Inhibition of microsomal triglyceride transfer protein expression and atherogenic risk factor apolipoprotein B100 secretion by tanshinone IIA in HepG2 cells

2008 ◽  
Vol 22 (12) ◽  
pp. 1640-1645 ◽  
Author(s):  
Yun-Jeong Kang ◽  
Un-Ho Jin ◽  
Hyen-Wook Chang ◽  
Jong-Keun Son ◽  
Seung Ho Lee ◽  
...  
Keyword(s):  
Risk Factor ◽  
Protein Expression ◽  
Hepg2 Cells ◽  
Microsomal Triglyceride Transfer Protein ◽  
Tanshinone Iia ◽  
Transfer Protein ◽  
Apolipoprotein B100

scholarly journals β-Apo-10′-carotenoids Modulate Placental Microsomal Triglyceride Transfer Protein Expression and Function to Optimize Transport of Intact β-Carotene to the Embryo

2016 ◽  
Vol 291 (35) ◽  
pp. 18525-18535 ◽  
Author(s):  
Brianna K. Costabile ◽  
Youn-Kyung Kim ◽  
Jahangir Iqbal ◽  
Michael V. Zuccaro ◽  
Lesley Wassef ◽  
...  
Keyword(s):  
Protein Expression ◽  
Microsomal Triglyceride Transfer Protein ◽  
Transfer Protein ◽  
And Function ◽  
Β Carotene

Design of a Targeted Peptide Nucleic Acid Prodrug To Inhibit Hepatic Human Microsomal Triglyceride Transfer Protein Expression in Hepatocytes†

2002 ◽  
Vol 13 (2) ◽  
pp. 295-302 ◽  
Author(s):  
Erik A. L. Biessen ◽  
Karen Sliedregt-Bol ◽  
Peter A. Chr. 'T Hoen ◽  
Perry Prince ◽  
Erica Van der Bilt ◽  
...  
Keyword(s):  
Nucleic Acid ◽  
Protein Expression ◽  
Peptide Nucleic Acid ◽  
Microsomal Triglyceride Transfer Protein ◽  
Transfer Protein

Microsomal triglyceride transfer protein expression in mouse intestine

2005 ◽  
Vol 123 (4-5) ◽  
pp. 475-482 ◽  
Author(s):  
Larry L. Swift ◽  
Aneta Jovanovska ◽  
Bharati Kakkad ◽  
David E. Ong
Keyword(s):  
Protein Expression ◽  
Microsomal Triglyceride Transfer Protein ◽  
Transfer Protein ◽  
Mouse Intestine

scholarly journals miR-130b is a potent stimulator of hepatic very-low-density lipoprotein assembly and secretion via marked induction of microsomal triglyceride transfer protein

2020 ◽  
Vol 318 (2) ◽  
pp. E262-E275 ◽  
Author(s):  
Jing Zhang ◽  
Ferdous Rastgar Jazii ◽  
Mahdi Montazer Haghighi ◽  
Danielle Alvares ◽  
Lipei Liu ◽  
...  
Keyword(s):  
Lipid Metabolism ◽  
Hepg2 Cells ◽  
Low Density Lipoprotein ◽  
Density Lipoprotein ◽  
Microsomal Triglyceride Transfer Protein ◽  
Luciferase Reporter ◽  
Very Low Density Lipoprotein ◽  
Low Density ◽  
Transfer Protein ◽  
Stimulation Of

miR-130b is a microRNA whose expression is particularly elevated within adipose tissue and in the circulation in diabetic states. Hepatic miR-130b expression has been linked to hepatocellular carcinoma and changes in lipid metabolism. Here, we investigated the role of miR-130b in hepatic lipid homeostasis and lipoprotein export. We observed that overexpression of miR-130b-3p or -5p in HepG2 cells markedly enhanced the secretion of very-low-density lipoprotein (VLDL) particles, enhanced the secretion of [3H]glycerol metabolically labeled triglyceride (TG), and significantly increased the number or the average size of lipid droplets (LDs), respectively. Overexpression of miR-130b also altered the expression of key genes involved in lipid metabolism and in particular markedly increased both mRNA and protein expression levels of microsomal triglyceride transfer protein (MTP). Conversely, the miR-130b inhibitor decreased mRNA levels of MTP and fatty acid synthase ( FAS) in HepG2 cells. However, dual-luciferase reporter assays indicated that MTP is not a direct target of miR-130b-3p. miR-130b overexpression did not alter de novo synthesized TG or the stability and secretion of apolipoprotein B 100. Interestingly, knockdown of phosphatase and tensin homolog ( PTEN) blocked the upregulation of MTP mRNA induced by miR-130b. Finally, miR-130b-induced stimulation of VLDL secretion was also observed in a second hepatocyte cell culture model, immortalized human hepatocytes, confirming the effects observed in HepG2 cells. Overall, these data suggest a potential role for miR-130b in promoting hepatic VLDL assembly and secretion mediated by marked stimulation of MTP expression and TG mobilization. Thus miR-130b overexpression corrects the defect in VLDL production in HepG2 cells.

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