γ-Glutamyl Transpeptidase and l-Cysteine Regulate Methylmercury Uptake by HepG2 Cells, a Human Hepatoma Cell Line

2000 ◽  
Vol 168 (1) ◽  
pp. 72-78 ◽  
Author(s):  
Wei Wang ◽  
Thomas W. Clarkson ◽  
Nazzareno Ballatori
Keyword(s):  
Cell Line ◽  
Hepg2 Cells ◽  
Hepatoma Cell ◽  
Hepatoma Cell Line ◽  
Human Hepatoma ◽  
Human Hepatoma Cell ◽  
Human Hepatoma Cell Line ◽  
Glutamyl Transpeptidase

Abstract 418: Bifunctional Role of Autophagy in Intracellular ApoB Degradation and Lipid Droplet Mobilization

2014 ◽  
Vol 34 (suppl_1) ◽  
Author(s):  
Patricia Christian ◽  
Mostafa Zamani ◽  
Wei Qui ◽  
Rianna Zhang ◽  
Khosrow Adeli
Keyword(s):  
Cell Line ◽  
Hepg2 Cells ◽  
Ex Vivo ◽  
Hepatoma Cell ◽  
Hepatoma Cell Line ◽  
Human Hepatoma ◽  
Human Hepatoma Cell ◽  
Human Hepatoma Cell Line ◽  
Vldl Assembly

Introduction: As apolipoprotein B (apoB) is translated and translocated into the ER, lipids from cytoplasmic lipid droplets (LDs) are added to promote folding and to initiate very-low-density-lipoprotein (VLDL) assembly. However, without sufficient lipid availability, apoB is misfolded and subject to proteasomal degradation. Evidence now shows that apoB can also be degraded through autophagy under certain conditions, and that LDs are also subject to autophagic degradation, a process referred to as lipophagy. We postulate that apoB autophagy and LD lipophagy integrate to regulate hepatic lipid export and VLDL production. Methods/Results: Studies were conducted in vitro using the human hepatoma cell line, HepG2 and ex vivo using primary Syrian Golden hamster hepatocytes. Cells were fat loaded with/without 0.4 mM OA for 4 hours and simultaneously treated with an autophagy inhibitor 3-methyadenine (3-MA; 100uM) or an autophagy inducer, Torin 1 (250nM). HepG2 cells were transfected with 10 nM of atg12 siRNA, an essential autophagy related gene, for a total of 72 hours. In freshly isolated primary hamster hepatocytes, inhibition of autophagosome formation, through treatment with 3-MA, significantly increased cellular levels of newly synthesized apoB, without a significant increase in apoB secreted into the media. Interestingly, treating these cells with Torin 1 to promote autophagy also significantly increased apoB recovery. However, modulation of autophagy activity also affected the average number of LDs per cell, indicating that lipophagy activity had also been modified, potentially affecting VLDL formation. Conversely, while inhibition and induction of autophagy in HepG2 cells, a human hepatoma cell line, reduced and increased apoB co-localization with autophagosomes respectively, siRNA knockdown of atg12 as well as 3-MA treatment decreased apoB recovery. However, this did not appear to be due to reduction in LD breakdown through autophagy. The data obtained with primary hamster hepatocytes suggest that autophagy may play a dual role in VLDL assembly in vivo by regulating both degradation of apoB and lipidation of VLDL particles through mobilization of lipid from LDs. Defects in these pathways can induce hepatic LD accumulation and steatosis.

Bis(hydroxyphenyl)methane—bisphenol F—metabolism by the HepG2 human hepatoma cell line and cryopreserved human hepatocytes

2011 ◽  
Vol 34 (4) ◽  
pp. 445-453 ◽  
Author(s):  
Coralie Dumont ◽  
Elisabeth Perdu ◽  
Georges de Sousa ◽  
Laurent Debrauwer ◽  
Roger Rahmani ◽  
...  
Keyword(s):  
Cell Line ◽  
Hepatoma Cell ◽  
Human Hepatocytes ◽  
Hepatoma Cell Line ◽  
Human Hepatoma ◽  
Human Hepatoma Cell ◽  
Human Hepatoma Cell Line ◽  
Bisphenol F
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