that was not necessary for estrogen-induced ERβ activity from an ERE in Hep G2 cells. Additionally, the progesterone receptor (PR) antagonist RU486 acted as a weak (IC50 >1 μm) antagonist via hERα and as a fairly potent (IC50 ∼200 nm) antagonist via hERβ from an ERE-driven reporter in cells that do not express PR. Although RU486 bound only weakly to ERα or ERβ in vitro, it did bind to ERβ in whole-cell binding assays, and therefore, it is likely metabolized to an ERβ-interacting compound in the cell. Interestingly, RU486 acted as an agonist through ERβ to stimulate the hRARα-1 promoter in Hep G2 cells. These findings may have ramifications in breast cancer treatment regimens utilizing tamoxifen or other ER antagonists and may explain some of the known estrogenic or antiestrogenic biological actions of RU486.

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